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Conserved domains on  [gi|489309308|ref|WP_003216734|]
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MULTISPECIES: ABC transporter ATP-binding protein [Pseudomonas]

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

CATH:  3.40.50.300
EC:  7.-.-.-
Gene Ontology:  GO:0055052|GO:0140359|GO:0042626|GO:0005524|GO:0016887
PubMed:  19234479|26517916|10529352|24638992|25750732
SCOP:  4003976
TCDB:  3.A.1

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];
101-604 1.10e-169

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


:

Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 495.07  E-value: 1.10e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 101 GALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGT 180
Cdd:COG1132   73 LRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGA 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 181 SGILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQE 260
Cdd:COG1132  153 LVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEE 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 261 VRDFAVNSQWKSDASSRASGLLFQFGIDIFRAAAMLTVLFSDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAAGGALT 340
Cdd:COG1132  233 LRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAE 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 341 RINELLARADEPQYAGGADPFTgRETVGIEVRGLNFGY-GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYT 419
Cdd:COG1132  313 RIFELLDEPPEIPDPPGAVPLP-PVRGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 420 PQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGR-ERSDQACWQALEIAQLDATVKALPLGLDSVVG 498
Cdd:COG1132  392 PTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVG 471

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 499 RSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGH 578
Cdd:COG1132  472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGR 551

                        490       500
                 ....*....|....*....|....*.
gi 489309308 579 IAEDGDHQQLIADGGLYAKLYgHLQQ 604
Cdd:COG1132  552 IVEQGTHEELLARGGLYARLY-RLQF 576
 
Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
101-604 1.10e-169

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 495.07  E-value: 1.10e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 101 GALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGT 180
Cdd:COG1132   73 LRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGA 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 181 SGILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQE 260
Cdd:COG1132  153 LVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEE 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 261 VRDFAVNSQWKSDASSRASGLLFQFGIDIFRAAAMLTVLFSDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAAGGALT 340
Cdd:COG1132  233 LRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAE 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 341 RINELLARADEPQYAGGADPFTgRETVGIEVRGLNFGY-GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYT 419
Cdd:COG1132  313 RIFELLDEPPEIPDPPGAVPLP-PVRGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 420 PQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGR-ERSDQACWQALEIAQLDATVKALPLGLDSVVG 498
Cdd:COG1132  392 PTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVG 471

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 499 RSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGH 578
Cdd:COG1132  472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGR 551

                        490       500
                 ....*....|....*....|....*.
gi 489309308 579 IAEDGDHQQLIADGGLYAKLYgHLQQ 604
Cdd:COG1132  552 IVEQGTHEELLARGGLYARLY-RLQF 576
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 112-599 8.60e-98

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: 309.72  E-value: 8.60e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  112 LFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGILMWMHWKL 191
Cdd:TIGR02203  77 LLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQL 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  192 ALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVRDFAVNSQWK 271
Cdd:TIGR02203 157 TLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSA 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  272 SDASSRASGLLFQFGIDIFRAAAMLTVLFSDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAAGGALTRINELLARADE 351
Cdd:TIGR02203 237 GSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  352 PQyAGGADPftGRETVGIEVRGLNFGYG--EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG 429
Cdd:TIGR02203 317 KD-TGTRAI--ERARGDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG 393

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  430 STQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRER--SDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGG 507
Cdd:TIGR02203 394 HDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqaDRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGG 473

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  508 QRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQ 587
Cdd:TIGR02203 474 QRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNE 553

                         490
                  ....*....|..
gi 489309308  588 LIADGGLYAKLY 599
Cdd:TIGR02203 554 LLARNGLYAQLH 565
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 369-599 8.89e-81

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: 254.08  E-value: 8.89e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYG-EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVV 447
Cdd:cd03253    1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALFNDTVRANLTMGRER-SDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVI 526
Cdd:cd03253   81 PQDTVLFNDTIGYNIRYGRPDaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308 527 LDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGGLYAKLY 599
Cdd:cd03253  161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMW 233
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
72-605 1.73e-68

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 233.07  E-value: 1.73e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  72 VMNHALPLGWQK--AAGYIGLMLLvtlllrcgALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVT 149
Cdd:PRK10790  54 VAKGNLPLGLVAglAAAYVGLQLL--------AAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLI 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 150 THLVTDLDTV-DKFVGETLSRFLVAmlTLVGTSGILMWM-HWKLALLILLFNPLVI--------YATvQLGKRVKHLKKL 219
Cdd:PRK10790 126 SRVTNDTEVIrDLYVTVVATVLRSA--ALIGAMLVAMFSlDWRMALVAIMIFPAVLvvmviyqrYST-PIVRRVRAYLAD 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 220 ENDStsrFTQALTeTLDAIQEVRagnRQGfflgRLGQRAQEvrdfAVNSQWKSDASS-RASGLLFQFGIDIFRAAAM--L 296
Cdd:PRK10790 203 INDG---FNEVIN-GMSVIQQFR---QQA----RFGERMGE----ASRSHYMARMQTlRLDGFLLRPLLSLFSALILcgL 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 297 TVLFS-----DLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAAGGALTRINELLaraDEPQYAGGAD--PFT-GRetvg 368
Cdd:PRK10790 268 LMLFGfsasgTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELM---DGPRQQYGNDdrPLQsGR---- 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEE-LVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVV 447
Cdd:PRK10790 341 IDIDNVSFAYRDDnLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALFNDTVRANLTMGRERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVIL 527
Cdd:PRK10790 421 QQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILIL 500

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 528 DEATSALDAATEYNLHQALaRFLSGRTTLI-IAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGGLYAKLYgHLQQV 605
Cdd:PRK10790 501 DEATANIDSGTEQAIQQAL-AAVREHTTLVvIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMY-QLQLA 577
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 384-532 3.61e-36

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 132.39  E-value: 3.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFND-TVRANL 462
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308  463 TMGR---ERSDQACWQalEIAQLDATVKaLPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATS 532
Cdd:pfam00005  81 RLGLllkGLSKREKDA--RAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
377-574 1.57e-26

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 106.93  E-value: 1.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 377 GYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQqeigletirenVSVVLQH---PAL 453
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGAR-----------VAYVPQRsevPDS 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 454 FNDTVRANLTMGRERsDQACWQALEIAQLDATVKALP-LGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATS 532
Cdd:NF040873  70 LPLTVRDLVAMGRWA-RRGLWRRLTRDDRAAVDDALErVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489309308 533 ALDAATEYNLHQALARFLS-GRTTLIIAHRLSAVKQADRVLVF 574
Cdd:NF040873 149 GLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
GguA NF040905
sugar ABC transporter ATP-binding protein;
384-579 1.40e-11

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 67.12  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYtPQA---GSIRFGGSTQQeigLETIR--ENVSVVLQH------PA 452
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVCR---FKDIRdsEALGIVIIHqelaliPY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 453 LfndTVRANLTMGRERSDQAC--WQA--LEIAQLDATVkalplGL----DSVVGRSGVrfsgGQRQRLAIARMVLAEPKV 524
Cdd:NF040905  93 L---SIAENIFLGNERAKRGVidWNEtnRRARELLAKV-----GLdespDTLVTDIGV----GKQQLVEIAKALSKDVKL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 525 VILDEATSALDAATEYNLHQALARFLS-GRTTLIIAHRLSAVKQ-ADRVLVF-DGGHI 579
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAqGITSIIISHKLNEIRRvADSITVLrDGRTI 218
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
368-606 2.04e-10

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 62.83  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 368 GIEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGG--KSTLVQLLLGlytPQAGS--IRFGGSTQQEIGLE-TIRE 442
Cdd:NF000106  13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRrpWRF*TWCANRRALRrTIG* 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 443 NVSVVLQHPALFNDtvRANLTM-GRErsdqacwqaLEIAQLDATVKALPL----GLDSVVGRSGVRFSGGQRQRLAIARM 517
Cdd:NF000106  90 HRPVR*GRRESFSG--RENLYMiGR*---------LDLSRKDARARADELlerfSLTEAAGRAAAKYSGGMRRRLDLAAS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 518 VLAEPKVVILDEATSALDAATEYNLHQALARFL-SGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQliadggLY 595
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDE------LK 232

                        250
                 ....*....|.
gi 489309308 596 AKLYGHLQQVR 606
Cdd:NF000106 233 TKVGGRTLQIR 243
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
360-535 2.73e-09

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 60.14  E-value: 2.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 360 PFTGRETVGIEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIR-FGgstqQEI--- 435
Cdd:NF033858 258 PADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlFG----QPVdag 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 436 GLETiRENVSVVLQHPALFND-TVRANLT-------MGRERSDQACWQALE----IAQLDATVKALPLGLdsvvgrsgvr 503
Cdd:NF033858 334 DIAT-RRRVGYMSQAFSLYGElTVRQNLElharlfhLPAAEIAARVAEMLErfdlADVADALPDSLPLGI---------- 402

                        170       180       190
                 ....*....|....*....|....*....|..
gi 489309308 504 fsggqRQRLAIARMVLAEPKVVILDEATSALD 535
Cdd:NF033858 403 -----RQRLSLAVAVIHKPELLILDEPTSGVD 429
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 393-575 5.12e-08

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: 52.38  E-value: 5.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   393 PGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFggstqqeIGLETIRENVSVVLQHPalfndtvranltmgrersdqa 472
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLDQLLLI--------------------- 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   473 cwqaleiaqldatvkalplgldsVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFL-- 550
Cdd:smart00382  53 -----------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109

                          170       180       190
                   ....*....|....*....|....*....|
gi 489309308   551 -----SGRTTLIIAHRLSAVKQADRVLVFD 575
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPALLRRRFD 139
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
369-535 1.50e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 44.73  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIR-FGGSTQQEIGLETIRENVSVV 447
Cdd:NF033858   2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGDMADARHRRAVCPRIAYM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQ------HPALfndTVRANLT-MGR-------ERsdqacwqALEIAQL-DATvkalplGLDSVVGRSGVRFSGGQRQRL 512
Cdd:NF033858  82 PQglgknlYPTL---SVFENLDfFGRlfgqdaaER-------RRRIDELlRAT------GLAPFADRPAGKLSGGMKQKL 145

                        170       180
                 ....*....|....*....|...
gi 489309308 513 AIARMVLAEPKVVILDEATSALD 535
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVD 168
 
Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
101-604 1.10e-169

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 495.07  E-value: 1.10e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 101 GALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGT 180
Cdd:COG1132   73 LRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGA 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 181 SGILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQE 260
Cdd:COG1132  153 LVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEE 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 261 VRDFAVNSQWKSDASSRASGLLFQFGIDIFRAAAMLTVLFSDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAAGGALT 340
Cdd:COG1132  233 LRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAE 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 341 RINELLARADEPQYAGGADPFTgRETVGIEVRGLNFGY-GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYT 419
Cdd:COG1132  313 RIFELLDEPPEIPDPPGAVPLP-PVRGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 420 PQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGR-ERSDQACWQALEIAQLDATVKALPLGLDSVVG 498
Cdd:COG1132  392 PTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVG 471

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 499 RSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGH 578
Cdd:COG1132  472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGR 551

                        490       500
                 ....*....|....*....|....*.
gi 489309308 579 IAEDGDHQQLIADGGLYAKLYgHLQQ 604
Cdd:COG1132  552 IVEQGTHEELLARGGLYARLY-RLQF 576
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 103-599 2.91e-136

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: 413.85  E-value: 2.91e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 103 LVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHlVTDLDTVDKFVGETLSRFLVAMLTLVGTSG 182
Cdd:COG2274  210 GLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASR-FRDVESIREFLTGSLLTALLDLLFVLIFLI 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 183 ILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVR 262
Cdd:COG2274  289 VLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYL 368

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 263 DFAVNSQWKSDASSRASGLLFQFG-IDIFRAAAMLtVLFSDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAAGGALTR 341
Cdd:COG2274  369 NARFKLRRLSNLLSTLSGLLQQLAtVALLWLGAYL-VIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALER 447

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 342 INELLARADEPQyAGGADPFTGRETVGIEVRGLNFGYG--EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYT 419
Cdd:COG2274  448 LDDILDLPPERE-EGRSKLSLPRLKGDIELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE 526

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 420 PQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRER-SDQACWQALEIAQLDATVKALPLGLDSVVG 498
Cdd:COG2274  527 PTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGYDTVVG 606

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 499 RSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGH 578
Cdd:COG2274  607 EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGR 686

                        490       500
                 ....*....|....*....|.
gi 489309308 579 IAEDGDHQQLIADGGLYAKLY 599
Cdd:COG2274  687 IVEDGTHEELLARKGLYAELV 707
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 123-599 7.80e-101

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: 317.48  E-value: 7.80e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 123 RIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGILMWMHWKLALLILLF---- 198
Cdd:COG4987   89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGllla 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 199 ----NPLVIYATVQLGKRVKHLKklendstSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVRDfavnSQWKSDA 274
Cdd:COG4987  169 glllPLLAARLGRRAGRRLAAAR-------AALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAA----AQRRLAR 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 275 SSRASGLLFQFGIDIFrAAAMLTVLFSDLSIGQ----MLAVFSylwFMISPV-EQLLNLQYAYYAAGG---ALTRINELL 346
Cdd:COG4987  238 LSALAQALLQLAAGLA-VVAVLWLAAPLVAAGAlsgpLLALLV---LAALALfEALAPLPAAAQHLGRvraAARRLNELL 313

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 347 ARADEPQYAGGADPFTGRetVGIEVRGLNFGY--GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGS 424
Cdd:COG4987  314 DAPPAVTEPAEPAPAPGG--PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS 391

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 425 IRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRER-SDQACWQALEIAQLDATVKALPLGLDSVVGRSGVR 503
Cdd:COG4987  392 ITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDaTDEELWAALERVGLGDWLAALPDGLDTWLGEGGRR 471

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 504 FSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDG 583
Cdd:COG4987  472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQG 551

                        490
                 ....*....|....*.
gi 489309308 584 DHQQLIADGGLYAKLY 599
Cdd:COG4987  552 THEELLAQNGRYRQLY 567
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 112-599 8.60e-98

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: 309.72  E-value: 8.60e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  112 LFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGILMWMHWKL 191
Cdd:TIGR02203  77 LLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQL 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  192 ALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVRDFAVNSQWK 271
Cdd:TIGR02203 157 TLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSA 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  272 SDASSRASGLLFQFGIDIFRAAAMLTVLFSDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAAGGALTRINELLARADE 351
Cdd:TIGR02203 237 GSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  352 PQyAGGADPftGRETVGIEVRGLNFGYG--EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG 429
Cdd:TIGR02203 317 KD-TGTRAI--ERARGDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG 393

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  430 STQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRER--SDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGG 507
Cdd:TIGR02203 394 HDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqaDRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGG 473

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  508 QRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQ 587
Cdd:TIGR02203 474 QRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNE 553

                         490
                  ....*....|..
gi 489309308  588 LIADGGLYAKLY 599
Cdd:TIGR02203 554 LLARNGLYAQLH 565
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 104-593 1.04e-97

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: 309.38  E-value: 1.04e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGI 183
Cdd:COG4988   73 LLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVA 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 184 LMWMHWKLALLILLFNPLVIYATVQLGKRVKhlKKLEN--DSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEV 261
Cdd:COG4988  153 VFPLDWLSGLILLVTAPLIPLFMILVGKGAA--KASRRqwRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDF 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 262 RD-------FAVNSqwksdasSRASGLLFQFGIdifrAAAMLTVLFSdLSIGQMlAVFSYLWF-MISPV--EQLLNLQYA 331
Cdd:COG4988  231 RKrtmkvlrVAFLS-------SAVLEFFASLSI----ALVAVYIGFR-LLGGSL-TLFAALFVlLLAPEffLPLRDLGSF 297

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 332 YYA---AGGALTRINELLArADEPQYAGGADPFTGRETVGIEVRGLNFGYGEE-LVLDQLNLNIAPGEKVAIVGASGGGK 407
Cdd:COG4988  298 YHAranGIAAAEKIFALLD-APEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGrPALDGLSLTIPPGERVALVGPSGAGK 376

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 408 STLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGR-ERSDQACWQALEIAQLDATV 486
Cdd:COG4988  377 STLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFV 456

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 487 KALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVK 566
Cdd:COG4988  457 AALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA 536

                        490       500
                 ....*....|....*....|....*..
gi 489309308 567 QADRVLVFDGGHIAEDGDHQQLIADGG 593
Cdd:COG4988  537 QADRILVLDDGRIVEQGTHEELLAKNG 563
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 369-599 8.89e-81

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: 254.08  E-value: 8.89e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYG-EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVV 447
Cdd:cd03253    1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALFNDTVRANLTMGRER-SDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVI 526
Cdd:cd03253   81 PQDTVLFNDTIGYNIRYGRPDaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308 527 LDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGGLYAKLY 599
Cdd:cd03253  161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMW 233
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 369-599 2.55e-80

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: 252.92  E-value: 2.55e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYG--EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSV 446
Cdd:cd03251    1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPALFNDTVRANLTMGRERSDQA-CWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVV 525
Cdd:cd03251   81 VSQDVFLFNDTVAENIAYGRPGATREeVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308 526 ILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGGLYAKLY 599
Cdd:cd03251  161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 369-593 7.98e-79

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: 248.68  E-value: 7.98e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGE-ELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVV 447
Cdd:cd03254    3 IEFENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALFNDTVRANLTMGRERSDQACWQ-ALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVI 526
Cdd:cd03254   83 LQDTFLFSGTIMENIRLGRPNATDEEVIeAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 527 LDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGG 593
Cdd:cd03254  163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 369-599 2.12e-78

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: 247.84  E-value: 2.12e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGY---GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVS 445
Cdd:cd03249    1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 446 VVLQHPALFNDTVRANLTMGR-ERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKV 524
Cdd:cd03249   81 LVSQEPVLFDGTIAENIRYGKpDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 525 VILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGGLYAKLY 599
Cdd:cd03249  161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 1-604 6.01e-78

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: 258.60  E-value: 6.01e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   1 MHDQPDPVEQPKRVDRLTWAEVRRLALHHKKSLWIANGVAVLATLCSVPIPLLLPLLVDEVLLGHGDAALKVMnhALPLG 80
Cdd:COG5265    2 PSARAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALL--VVPVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  81 WqkAAGYIGLmllvtlllRCGALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTThlvtDLDTVD 160
Cdd:COG5265   80 L--LLAYGLL--------RLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSR----DIERGT 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 161 KFVgETLSRFLV-----AMLTLVGTSGILMWM-HWKLALLILLfnPLVIYATVQLG---KRVKHLKK---LENDSTSRFT 228
Cdd:COG5265  146 KGI-EFLLRFLLfnilpTLLEIALVAGILLVKyDWWFALITLV--TVVLYIAFTVVvteWRTKFRREmneADSEANTRAV 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 229 QAL--TETldaiqeVRAGNRQGFFLGRLGQRAQEVRDFAVNSQwKSDAssrasglLFQFGIDIFRAAAMLTVLF------ 300
Cdd:COG5265  223 DSLlnYET------VKYFGNEAREARRYDEALARYERAAVKSQ-TSLA-------LLNFGQALIIALGLTAMMLmaaqgv 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 301 --SDLSIGQMLAVFSYlwfMIspveQL---LN-LQYAYYAAGGALTRIN---ELLARADEPQYAGGADPFTGREtVGIEV 371
Cdd:COG5265  289 vaGTMTVGDFVLVNAY---LI----QLyipLNfLGFVYREIRQALADMErmfDLLDQPPEVADAPDAPPLVVGG-GEVRF 360

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 372 RGLNFGYGEE-LVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQH 450
Cdd:COG5265  361 ENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD 440

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 451 PALFNDTVRANLTMGR-ERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDE 529
Cdd:COG5265  441 TVLFNDTIAYNIAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDE 520

                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 530 ATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGGLYAKLYgHLQQ 604
Cdd:COG5265  521 ATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMW-ARQQ 594
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 369-578 2.55e-72

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: 229.58  E-value: 2.55e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEEL--VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSV 446
Cdd:cd03228    1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPALFNDTVRANLtmgrersdqacwqaleiaqldatvkalplgldsvvgrsgvrFSGGQRQRLAIARMVLAEPKVVI 526
Cdd:cd03228   81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489309308 527 LDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGH 578
Cdd:cd03228  120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 120-598 7.43e-71

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 241.94  E-value: 7.43e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  120 IVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGILMWMHWKLALLILLFN 199
Cdd:TIGR00958 232 INLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINL 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  200 PLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVRDFAvnsqWKSD------ 273
Cdd:TIGR00958 312 PLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLN----KRKAlayagy 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  274 -ASSRASGLLFQFGIDIFRAAAMLTvlfSDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAAGGALTRINELLARADEP 352
Cdd:TIGR00958 388 lWTTSVLGMLIQVLVLYYGGQLVLT---GKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNI 464

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  353 QYAGG--ADPFTGRetvgIEVRGLNFGY---GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRF 427
Cdd:TIGR00958 465 PLTGTlaPLNLEGL----IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL 540

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  428 GGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRERSDQACWQAL-EIAQLDATVKALPLGLDSVVGRSGVRFSG 506
Cdd:TIGR00958 541 DGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAaKAANAHDFIMEFPNGYDTEVGEKGSQLSG 620

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  507 GQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQalARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQ 586
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698

                         490
                  ....*....|..
gi 489309308  587 QLIADGGLYAKL 598
Cdd:TIGR00958 699 QLMEDQGCYKHL 710
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 108-598 5.67e-70

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: 239.85  E-value: 5.67e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  108 LQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHlVTDLDTVDKFVGETLSRFLVAMLTLVGTSGILMWM 187
Cdd:TIGR03796 213 LQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASR-VQLNDQVAEFLSGQLATTALDAVMLVFYALLMLLY 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  188 HWKLALLILLFNPLVIYATVQLGKRVKhlkklenDSTSRFTQ-------------ALTETLDAiqevrAGNRQGFFLGRL 254
Cdd:TIGR03796 292 DPVLTLIGIAFAAINVLALQLVSRRRV-------DANRRLQQdagkltgvaisglQSIETLKA-----SGLESDFFSRWA 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  255 GQRAQevrdfAVNSQWKSDASSRASGLLFQFgIDIFRAAAMLT-----VLFSDLSIGQMLAVFSYLWFMISPVEQLLNLQ 329
Cdd:TIGR03796 360 GYQAK-----LLNAQQELGVLTQILGVLPTL-LTSLNSALILVvgglrVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFG 433

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  330 YAYYAAGGALTRINELL-----ARADEPQYAGGADPFTGRETVGIEVRGLNFGYG--EELVLDQLNLNIAPGEKVAIVGA 402
Cdd:TIGR03796 434 GTLQELEGDLNRLDDVLrnpvdPLLEEPEGSAATSEPPRRLSGYVELRNITFGYSplEPPLIENFSLTLQPGQRVALVGG 513

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  403 SGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTM-GRERSDQACWQALEIAQ 481
Cdd:TIGR03796 514 SGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLwDPTIPDADLVRACKDAA 593

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  482 LDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARflSGRTTLIIAHR 561
Cdd:TIGR03796 594 IHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHR 671

                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 489309308  562 LSAVKQADRVLVFDGGHIAEDGDHQQLIADGGLYAKL 598
Cdd:TIGR03796 672 LSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 369-583 1.51e-68

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: 221.60  E-value: 1.51e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEEL--VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSV 446
Cdd:cd03244    3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPALFNDTVRANLTMGRERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVI 526
Cdd:cd03244   83 IPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 527 LDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDG 583
Cdd:cd03244  163 LDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
72-605 1.73e-68

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 233.07  E-value: 1.73e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  72 VMNHALPLGWQK--AAGYIGLMLLvtlllrcgALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVT 149
Cdd:PRK10790  54 VAKGNLPLGLVAglAAAYVGLQLL--------AAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLI 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 150 THLVTDLDTV-DKFVGETLSRFLVAmlTLVGTSGILMWM-HWKLALLILLFNPLVI--------YATvQLGKRVKHLKKL 219
Cdd:PRK10790 126 SRVTNDTEVIrDLYVTVVATVLRSA--ALIGAMLVAMFSlDWRMALVAIMIFPAVLvvmviyqrYST-PIVRRVRAYLAD 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 220 ENDStsrFTQALTeTLDAIQEVRagnRQGfflgRLGQRAQEvrdfAVNSQWKSDASS-RASGLLFQFGIDIFRAAAM--L 296
Cdd:PRK10790 203 INDG---FNEVIN-GMSVIQQFR---QQA----RFGERMGE----ASRSHYMARMQTlRLDGFLLRPLLSLFSALILcgL 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 297 TVLFS-----DLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAAGGALTRINELLaraDEPQYAGGAD--PFT-GRetvg 368
Cdd:PRK10790 268 LMLFGfsasgTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELM---DGPRQQYGNDdrPLQsGR---- 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEE-LVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVV 447
Cdd:PRK10790 341 IDIDNVSFAYRDDnLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALFNDTVRANLTMGRERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVIL 527
Cdd:PRK10790 421 QQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILIL 500

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 528 DEATSALDAATEYNLHQALaRFLSGRTTLI-IAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGGLYAKLYgHLQQV 605
Cdd:PRK10790 501 DEATANIDSGTEQAIQQAL-AAVREHTTLVvIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMY-QLQLA 577
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
104-598 2.97e-68

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 232.16  E-value: 2.97e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLI----ERLKRISLSEYESLGSGTVtthLVTDLDTVDKFVGETLSRF------LVA 173
Cdd:PRK13657  67 LFNIIAGVLVARHADRLAHRRRLAVLteyfERIIQLPLAWHSQRGSGRA---LHTLLRGTDALFGLWLEFMrehlatLVA 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 174 MLTLVGTSgilMWMHWKLAllILLFNPLVIYatVQLGKRVKHLKKLENDSTSRFTQALTE-TLDAIQEVRAgnRQGFflG 252
Cdd:PRK13657 144 LVVLLPLA---LFMNWRLS--LVLVVLGIVY--TLITTLVMRKTKDGQAAVEEHYHDLFAhVSDAIGNVSV--VQSY--N 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 253 RLGQRAQEVRDFA---------VNSQWK-SDASSRASGLLFQFGidIFRAAAMLtVLFSDLSIGQMLAVFSYLWFMISPV 322
Cdd:PRK13657 213 RIEAETQALRDIAdnllaaqmpVLSWWAlASVLNRAASTITMLA--ILVLGAAL-VQKGQLRVGEVVAFVGFATLLIGRL 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 323 EQLLNLQYAYYAAGGALTRINELL---ARADEPQYAGGADPFTGRetvgIEVRGLNFGY-GEELVLDQLNLNIAPGEKVA 398
Cdd:PRK13657 290 DQVVAFINQVFMAAPKLEEFFEVEdavPDVRDPPGAIDLGRVKGA----VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVA 365

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 399 IVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRE-RSDQACWQAL 477
Cdd:PRK13657 366 IVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPdATDEEMRAAA 445

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 478 EIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLI 557
Cdd:PRK13657 446 ERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI 525

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 489309308 558 IAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGGLYAKL 598
Cdd:PRK13657 526 IAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 369-599 2.03e-67

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: 219.28  E-value: 2.03e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYG--EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSV 446
Cdd:cd03252    1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPALFNDTVRANLTMGRERSD-QACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVV 525
Cdd:cd03252   81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308 526 ILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGGLYAKLY 599
Cdd:cd03252  161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 104-601 5.12e-66

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: 228.86  E-value: 5.12e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFL-VAMLTLVGTsg 182
Cdd:TIGR01193 211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLdMWILVIVGL-- 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  183 ILMWMHWKLALLILLFNPL---VIYATVQLGKRVKHlKKLENDSTsrFTQALTETLDAIQEVRAGNRQGFflgRLGQRAQ 259
Cdd:TIGR01193 289 FLVRQNMLLFLLSLLSIPVyavIIILFKRTFNKLNH-DAMQANAV--LNSSIIEDLNGIETIKSLTSEAE---RYSKIDS 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  260 EVRDFaVNSQW---KSDASSRA--SGLLFQFGIDIFRAAAMLtVLFSDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYA 334
Cdd:TIGR01193 363 EFGDY-LNKSFkyqKADQGQQAikAVTKLILNVVILWTGAYL-VMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQA 440

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  335 AGGALTRINELLARADEPQYAGGADpFTGRETVGIEVRGL--NFGYGEElVLDQLNLNIAPGEKVAIVGASGGGKSTLVQ 412
Cdd:TIGR01193 441 ARVANNRLNEVYLVDSEFINKKKRT-ELNNLNGDIVINDVsySYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAK 518

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  413 LLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRER--SDQACWQALEIAQLDATVKALP 490
Cdd:TIGR01193 519 LLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKEnvSQDEIWAACEIAEIKDDIENMP 598

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  491 LGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALArFLSGRTTLIIAHRLSAVKQADR 570
Cdd:TIGR01193 599 LGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLL-NLQDKTIIFVAHRLSVAKQSDK 677

                         490       500       510
                  ....*....|....*....|....*....|.
gi 489309308  571 VLVFDGGHIAEDGDHQQLIADGGLYAKLYGH 601
Cdd:TIGR01193 678 IIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 108-601 6.33e-66

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: 228.47  E-value: 6.33e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  108 LQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHlVTDLDTVDKFV-GETLSRFLVAMLTLVGTsGILMW 186
Cdd:TIGR01846 198 LRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVAR-VRELEQIRNFLtGSALTVVLDLLFVVVFL-AVMFF 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  187 MHWKLALLILLfnPLVIYATVQLG------KRVKhlKKLENDSTSrfTQALTETLDAIQEVRAGNRQGfflgRLGQRAQE 260
Cdd:TIGR01846 276 YSPTLTGVVIG--SLVCYALLSVFvgpilrKRVE--DKFERSAAA--TSFLVESVTGIETIKATATEP----QFQNRWDR 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  261 VRDFAVNSQWKSdassRASGLLFQFGIDIFRAAAMLTVLF--------SDLSIGQMLAVFSYLWFMISPVEQLLNLQYAY 332
Cdd:TIGR01846 346 QLAAYVAASFRV----TNLGNIAGQAIELIQKLTFAILLWfgahlvigGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDF 421

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  333 YAAGGALTRINELLARADEPQYAGGAdpfTGRETVG-IEVRGLNFGYGEE--LVLDQLNLNIAPGEKVAIVGASGGGKST 409
Cdd:TIGR01846 422 QQTGIALERLGDILNSPTEPRSAGLA---ALPELRGaITFENIRFRYAPDspEVLSNLNLDIKPGEFIGIVGPSGSGKST 498

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  410 LVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRER-SDQACWQALEIAQLDATVKA 488
Cdd:TIGR01846 499 LTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGaPFEHVIHAAKLAGAHDFISE 578

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  489 LPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQA 568
Cdd:TIGR01846 579 LPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRAC 658

                         490       500       510
                  ....*....|....*....|....*....|...
gi 489309308  569 DRVLVFDGGHIAEDGDHQQLIADGGLYAKLYGH 601
Cdd:TIGR01846 659 DRIIVLEKGQIAESGRHEELLALQGLYARLWQQ 691
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
120-599 3.59e-65

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 223.74  E-value: 3.59e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 120 IVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVdkfvGETLSRFLVAML----TLVGTSGILMWMHWKLALLI 195
Cdd:PRK11176  96 VVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQV----ASSSSGALITVVregaSIIGLFIMMFYYSWQLSLIL 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 196 LLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNrqgfflgrlGQRAQEVRDFAVNSQWKSD-- 273
Cdd:PRK11176 172 IVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFG---------GQEVETKRFDKVSNRMRQQgm 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 274 ----ASSRASGLlfqfgIDIFRAAAMLTVLF--------SDLSIGQMLAVFSYLWFMISPVEQLLNLQYAY---YAAGGA 338
Cdd:PRK11176 243 kmvsASSISDPI-----IQLIASLALAFVLYaasfpsvmDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFqrgMAACQT 317

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 339 LTRINELLARADEPQYAggADPFTGRetvgIEVRGLNFGY--GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLG 416
Cdd:PRK11176 318 LFAILDLEQEKDEGKRV--IERAKGD----IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTR 391

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 417 LYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRER--SDQACWQALEIAQLDATVKALPLGLD 494
Cdd:PRK11176 392 FYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEqySREQIEEAARMAYAMDFINKMDNGLD 471

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 495 SVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVF 574
Cdd:PRK11176 472 TVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVV 551

                        490       500
                 ....*....|....*....|....*
gi 489309308 575 DGGHIAEDGDHQQLIADGGLYAKLY 599
Cdd:PRK11176 552 EDGEIVERGTHAELLAQNGVYAQLH 576
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 369-583 4.76e-65

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: 212.45  E-value: 4.76e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEE--LVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSV 446
Cdd:cd03245    3 IEFRNVSFSYPNQeiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPALFNDTVRANLTMGR-ERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVV 525
Cdd:cd03245   83 VPQDVTLFYGTLRDNITLGApLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 526 ILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDG 583
Cdd:cd03245  163 LLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
 101-598 2.34e-63

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: 221.37  E-value: 2.34e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  101 GALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGtvttHLVTDLDTVDKfVGETLSrflVAMLTLVGT 180
Cdd:TIGR03797 188 GAAAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFFRQYSTG----DLASRAMGISQ-IRRILS---GSTLTTLLS 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  181 S-------GILMWMHWKLALLILLFNPLVIYATVQLG-KRVKHLKKLENDSTSRFTQALtETLDAIQEVR-AGNRQGFFL 251
Cdd:TIGR03797 260 GifallnlGLMFYYSWKLALVAVALALVAIAVTLVLGlLQVRKERRLLELSGKISGLTV-QLINGISKLRvAGAENRAFA 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  252 GRLGQRAQEVRDFAVNSQWKSDASSRASGLLFQFGIDIFrAAAMLTVLFSDLSIGQMLAVFSYLWFMISPVEQLLNLQYA 331
Cdd:TIGR03797 339 RWAKLFSRQRKLELSAQRIENLLTVFNAVLPVLTSAALF-AAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLIS 417

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  332 YYAAGGALTRINELLAraDEPQYAGG-ADPftGRETVGIEVRGLNFGYGEE--LVLDQLNLNIAPGEKVAIVGASGGGKS 408
Cdd:TIGR03797 418 ILAVIPLWERAKPILE--ALPEVDEAkTDP--GKLSGAIEVDRVTFRYRPDgpLILDDVSLQIEPGEFVAIVGPSGSGKS 493

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  409 TLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRERSDQACWQALEIAQLDATVKA 488
Cdd:TIGR03797 494 TLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRA 573

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  489 LPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARfLSGrTTLIIAHRLSAVKQA 568
Cdd:TIGR03797 574 MPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLER-LKV-TRIVIAHRLSTIRNA 651

                         490       500       510
                  ....*....|....*....|....*....|
gi 489309308  569 DRVLVFDGGHIAEDGDHQQLIADGGLYAKL 598
Cdd:TIGR03797 652 DRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 108-573 4.65e-61

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: 211.38  E-value: 4.65e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  108 LQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFvgetLSRFLVAM-LTLVGTSGIL-- 184
Cdd:TIGR02857  63 LQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGY----FARYLPQLvLAVIVPLAILaa 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  185 -MWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVRD 263
Cdd:TIGR02857 139 vFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRE 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  264 FAVNSQWKSDASSRASGLLFQFGIDIFRAAAMLTVLFSDLSIGQ-----MLAVFSYLwfmisPVEQLLNLQYAYYAAGGA 338
Cdd:TIGR02857 219 RTMRVLRIAFLSSAVLELFATLSVALVAVYIGFRLLAGDLDLATglfvlLLAPEFYL-----PLRQLGAQYHARADGVAA 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  339 LTRINELLARAdePQYAGGADPFTGRETVGIEVRGLNFGY-GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGL 417
Cdd:TIGR02857 294 AEALFAVLDAA--PRPLAGKAPVTAAPASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF 371

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  418 YTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGR-ERSDQACWQALEIAQLDATVKALPLGLDSV 496
Cdd:TIGR02857 372 VDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARpDASDAEIREALERAGLDEFVAALPQGLDTP 451

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308  497 VGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLV 573
Cdd:TIGR02857 452 IGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVV 528
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 110-562 2.53e-58

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: 204.13  E-value: 2.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  110 ARLFARLA-KDIVYRI----RVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGIL 184
Cdd:TIGR02868  69 FRYLERLVgHDAALRSlgalRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAI 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  185 MWMHWKLA-------LLILLFNPLVIY-ATVQLGKRVKHLKklendstSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQ 256
Cdd:TIGR02868 149 AVLSVPAAlilaaglLLAGFVAPLVSLrAARAAEQALARLR-------GELAAQLTDALDGAAELVASGALPAALAQVEE 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  257 RAQEVRDfAVNSQWKSDASSRASGLLFQfGIDIFRAAAMLTVLFSDLSI-GQMLAVFSYLWF-MISPVEQLLNLQYAYYA 334
Cdd:TIGR02868 222 ADRELTR-AERRAAAATALGAALTLLAA-GLAVLGALWAGGPAVADGRLaPVTLAVLVLLPLaAFEAFAALPAAAQQLTR 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  335 AGGALTRINELLARA---DEPQYAGGADpfTGRETVGIEVRGLNFGY-GEELVLDQLNLNIAPGEKVAIVGASGGGKSTL 410
Cdd:TIGR02868 300 VRAAAERIVEVLDAAgpvAEGSAPAAGA--VGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTL 377

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  411 VQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGR-ERSDQACWQALEIAQLDATVKAL 489
Cdd:TIGR02868 378 LATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRAL 457

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308  490 PLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRL 562
Cdd:TIGR02868 458 PDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
189-604 5.00e-55

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 196.09  E-value: 5.00e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 189 WKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAgnrqgfflgrLGQRAQEVRDFAVNS 268
Cdd:PRK10789 137 WQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKA----------FGLEDRQSALFAADA 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 269 QWKSDASSRASGLLFQFGIDIFRAAAMLT----------VLFSDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAAGGA 338
Cdd:PRK10789 207 EDTGKKNMRVARIDARFDPTIYIAIGMANllaigggswmVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAA 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 339 LTRINELLARAdePQYAGGADPF-TGRETVGIEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGL 417
Cdd:PRK10789 287 YSRIRAMLAEA--PVVKDGSEPVpEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRH 364

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 418 YTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRERSDQAcwQALEIAQLdATVKA----LPLGL 493
Cdd:PRK10789 365 FDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQ--EIEHVARL-ASVHDdilrLPQGY 441

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 494 DSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLV 573
Cdd:PRK10789 442 DTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILV 521

                        410       420       430
                 ....*....|....*....|....*....|.
gi 489309308 574 FDGGHIAEDGDHQQLIADGGLYAKLYgHLQQ 604
Cdd:PRK10789 522 MQHGHIAQRGNHDQLAQQSGWYRDMY-RYQQ 551
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 152-602 1.10e-54

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 195.04  E-value: 1.10e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 152 LVTDLDTVDKFVGETLSRFLVAMLTLVGTSGILMWMHWKLA-------LLILLFNPLVIYatvQLGKRV-KHLkkleNDS 223
Cdd:PRK11160 123 LVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDLTLAltlggilLLLLLLLPLLFY---RLGKKPgQDL----THL 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 224 TSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVrdfaVNSQWK-SDASSRASGLL-FQFGIdifraAAMLTVLFS 301
Cdd:PRK11160 196 RAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQW----LAAQRRqANLTGLSQALMiLANGL-----TVVLMLWLA 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 302 DLSIGQ------MLAVFSylwFMI-SPVEQLLNLQYAYYAAGGALT---RINELLARADEPQYAGGADPFTGRetVGIEV 371
Cdd:PRK11160 267 AGGVGGnaqpgaLIALFV---FAAlAAFEALMPVAGAFQHLGQVIAsarRINEITEQKPEVTFPTTSTAAADQ--VSLTL 341

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 372 RGLNFGY--GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQ 449
Cdd:PRK11160 342 NNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQ 421

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 450 HPALFNDTVRANLTMGRER-SDQACWQALEIAQLDATVKAlPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILD 528
Cdd:PRK11160 422 RVHLFSATLRDNLLLAAPNaSDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLD 500

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308 529 EATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGGLYAKLYGHL 602
Cdd:PRK11160 501 EPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 334-606 2.00e-54

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 194.68  E-value: 2.00e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 334 AAGGALTRINELLArADEPQYAGGADPFTGRETVGIEVRGLN-FGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQ 412
Cdd:PRK11174 316 QAVGAAESLVTFLE-TPLAHPQQGEKELASNDPVTIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLN 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 413 LLLGlYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRER-SDQACWQALEIAQLDATVKALPL 491
Cdd:PRK11174 395 ALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDaSDEQLQQALENAWVSEFLPLLPQ 473

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 492 GLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRV 571
Cdd:PRK11174 474 GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQI 553

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 489309308 572 LVFDGGHIAEDGDHQQLIADGGLYAKLYGHLQQVR 606
Cdd:PRK11174 554 WVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEEI 588
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 123-595 1.62e-52

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: 194.78  E-value: 1.62e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   123 RIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGILMWMHWKLALLILlfnPL- 201
Cdd:TIGR00957 1039 VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIP---PLg 1115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   202 VIYATVQ--LGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQgfflgrlgqraqevRDFAVNSQWKSDASSRA- 278
Cdd:TIGR00957 1116 LLYFFVQrfYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQ--------------ERFIHQSDLKVDENQKAy 1181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   279 -----SGLLFQFGID-----IFRAAAMLTVL--------FSDLSIGQMLAVFSYLWFMISPVEQL-LNLQyayyaaggAL 339
Cdd:TIGR00957 1182 ypsivANRWLAVRLEcvgncIVLFAALFAVIsrhslsagLVGLSVSYSLQVTFYLNWLVRMSSEMeTNIV--------AV 1253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   340 TRINELLARADE-PQYAGGADPFTGRETVG-IEVRGLNFGYGE--ELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLL 415
Cdd:TIGR00957 1254 ERLKEYSETEKEaPWQIQETAPPSGWPPRGrVEFRNYCLRYREdlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLF 1333

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   416 GLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRERSDQACWQALEIAQLDATVKALPLGLDS 495
Cdd:TIGR00957 1334 RINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDH 1413

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   496 VVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEyNLHQALARF-LSGRTTLIIAHRLSAVKQADRVLVF 574
Cdd:TIGR00957 1414 ECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-NLIQSTIRTqFEDCTVLTIAHRLNTIMDYTRVIVL 1492

                          490       500
                   ....*....|....*....|.
gi 489309308   575 DGGHIAEDGDHQQLIADGGLY 595
Cdd:TIGR00957 1493 DKGEVAEFGAPSNLLQQRGIF 1513
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 369-591 1.62e-51

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: 176.75  E-value: 1.62e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGY-GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVV 447
Cdd:COG1122    1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPA--LFNDTVRA-------NLTMGRERSDQACWQALEIaqldatvkalpLGLDSVVGRSGVRFSGGQRQRLAIARmV 518
Cdd:COG1122   81 FQNPDdqLFAPTVEEdvafgpeNLGLPREEIRERVEEALEL-----------VGLEHLADRPPHELSGGQKQRVAIAG-V 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308 519 LA-EPKVVILDEATSALDAATEYNLHQALARF-LSGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:COG1122  149 LAmEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDlVAELADRVIVLDDGRIVADGTPREVFSD 224
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 369-579 4.73e-49

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: 170.34  E-value: 4.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGY---GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVS 445
Cdd:cd03248   12 VKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 446 VVLQHPALFNDTVRANLTMG-RERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKV 524
Cdd:cd03248   92 LVGQEPVLFARSLQDNIAYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 525 VILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHI 579
Cdd:cd03248  172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 104-590 1.43e-48

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: 178.02  E-value: 1.43e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLseyesLGSGTVTTHLVTDLDTVDKFV-GETLSRFLVAMLTLVgtsg 182
Cdd:COG4618   75 LLDAVRSRILVRVGARLDRRLGPRVFDAAFRAAL-----RGGGGAAAQALRDLDTLRQFLtGPGLFALFDLPWAPI---- 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 183 ilmwmhwkLALLILLFNPL-----VIYATVQLG------KRVKHLKKLENDSTSRFTQALTETLDAIQEVRAgnrQGFfL 251
Cdd:COG4618  146 --------FLAVLFLFHPLlgllaLVGALVLVAlallneRLTRKPLKEANEAAIRANAFAEAALRNAEVIEA---MGM-L 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 252 GRLGQRAQEVRDFAVNSQwkSDASSRASG---------LLFQfgIDIFRAAAMLtVLFSDLSIGQMLAVfSYLwfM---I 319
Cdd:COG4618  214 PALRRRWQRANARALALQ--ARASDRAGGfsalskflrLLLQ--SAVLGLGAYL-VIQGEITPGAMIAA-SIL--MgraL 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 320 SPVEQLLNLQYAYYAAGGALTRINELLA-RADEPQYAGGADPfTGRetvgIEVRGLNFGY--GEELVLDQLNLNIAPGEK 396
Cdd:COG4618  286 APIEQAIGGWKQFVSARQAYRRLNELLAaVPAEPERMPLPRP-KGR----LSVENLTVVPpgSKRPILRGVSFSLEPGEV 360

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 397 VAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRERSDQACWQA 476
Cdd:COG4618  361 LGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAA 440

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 477 LEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARF-LSGRTT 555
Cdd:COG4618  441 AKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATV 520

                        490       500       510
                 ....*....|....*....|....*....|....*
gi 489309308 556 LIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:COG4618  521 VVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 369-583 1.54e-47

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: 164.41  E-value: 1.54e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEE--LVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGlETIRENVSV 446
Cdd:cd03247    1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPALFNDTVRANLtmgrersdqacwqaleiaqldatvkalplgldsvvgrsGVRFSGGQRQRLAIARMVLAEPKVVI 526
Cdd:cd03247   80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 527 LDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDG 583
Cdd:cd03247  122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
369-579 4.38e-47

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 164.22  E-value: 4.38e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVL 448
Cdd:COG4619    1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALFNDTVRANLTMGRERSDQACWQALEIAQLDAtvkalpLGLD-SVVGRSGVRFSGGQRQRLAIARMVLAEPKVVIL 527
Cdd:COG4619   81 QEPALWGGTVRDNLPFPFQLRERKFDRERALELLER------LGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 528 DEATSALDAATEYNLHQALARFL--SGRTTLIIAH-RLSAVKQADRVLVFDGGHI 579
Cdd:COG4619  155 DEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 370-578 4.40e-46

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: 161.48  E-value: 4.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 370 EVRGLNFGY--GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVV 447
Cdd:cd03225    1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPA--LFNDTVRA-------NLTMGRERSDQACWQALEIaqldatvkalpLGLDSVVGRSGVRFSGGQRQRLAIARMV 518
Cdd:cd03225   81 FQNPDdqFFGPTVEEevafgleNLGLPEEEIEERVEEALEL-----------VGLEGLRDRSPFTLSGGQKQRVAIAGVL 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 519 LAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIA-HRLSAVKQ-ADRVLVFDGGH 578
Cdd:cd03225  150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 339-591 4.75e-46

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: 170.08  E-value: 4.75e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 339 LTRINELLARADEPQYAGGADPFTGRETVGIEVRGLNFGY-----GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQL 413
Cdd:COG1123  231 LAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARL 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 414 LLGLYTPQAGSIRFGG---STQQEIGLETIRENVSVVLQHP-ALFN--DTVRANLTMG---------RERSDQACwQALE 478
Cdd:COG1123  311 LLGLLRPTSGSILFDGkdlTKLSRRSLRELRRRVQMVFQDPySSLNprMTVGDIIAEPlrlhgllsrAERRERVA-ELLE 389

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 479 IAQLDAtvkalplgldSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEY---NLHQALARFLsGRTT 555
Cdd:COG1123  390 RVGLPP----------DLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAqilNLLRDLQREL-GLTY 458

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 489309308 556 LIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:COG1123  459 LFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 369-581 2.59e-44

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: 156.80  E-value: 2.59e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEEL--VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSV 446
Cdd:cd03369    7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPALFNDTVRANLTMGRERSDQACWQALEIAQldatvkalplgldsvvgrSGVRFSGGQRQRLAIARMVLAEPKVVI 526
Cdd:cd03369   87 IPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRVSE------------------GGLNLSQGQRQLLCLARALLKRPRVLV 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 527 LDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAE 581
Cdd:cd03369  149 LDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 369-598 4.21e-44

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: 157.76  E-value: 4.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEEL--VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSV 446
Cdd:cd03288   20 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPALFNDTVRANLTMGRERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVI 526
Cdd:cd03288  100 ILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308 527 LDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIA-DGGLYAKL 598
Cdd:cd03288  180 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAqEDGVFASL 252
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
369-590 1.12e-43

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 155.99  E-value: 1.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLEtIRENVSVVL 448
Cdd:COG1131    1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALFND-TVRANLT-------MGRERSDQACWQALEIaqldatvkalpLGLDSVVGRSGVRFSGGQRQRLAIARMVLA 520
Cdd:COG1131   80 QEPALYPDlTVRENLRffarlygLPRKEARERIDELLEL-----------FGLTDAADRKVGTLSGGMKQRLGLALALLH 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 521 EPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIA-HRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:COG1131  149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 369-591 5.46e-43

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: 154.58  E-value: 5.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEEL----VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENV 444
Cdd:COG1124    2 LEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 445 SVVLQHPAL-FND--TVRANLT-----MGRERSDQACWQALEIAQLDAtvkalplgldSVVGRSGVRFSGGQRQRLAIAR 516
Cdd:COG1124   82 QMVFQDPYAsLHPrhTVDRILAeplriHGLPDREERIAELLEQVGLPP----------SFLDRYPHQLSGGQRQRVAIAR 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 517 MVLAEPKVVILDEATSALDAATeynlhQA-LARFL------SGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQL 588
Cdd:COG1124  152 ALILEPELLLLDEPTSALDVSV-----QAeILNLLkdlreeRGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226


                 ...
gi 489309308 589 IAD 591
Cdd:COG1124  227 LAG 229
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 251-590 4.80e-42

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: 159.44  E-value: 4.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  251 LGRLGQRAQEVRDFAVNSQwkSDASSRASGLlfQFGIDIFRAA---AMLT-----VLFSDLSIGQMLAVFSYLWFMISPV 322
Cdd:TIGR01842 199 MGNLTKRWGRFHSKYLSAQ--SAASDRAGML--SNLSKYFRIVlqsLVLGlgaylAIDGEITPGMMIAGSILVGRALAPI 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  323 EQLLNLQYAYYAAGGALTRINELLAradepQYAGGADPFTGRETVG-IEVRGLNFGY--GEELVLDQLNLNIAPGEKVAI 399
Cdd:TIGR01842 275 DGAIGGWKQFSGARQAYKRLNELLA-----NYPSRDPAMPLPEPEGhLSVENVTIVPpgGKKPTLRGISFSLQAGEALAI 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  400 VGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLT-MGRERSDQACWQALE 478
Cdd:TIGR01842 350 IGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIArFGENADPEKIIEAAK 429

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  479 IAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARF-LSGRTTLI 557
Cdd:TIGR01842 430 LAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVV 509

                         330       340       350
                  ....*....|....*....|....*....|...
gi 489309308  558 IAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:TIGR01842 510 ITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 369-579 5.39e-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: 149.29  E-value: 5.39e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYG--EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSV 446
Cdd:cd03246    1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPALFNDTVRANLtmgrersdqacwqaleiaqldatvkalplgldsvvgrsgvrFSGGQRQRLAIARMVLAEPKVVI 526
Cdd:cd03246   81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489309308 527 LDEATSALDAATEYNLHQALARF-LSGRTTLIIAHRLSAVKQADRVLVFDGGHI 579
Cdd:cd03246  120 LDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 369-577 1.30e-41

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: 149.16  E-value: 1.30e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEE-----LVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGStqqeigletiren 443
Cdd:cd03250    1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 444 VSVVLQHPALFNDTVRANLTMGRERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPK 523
Cdd:cd03250   68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308 524 VVILDEATSALDAATEYNL-HQALARFLS-GRTTLIIAHRLSAVKQADRVLVFDGG 577
Cdd:cd03250  148 IYLLDDPLSAVDAHVGRHIfENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNG 203
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 369-590 1.68e-41

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: 149.96  E-value: 1.68e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG---STQQEIGLETIRENVS 445
Cdd:cd03261    1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGediSGLSEAELYRLRRRMG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 446 VVLQHPALFND-TV--------RANLTMGRERSDQACWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIAR 516
Cdd:cd03261   81 MLFQSGALFDSlTVfenvafplREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAEL-----------SGGMKKRVALAR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 517 MVLAEPKVVILDEATSALD--AATEYN-----LHQALarflsGRTTLIIAHRL-SAVKQADRVLVFDGGHIAEDGDHQQL 588
Cdd:cd03261  150 ALALDPELLLYDEPTAGLDpiASGVIDdlirsLKKEL-----GLTSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEEL 224


                 ..
gi 489309308 589 IA 590
Cdd:cd03261  225 RA 226
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 369-582 5.04e-41

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: 148.39  E-value: 5.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEE----LVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLEtirenV 444
Cdd:cd03293    1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 445 SVVLQHPALFN-DTVRANLTMG--------RERSDQACwQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIA 515
Cdd:cd03293   76 GYVFQQDALLPwLTVLDNVALGlelqgvpkAEARERAE-ELLELVGLSGFENAYPHQL-----------SGGMRQRVALA 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 516 RMVLAEPKVVILDEATSALDAATEYNLHQALARFLS--GRTTLIIAHRLS-AVKQADRVLVFDG--GHIAED 582
Cdd:cd03293  144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 369-591 5.90e-41

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 148.60  E-value: 5.90e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEIG-----LETIREN 443
Cdd:COG1126    2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDG---EDLTdskkdINKLRRK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 444 VSVVLQHPALFND-TVRANLTMG----RERSDQacwQALEIAQ-------LDATVKALPLGLdsvvgrsgvrfSGGQRQR 511
Cdd:COG1126   79 VGMVFQQFNLFPHlTVLENVTLApikvKKMSKA---EAEERAMellervgLADKADAYPAQL-----------SGGQQQR 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 512 LAIARmVLA-EPKVVILDEATSALDAatEY-----NLHQALARflSGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGD 584
Cdd:COG1126  145 VAIAR-ALAmEPKVMLFDEPTSALDP--ELvgevlDVMRDLAK--EGMTMVVVTHEMGfAREVADRVVFMDGGRIVEEGP 219


                 ....*..
gi 489309308 585 HQQLIAD 591
Cdd:COG1126  220 PEEFFEN 226
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 369-582 1.34e-40

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 148.31  E-value: 1.34e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGY----GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLEtirenV 444
Cdd:COG1116    8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 445 SVVLQHPALFN-DTVRANLTMG--------RERSDQACwQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIA 515
Cdd:COG1116   83 GVVFQEPALLPwLTVLDNVALGlelrgvpkAERRERAR-ELLELVGLAGFEDAYPHQL-----------SGGMRQRVAIA 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 516 RMVLAEPKVVILDEATSALDAATEYNLHQALARFL--SGRTTLIIAHRLS-AVKQADRVLVFDG--GHIAED 582
Cdd:COG1116  151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWqeTGKTVLFVTHDVDeAVFLADRVVVLSArpGRIVEE 222
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 369-579 1.39e-40

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: 146.91  E-value: 1.39e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGS--TQQEIGLETIRENVSV 446
Cdd:cd03262    1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLklTDDKKNINELRQKVGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPALF-NDTVRANLTMG----RERSDQacwQALEIA-QLDATVkalplGLDSVVGRSGVRFSGGQRQRLAIARMVLA 520
Cdd:cd03262   81 VFQQFNLFpHLTVLENITLApikvKGMSKA---EAEERAlELLEKV-----GLADKADAYPAQLSGGQQQRVAIARALAM 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308 521 EPKVVILDEATSALDA--ATE-YNLHQALARflSGRTTLIIAHRLS-AVKQADRVLVFDGGHI 579
Cdd:cd03262  153 NPKVMLFDEPTSALDPelVGEvLDVMKDLAE--EGMTMVVVTHEMGfAREVADRVIFMDDGRI 213
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 369-601 1.65e-40

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 147.54  E-value: 1.65e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTqqeigLETIRENVSVVL 448
Cdd:COG1121    7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIGYVP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALFND---TVRANLTMGR-----------ERSDQACWQALEiaqldaTVKALPLgLDSVVGRsgvrFSGGQRQRLAI 514
Cdd:COG1121   82 QRAEVDWDfpiTVRDVVLMGRygrrglfrrpsRADREAVDEALE------RVGLEDL-ADRPIGE----LSGGQQQRVLL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 515 ARMVLAEPKVVILDEATSALDAATEYNLHQALARFLS-GRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAeDGDHQQLIADG 592
Cdd:COG1121  151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREyFDRVLLLNRGLVA-HGPPEEVLTPE 229


                 ....*....
gi 489309308 593 GLyAKLYGH 601
Cdd:COG1121  230 NL-SRAYGG 237
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 369-588 2.28e-40

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: 146.56  E-value: 2.28e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLY-----TPQAGSIRFGGST--QQEIGLETIR 441
Cdd:cd03260    1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDiyDLDVDVLELR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 442 ENVSVVLQHPALFNDTVRANLTMG--------RERSDQACWQALEIAQLDATVK--ALPLGLdsvvgrsgvrfSGGQRQR 511
Cdd:cd03260   81 RRVGMVFQKPNPFPGSIYDNVAYGlrlhgiklKEELDERVEEALRKAALWDEVKdrLHALGL-----------SGGQQQR 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 512 LAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQL 588
Cdd:cd03260  150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 369-583 2.76e-40

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: 146.50  E-value: 2.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEEL----VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG---STQQEIGLETIR 441
Cdd:cd03257    2 LEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIRR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 442 ENVSVVLQHP-----------ALFNDTVRANLTMGRErsdqacwQALEIAQLDATVKalpLGLDS-VVGRSGVRFSGGQR 509
Cdd:cd03257   82 KEIQMVFQDPmsslnprmtigEQIAEPLRIHGKLSKK-------EARKEAVLLLLVG---VGLPEeVLNRYPHELSGGQR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 510 QRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARF--LSGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDG 583
Cdd:cd03257  152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 369-590 4.70e-40

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: 146.28  E-value: 4.70e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG---STQQEIGLETIRENVS 445
Cdd:COG1127    6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdiTGLSEKELYELRRRIG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 446 VVLQHPALFND-TVRANLTMG-RERSDqacwqaLEIAQLDATVKALpLGLdsvVGRSGVRF------SGGQRQRLAIARM 517
Cdd:COG1127   86 MLFQGGALFDSlTVFENVAFPlREHTD------LSEAEIRELVLEK-LEL---VGLPGAADkmpselSGGMRKRVALARA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 518 VLAEPKVVILDEATSALD--AATEYN-----LHQALarflsGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLI 589
Cdd:COG1127  156 LALDPEILLYDEPTAGLDpiTSAVIDelireLRDEL-----GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELL 230


                 .
gi 489309308 590 A 590
Cdd:COG1127  231 A 231
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 369-583 1.04e-39

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: 144.20  E-value: 1.04e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstQQEIGLETIRENVSVVL 448
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG--RDVTGVPPERRNIGMVF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALF-NDTVRAN----LTMGRERSDQACWQALEIAQLdatvkalpLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPK 523
Cdd:cd03259   79 QDYALFpHLTVAENiafgLKLRGVPKAEIRARVRELLEL--------VGLEGLLNRYPHELSGGQQQRVALARALAREPS 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308 524 VVILDEATSALDAATEYNLHQALARFLS--GRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDG 583
Cdd:cd03259  151 LLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
PLN03130 PLN03130
ABC transporter C family member; Provisional
 369-593 1.05e-39

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 156.44  E-value: 1.05e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  369 IEVRGLNFGYGEEL--VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSV 446
Cdd:PLN03130 1238 IKFEDVVLRYRPELppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGI 1317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  447 VLQHPALFNDTVRANLTMGRERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVI 526
Cdd:PLN03130 1318 IPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILV 1397

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308  527 LDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGG 593
Cdd:PLN03130 1398 LDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
PLN03232 PLN03232
ABC transporter C family member; Provisional
 123-598 3.74e-39

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 154.75  E-value: 3.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  123 RIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRF------LVAMLTLVGT-SGILMWMhwKLALLI 195
Cdd:PLN03232  984 RLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFmnqlwqLLSTFALIGTvSTISLWA--IMPLLI 1061

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  196 LLFNPLVIYATVQlgKRVKHLkklenDSTSR------FTQALTeTLDAIQEVRAGNRQGFFLGRlgQRAQEVRDFAVNS- 268
Cdd:PLN03232 1062 LFYAAYLYYQSTS--REVRRL-----DSVTRspiyaqFGEALN-GLSSIRAYKAYDRMAKINGK--SMDNNIRFTLANTs 1131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  269 --QWKSDASSRASGLLFqfgidifraaaMLTVLFSDLSIGQM--LAVFS-----YLWFMISPVEQLLNLQYAYYAAGGAL 339
Cdd:PLN03232 1132 snRWLTIRLETLGGVMI-----------WLTATFAVLRNGNAenQAGFAstmglLLSYTLNITTLLSGVLRQASKAENSL 1200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  340 TRINELLARADEPQYAGGAD----PFTGRETVG-IEVRGLNFGYGEEL--VLDQLNLNIAPGEKVAIVGASGGGKSTLVQ 412
Cdd:PLN03232 1201 NSVERVGNYIDLPSEATAIIennrPVSGWPSRGsIKFEDVHLRYRPGLppVLHGLSFFVSPSEKVGVVGRTGAGKSSMLN 1280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  413 LLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRERSDQACWQALEIAQLDATVKALPLG 492
Cdd:PLN03232 1281 ALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFG 1360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  493 LDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVL 572
Cdd:PLN03232 1361 LDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKIL 1440

                         490       500
                  ....*....|....*....|....*..
gi 489309308  573 VFDGGHIAEDGDHQQLIA-DGGLYAKL 598
Cdd:PLN03232 1441 VLSSGQVLEYDSPQELLSrDTSAFFRM 1467
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 102-590 4.81e-39

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: 150.72  E-value: 4.81e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 102 ALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVgETLSRFLVAMLTLVGTS 181
Cdd:COG4615   61 LLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAF-VRLPELLQSVALVLGCL 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 182 GILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVR--AGNRQGFFLGRLGQRAQ 259
Cdd:COG4615  140 AYLAWLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKlnRRRRRAFFDEDLQPTAE 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 260 EVRDFAV--NSQWkSDASSRASGLLFQF-GIDIFraaamLTVLFSDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAAG 336
Cdd:COG4615  220 RYRDLRIraDTIF-ALANNWGNLLFFALiGLILF-----LLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRAN 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 337 GALTRINELLAR--ADEPQYAGGADPFTGRETVGIEVRGLNFGYGEEL-----VLDQLNLNIAPGEKVAIVGASGGGKST 409
Cdd:COG4615  294 VALRKIEELELAlaAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKST 373

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 410 LVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVranltmgrersdqacwqALEIAQLDATVKAL 489
Cdd:COG4615  374 LAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRLL-----------------GLDGEADPARAREL 436

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 490 --PLGLDSVV----GR-SGVRFSGGQRQRLAIArMVLAEPK-VVILDEATSALDAA------TEynLHQALARflSGRTT 555
Cdd:COG4615  437 leRLELDHKVsvedGRfSTTDLSQGQRKRLALL-VALLEDRpILVFDEWAADQDPEfrrvfyTE--LLPELKA--RGKTV 511

                        490       500       510
                 ....*....|....*....|....*....|....*
gi 489309308 556 LIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:COG4615  512 IAISHDDRYFDLADRVLKMDYGKLVELTGPAALAA 546
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 369-579 1.10e-38

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: 141.86  E-value: 1.10e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEE----LVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG---STQQEIGLETIR 441
Cdd:cd03255    1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdiSKLSEKELAAFR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 442 -ENVSVVLQHPALFND-TVRANLTM-----GRERSDQACW--QALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRL 512
Cdd:cd03255   81 rRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRERaeELLERVGLGDRLNHYPSEL-----------SGGQQQRV 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 513 AIARMVLAEPKVVILDEATSALDAATE---YNLHQALARfLSGRTTLIIAHRLSAVKQADRVLVFDGGHI 579
Cdd:cd03255  150 AIARALANDPKIILADEPTGNLDSETGkevMELLRELNK-EAGTTIVVVTHDPELAEYADRIIELRDGKI 218
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 369-579 1.70e-38

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 139.46  E-value: 1.70e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIR-FGGSTQQEIglETIRENVSVV 447
Cdd:cd03230    1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvLGKDIKKEP--EEVKRRIGYL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALFND-TVRANLtmgrersdqacwqaleiaqldatvkalplgldsvvgrsgvRFSGGQRQRLAIARMVLAEPKVVI 526
Cdd:cd03230   79 PEEPSLYENlTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLI 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 527 LDEATSALDAATEYNLHQALARFLS-GRTTLIIAHRLSAVKQ-ADRVLVFDGGHI 579
Cdd:cd03230  119 LDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 370-578 1.84e-38

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 138.92  E-value: 1.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 370 EVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQ 449
Cdd:cd00267    1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 450 hpalfndtvranltmgrersdqacwqaleiaqldatvkalplgldsvvgrsgvrFSGGQRQRLAIARMVLAEPKVVILDE 529
Cdd:cd00267   81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489309308 530 ATSALDAATEYNLHQALARFL-SGRTTLIIAHRLSAVKQA-DRVLVFDGGH 578
Cdd:cd00267  107 PTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
 104-342 4.45e-38

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: 142.30  E-value: 4.45e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGI 183
Cdd:cd07346   54 LLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVI 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 184 LMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVRD 263
Cdd:cd07346  134 LFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRD 213

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 264 FAVNSQWKSDASSRASGLLFQFGIDIFRAAAMLTVLFSDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAAGGALTRI 342
Cdd:cd07346  214 ANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 369-590 2.31e-37

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: 138.48  E-value: 2.31e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLN--FG--YGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG---STQQEIGLETIR 441
Cdd:cd03258    2 IELKNVSkvFGdtGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdlTLLSGKELRKAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 442 ENVSVVLQHPALFND-TVRANLTMgrersdqacwqALEIAQLD-ATVKALPLGLDSVVGRSGVR------FSGGQRQRLA 513
Cdd:cd03258   82 RRIGMIFQHFNLLSSrTVFENVAL-----------PLEIAGVPkAEIEERVLELLELVGLEDKAdaypaqLSGGQKQRVG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 514 IARMVLAEPKVVILDEATSALDAATEynlHQALARFLS-----GRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQ 587
Cdd:cd03258  151 IARALANNPKVLLCDEATSALDPETT---QSILALLRDinrelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227


                 ...
gi 489309308 588 LIA 590
Cdd:cd03258  228 VFA 230
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 369-591 6.16e-37

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: 144.28  E-value: 6.16e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGY--GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQA---GSIRFGGSTQQEIGLETIREN 443
Cdd:COG1123    5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 444 VSVVLQHP--ALFNDTVRANLTMGRERSDQACWQALEIA-QLDATVkalplGLDSVVGRSGVRFSGGQRQRLAIARMVLA 520
Cdd:COG1123   85 IGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEARARVlELLEAV-----GLERRLDRYPHQLSGGQRQRVAIAMALAL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308 521 EPKVVILDEATSALDAATEYNLHQALARFL--SGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:COG1123  160 DPDLLIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
369-582 6.52e-37

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 137.10  E-value: 6.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYG----EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG---STQQEIGLETIR 441
Cdd:COG1136    5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdiSSLSERELARLR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 442 -ENVSVVLQHPALFND-TVRANLTM--------GRERSDQAcWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQR 511
Cdd:COG1136   85 rRHIGFVFQFFNLLPElTALENVALplllagvsRKERRERA-RELLERVGLGDRLDHRPSQL-----------SGGQQQR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308 512 LAIARMVLAEPKVVILDEATSALDAATEYNLHQALARF--LSGRTTLIIAHRLSAVKQADRVLVFDGGHIAED 582
Cdd:COG1136  153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 369-589 8.53e-37

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: 137.48  E-value: 8.53e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVL 448
Cdd:COG1120    2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 Q-HPALFNDTVRANLTMGR-----------ERSDQACWQALEIaqldatvkalpLGLDSVVGRSGVRFSGGQRQRLAIAR 516
Cdd:COG1120   82 QePPAPFGLTVRELVALGRyphlglfgrpsAEDREAVEEALER-----------TGLEHLADRPVDELSGGERQRVLIAR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 517 mVLA-EPKVVILDEATSALDAAteynlHQ----ALARFLS---GRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQ 587
Cdd:COG1120  151 -ALAqEPPLLLLDEPTSHLDLA-----HQlevlELLRRLArerGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEE 224


                 ..
gi 489309308 588 LI 589
Cdd:COG1120  225 VL 226
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 369-578 1.02e-36

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: 135.01  E-value: 1.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGS--TQQEIGLETIRENVSV 446
Cdd:cd03229    1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdlTDLEDELPPLRRRIGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPALF-NDTVRANLTMGrersdqacwqaleiaqldatvkalplgldsvvgrsgvrFSGGQRQRLAIARMVLAEPKVV 525
Cdd:cd03229   81 VFQDFALFpHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 526 ILDEATSALDAATEYNLhQALARFL---SGRTTLIIAHRLS-AVKQADRVLVFDGGH 578
Cdd:cd03229  123 LLDEPTSALDPITRREV-RALLKSLqaqLGITVVLVTHDLDeAARLADRVVVLRDGK 178
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 384-583 3.28e-36

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: 134.73  E-value: 3.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIA---PGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG----STQQEIGLETIRENVSVVLQHPALF-N 455
Cdd:cd03297   10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfDSRKKINLPPQQRKIGLVFQQYALFpH 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 456 DTVRANLTMGRERSDQACWQALEIAQLDAtvkalpLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALD 535
Cdd:cd03297   90 LNVRENLAFGLKRKRNREDRISVDELLDL------LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489309308 536 AATEYNLHQALARFLS--GRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDG 583
Cdd:cd03297  164 RALRLQLLPELKQIKKnlNIPVIFVTHDLSeAEYLADRIVVMEDGRLQYIG 214
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 384-532 3.61e-36

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 132.39  E-value: 3.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFND-TVRANL 462
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308  463 TMGR---ERSDQACWQalEIAQLDATVKaLPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATS 532
Cdd:pfam00005  81 RLGLllkGLSKREKDA--RAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 368-588 4.99e-36

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 138.36  E-value: 4.99e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 368 GIEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGsTQQEIGLETIRENVSVV 447
Cdd:COG1118    2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG-RDLFTNLPPRERRVGFV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALF-NDTVRANLTMG-----------RERSDQacWqaLEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIA 515
Cdd:COG1118   81 FQHYALFpHMTVAENIAFGlrvrppskaeiRARVEE--L--LELVQLEGLADRYPSQL-----------SGGQRQRVALA 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308 516 RMVLAEPKVVILDEATSALDAATEYNLHQALARFLS--GRTTLIIAH-RLSAVKQADRVLVFDGGHIAEDGDHQQL 588
Cdd:COG1118  146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEV 221
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 369-559 3.29e-35

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


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 131.83  E-value: 3.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGsTQQEIGLETIRENVSVVL 448
Cdd:COG4133    3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG-EPIRDAREDYRRRLAYLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALFND-TVRANLTM-----GRERSDQACWQALEIaqldatvkalpLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEP 522
Cdd:COG4133   82 HADGLKPElTVRENLRFwaalyGLRADREAIDEALEA-----------VGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 489309308 523 KVVILDEATSALDAATEYNLHQALARFLSGRTTLIIA 559
Cdd:COG4133  151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLT 187
PLN03232 PLN03232
ABC transporter C family member; Provisional
 103-598 4.42e-34

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 138.96  E-value: 4.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  103 LVFNVL-QARLFARLAKdIVYRIRVRLIERLKRISL----SEYESLGSGTVTTHLVTDLDTVDKfVGETLSRFLVAMLTL 177
Cdd:PLN03232  351 VTFGVLcESQYFQNVGR-VGFRLRSTLVAAIFHKSLrlthEARKNFASGKVTNMITTDANALQQ-IAEQLHGLWSAPFRI 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  178 VgTSGILMWMHWKLALLillFNPLVIYATVQLG----KRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGR 253
Cdd:PLN03232  429 I-VSMVLLYQQLGVASL---FGSLILFLLIPLQtlivRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESR 504

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  254 L-GQRAQEVRDFavnsqwksdassRASGLLFQFGIDIFRAAAMLTVLFS---------DLSIGQMLAVFSYLWFMISPVE 323
Cdd:PLN03232  505 IqGIRNEELSWF------------RKAQLLSAFNSFILNSIPVVVTLVSfgvfvllggDLTPARAFTSLSLFAVLRSPLN 572

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  324 QLLNLQYAYYAAGGALTRINELLArADEPQYAggADPFTGRETVGIEVRGLNFGYGEEL---VLDQLNLNIAPGEKVAIV 400
Cdd:PLN03232  573 MLPNLLSQVVNANVSLQRIEELLL-SEERILA--QNPPLQPGAPAISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIV 649

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  401 GASGGGKSTLVQLLLGLYTPQagsirfggstqqEIGLETIRENVSVVLQHPALFNDTVRANLTMGRERSDQACWQALEIA 480
Cdd:PLN03232  650 GGTGEGKTSLISAMLGELSHA------------ETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVT 717

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  481 QLDATVKALPlGLD-SVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARF-LSGRTTLII 558
Cdd:PLN03232  718 ALQHDLDLLP-GRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDeLKGKTRVLV 796

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 489309308  559 AHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGGLYAKL 598
Cdd:PLN03232  797 TNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL 836
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 369-590 4.48e-34

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: 129.59  E-value: 4.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLEtIRENVSVVL 448
Cdd:COG4555    2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALF-NDTVRANLTM----GRERSDQACWQALEIAQLdatvkalpLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPK 523
Cdd:COG4555   81 DERGLYdRLTVRENIRYfaelYGLFDEELKKRIEELIEL--------LGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 524 VVILDEATSALDAATEYNLHQALARFL-SGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:COG4555  153 VLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQeVEALCDRVVILHKGKVVAQGSLDELRE 221
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 366-591 6.35e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 130.11  E-value: 6.35e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 366 TVGIEVRGLNFGYGEE--LVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIREN 443
Cdd:PRK13632   5 SVMIKVENVSFSYPNSenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 444 VSVVLQHP--ALFNDTVRANLTMGRERSdqaCWQALEIAQ--LDATVKAlplGLDSVVGRSGVRFSGGQRQRLAIARmVL 519
Cdd:PRK13632  85 IGIIFQNPdnQFIGATVEDDIAFGLENK---KVPPKKMKDiiDDLAKKV---GMEDYLDKEPQNLSGGQKQRVAIAS-VL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 520 A-EPKVVILDEATSALDAATEYNLHQALARFLSGRT-TLI-IAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:PRK13632 158 AlNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
369-592 9.40e-34

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 130.14  E-value: 9.40e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGY--GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSV 446
Cdd:PRK13635   6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHP--ALFNDTVRANLTMGRErsDQACWQALEIAQLDATVKAlpLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKV 524
Cdd:PRK13635  86 VFQNPdnQFVGATVQDDVAFGLE--NIGVPREEMVERVDQALRQ--VGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 525 VILDEATSALDA-------ATEYNLHQAlarflSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADG 592
Cdd:PRK13635 162 IILDEATSMLDPrgrrevlETVRQLKEQ-----KGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 368-583 1.07e-33

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: 128.61  E-value: 1.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 368 GIEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEIGLETIRE-NVSV 446
Cdd:cd03296    2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVPVQErNVGF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPALFND-TVRANLTMG-RERSDQACWQALEIaqlDATVKAL--PLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEP 522
Cdd:cd03296   79 VFQHYALFRHmTVFDNVAFGlRVKPRSERPPEAEI---RAKVHELlkLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308 523 KVVILDEATSALDAATEYNLHQALARFLS--GRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDG 583
Cdd:cd03296  156 KVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVG 219
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 369-584 1.08e-33

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 131.76  E-value: 1.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEI-GLETIRENVSVV 447
Cdd:COG3842    6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG---RDVtGLPPEKRNVGMV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALF-NDTVRANLT-------MGRERSDQACWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIARMVL 519
Cdd:COG3842   83 FQDYALFpHLTVAENVAfglrmrgVPKAEIRARVAELLELVGLEGLADRYPHQL-----------SGGQQQRVALARALA 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 520 AEPKVVILDEATSALDAATEYNLHQALARFL--SGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGD 584
Cdd:COG3842  152 PEPRVLLLDEPLSALDAKLREEMREELRRLQreLGITFIYVTHDQEeALALADRIAVMNDGRIEQVGT 219
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
369-591 2.29e-32

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 127.50  E-value: 2.29e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLN--F--GYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG---STQQEIGLETIR 441
Cdd:COG1135    2 IELENLSktFptKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdlTALSERELRAAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 442 ENVSVVLQHPALFND-TVRANLTMgrersdqacwqALEIA-----QLDATVKALplgLDsVVGRSG------VRFSGGQR 509
Cdd:COG1135   82 RKIGMIFQHFNLLSSrTVAENVAL-----------PLEIAgvpkaEIRKRVAEL---LE-LVGLSDkadaypSQLSGGQK 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 510 QRLAIARMVLAEPKVVILDEATSALDAAT-------------EYNLhqalarflsgrTTLIIAHRLSAVKQ-ADRVLVFD 575
Cdd:COG1135  147 QRVGIARALANNPKVLLCDEATSALDPETtrsildllkdinrELGL-----------TIVLITHEMDVVRRiCDRVAVLE 215

                        250
                 ....*....|....*.
gi 489309308 576 GGHIAEDGDHQQLIAD 591
Cdd:COG1135  216 NGRIVEQGPVLDVFAN 231
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 369-591 3.55e-32

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: 126.71  E-value: 3.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLN--FGYGEELV--LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQA---GSIRFGGstqQEIG----- 436
Cdd:COG0444    2 LEVRNLKvyFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDG---EDLLklsek 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 437 -LETIREN-VSVVLQHP--AL---------FNDTVRANLTMGRERSDQACWQALEIAQLDATvkalplglDSVVGRSGVR 503
Cdd:COG0444   79 eLRKIRGReIQMIFQDPmtSLnpvmtvgdqIAEPLRIHGGLSKAEARERAIELLERVGLPDP--------ERRLDRYPHE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 504 FSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEY---NLHQALARFLsGRTTLIIAHRLSAVKQ-ADRVLVFDGGHI 579
Cdd:COG0444  151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAqilNLLKDLQREL-GLAILFITHDLGVVAEiADRVAVMYAGRI 229

                        250
                 ....*....|..
gi 489309308 580 AEDGDHQQLIAD 591
Cdd:COG0444  230 VEEGPVEELFEN 241
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 370-580 4.49e-32

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 123.03  E-value: 4.49e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 370 EVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGStqqeiGLETIRENVSVVLQ 449
Cdd:cd03235    1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 450 HPAL---FNDTVRANLTMGR-------ERSDQACWQALEIAqLDATvkalplGLDSVVGRSGVRFSGGQRQRLAIARMVL 519
Cdd:cd03235   76 RRSIdrdFPISVRDVVLMGLyghkglfRRLSKADKAKVDEA-LERV------GLSELADRQIGELSGGQQQRVLLARALV 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 520 AEPKVVILDEATSALDAATE---YNLHQALARflSGRTTLIIAHRLSAV-KQADRVLVFDGGHIA 580
Cdd:cd03235  149 QDPDLLLLDEPFAGVDPKTQediYELLRELRR--EGMTILVVTHDLGLVlEYFDRVLLLNRTVVA 211
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 369-591 4.86e-32

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: 123.31  E-value: 4.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEI-GLET---IRENV 444
Cdd:cd03224    1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG---RDItGLPPherARAGI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 445 SVVLQHPALFND-TVRANLTMG---RERSDQAcwqaleiAQLDATVKALPLgLDSVVGRSGVRFSGGQRQRLAIARMVLA 520
Cdd:cd03224   78 GYVPEGRRIFPElTVEENLLLGayaRRRAKRK-------ARLERVYELFPR-LKERRKQLAGTLSGGEQQMLAIARALMS 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308 521 EPKVVILDEATSALDAATEYNLHQALARF-LSGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:cd03224  150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELrDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
PTZ00243 PTZ00243
ABC transporter; Provisional
 379-589 7.20e-32

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 132.21  E-value: 7.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  379 GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTV 458
Cdd:PTZ00243 1321 GLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTV 1400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  459 RANLTMGRERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVIL-DEATSALDAA 537
Cdd:PTZ00243 1401 RQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPA 1480

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489309308  538 TEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLI 589
Cdd:PTZ00243 1481 LDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 370-591 8.08e-32

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 126.00  E-value: 8.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 370 EVRGLNFGYGEELV--LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEIG------LETIR 441
Cdd:COG4608   18 PVRGGLFGRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG---QDITglsgreLRPLR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 442 ENVSVVLQHP-ALFND--TVRA---------NLTMGRERSDqacwqalEIAQLDATVkalplGLD-SVVGRSGVRFSGGQ 508
Cdd:COG4608   95 RRMQMVFQDPyASLNPrmTVGDiiaeplrihGLASKAERRE-------RVAELLELV-----GLRpEHADRYPHEFSGGQ 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 509 RQRLAIARMVLAEPKVVILDEATSALDA---ATEYNLHQALARFLsGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGD 584
Cdd:COG4608  163 RQRIGIARALALNPKLIVCDEPVSALDVsiqAQVLNLLEDLQDEL-GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAP 241


                 ....*..
gi 489309308 585 HQQLIAD 591
Cdd:COG4608  242 RDELYAR 248
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 370-583 8.65e-32

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: 121.39  E-value: 8.65e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 370 EVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQ 449
Cdd:cd03214    1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 450 hpalfndtvranltmgrersdqacwqALEIaqldatvkalpLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDE 529
Cdd:cd03214   81 --------------------------ALEL-----------LGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 530 ATSALDAATEYNLHQALARF--LSGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDG 583
Cdd:cd03214  124 PTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 369-579 1.35e-31

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 125.57  E-value: 1.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEI-GLETIRENVSVV 447
Cdd:COG3839    4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG---RDVtDLPPKDRNIAMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALF-NDTVRANLTMG-----------RERSDQAcwqaLEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIA 515
Cdd:COG3839   81 FQSYALYpHMTVYENIAFPlklrkvpkaeiDRRVREA----AELLGLEDLLDRKPKQL-----------SGGQRQRVALG 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 516 RMVLAEPKVVILDEATSALDAA------TE-YNLHQALarflsGRTTLIIAHRLS-AVKQADRVLVFDGGHI 579
Cdd:COG3839  146 RALVREPKVFLLDEPLSNLDAKlrvemrAEiKRLHRRL-----GTTTIYVTHDQVeAMTLADRIAVMNDGRI 212
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 381-591 3.84e-31

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 128.00  E-value: 3.84e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 381 ELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqqeigletiRENVSVVLQHPALFNDTVRA 460
Cdd:COG4178  376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA-----------GARVLFLPQRPYLPLGTLRE 444

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 461 NLT---MGRERSDQACWQALEIAQLDATVKALplgldSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAA 537
Cdd:COG4178  445 ALLypaTAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 538 TEYNLHQALARFLSGrTTLI-IAHRLSAVKQADRVLvfdggHIAEDGDHQQLIAD 591
Cdd:COG4178  520 NEAALYQLLREELPG-TTVIsVGHRSTLAAFHDRVL-----ELTGDGSWQLLPAE 568
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 369-583 6.20e-31

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: 120.05  E-value: 6.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEigLETIRENVSVVL 448
Cdd:cd03301    1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD--LPPKDRDIAMVF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALF-NDTVRAN----LTMGRERSDQACWQALEIAQLdatvkalpLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPK 523
Cdd:cd03301   79 QNYALYpHMTVYDNiafgLKLRKVPKDEIDERVREVAEL--------LQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308 524 VVILDEATSALDAATEYNLHQALARFLS--GRTTLIIAH-RLSAVKQADRVLVFDGGHIAEDG 583
Cdd:cd03301  151 VFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 369-583 7.20e-31

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: 119.63  E-value: 7.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEigLETIRENVSVVL 448
Cdd:cd03268    1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGALI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALF-NDTVRANLTM---GRERSDQACWQALEIaqldatvkalpLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKV 524
Cdd:cd03268   79 EAPGFYpNLTARENLRLlarLLGIRKKRIDEVLDV-----------VGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489309308 525 VILDEATSALDAATEYNLHQALARFL-SGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDG 583
Cdd:cd03268  148 LILDEPTNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
368-585 7.45e-31

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 120.89  E-value: 7.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 368 GIEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGST---QQEIGLETIRE-- 442
Cdd:COG4161    2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEKAIRLlr 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 443 -NVSVVLQH----PALfndTVRANLTmgrersdQACWQALEIAQLDATVKALP----LGLDSVVGRSGVRFSGGQRQRLA 513
Cdd:COG4161   82 qKVGMVFQQynlwPHL---TVMENLI-------EAPCKVLGLSKEQAREKAMKllarLRLTDKADRFPLHLSGGQQQRVA 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308 514 IARMVLAEPKVVILDEATSALD---AATEYNLHQALARflSGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDH 585
Cdd:COG4161  152 IARALMMEPQVLLFDEPTAALDpeiTAQVVEIIRELSQ--TGITQVIVTHEVEfARKVASQVVYMEKGRIIEQGDA 225
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 369-591 1.13e-30

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: 119.85  E-value: 1.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEI-GL---ETIRENV 444
Cdd:cd03219    1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG---EDItGLpphEIARLGI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 445 SVVLQHPALFND-TVRANLTMGRERSDQACWQAL----EIAQLDATVKAL--PLGLDSVVGRSGVRFSGGQRQRLAIARM 517
Cdd:cd03219   78 GRTFQIPRLFPElTVLENVMVAAQARTGSGLLLArarrEEREARERAEELleRVGLADLADRPAGELSYGQQRRLEIARA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 518 VLAEPKVVILDEATSALDAAteynLHQALARFL-----SGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:cd03219  158 LATDPKLLLLDEPAAGLNPE----ETEELAELIrelreRGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNN 233
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 369-579 2.43e-30

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: 118.88  E-value: 2.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstQQEIGLETIRENVSVVL 448
Cdd:cd03300    1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG--KDITNLPPHKRPVNTVF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALFND-TVRANLTMGRERsdqacwQALEIAQLDATVK-ALPL-GLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVV 525
Cdd:cd03300   79 QNYALFPHlTVFENIAFGLRL------KKLPKAEIKERVAeALDLvQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 526 ILDEATSALDAATEY-------NLHQALarflsGRTTLIIAHRLS-AVKQADRVLVFDGGHI 579
Cdd:cd03300  153 LLDEPLGALDLKLRKdmqlelkRLQKEL-----GITFVFVTHDQEeALTMSDRIAVMNKGKI 209
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 369-589 5.84e-30

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: 117.82  E-value: 5.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEeLVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEI-GLETIRENVSVV 447
Cdd:cd03299    1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG---KDItNLPPEKRDISYV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALF-NDTVRANLTMG----RERSDQACWQALEIAQLdatvkalpLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEP 522
Cdd:cd03299   77 PQNYALFpHMTVYKNIAYGlkkrKVDKKEIERKVLEIAEM--------LGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 523 KVVILDEATSALDAATEYNLHQALARF--LSGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLI 589
Cdd:cd03299  149 KILLLDEPFSALDVRTKEKLREELKKIrkEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
cbiO PRK13637
energy-coupling factor transporter ATPase;
369-583 7.24e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 119.38  E-value: 7.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYG-----EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGS--TQQEIGLETIR 441
Cdd:PRK13637   3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVdiTDKKVKLSDIR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 442 ENVSVVLQHP--ALFNDTVR-------ANLTMGRERSDQACWQALEIAQLDatvkalplgLDSVVGRSGVRFSGGQRQRL 512
Cdd:PRK13637  83 KKVGLVFQYPeyQLFEETIEkdiafgpINLGLSEEEIENRVKRAMNIVGLD---------YEDYKDKSPFELSGGQKRRV 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 513 AIARMVLAEPKVVILDEATSALDAATE-------YNLHQAlarflSGRTTLIIAHRLSAV-KQADRVLVFDGGHIAEDG 583
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRdeilnkiKELHKE-----YNMTIILVSHSMEDVaKLADRIIVMNKGKCELQG 227
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 369-586 8.03e-30

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 117.81  E-value: 8.03e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGST---QQEIGLETIRE--- 442
Cdd:PRK11124   3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfSKTPSDKAIRElrr 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 443 NVSVVLQH----PALfndTVRANLT--------MGRERSDQACWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQ 510
Cdd:PRK11124  83 NVGMVFQQynlwPHL---TVQQNLIeapcrvlgLSKDQALARAEKLLERLRLKPYADRFPLHL-----------SGGQQQ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 511 RLAIARMVLAEPKVVILDEATSALD---AATEYNLHQALARflSGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQ 586
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDpeiTAQIVSIIRELAE--TGITQVIVTHEVEvARKTASRVVYMENGHIVEQGDAS 226
PLN03130 PLN03130
ABC transporter C family member; Provisional
 309-598 8.33e-30

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 126.01  E-value: 8.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  309 LAVFSYLWFmisPVEQLLNLQYAYYAAGGALTRINELLArADEPQYAggADPFTGRETVGIEVRGLNFGY---GEELVLD 385
Cdd:PLN03130  561 LSLFAVLRF---PLFMLPNLITQAVNANVSLKRLEELLL-AEERVLL--PNPPLEPGLPAISIKNGYFSWdskAERPTLS 634

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  386 QLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGsirfggstqqeiGLETIRENVSVVLQHPALFNDTVRANLTMG 465
Cdd:PLN03130  635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD------------ASVVIRGTVAYVPQVSWIFNATVRDNILFG 702

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  466 RERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNL-HQ 544
Cdd:PLN03130  703 SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDK 782

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489309308  545 ALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGGLYAKL 598
Cdd:PLN03130  783 CIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
369-583 1.76e-29

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 116.31  E-value: 1.76e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGY-GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG---STQQEIGLETIRENV 444
Cdd:COG2884    2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlSRLKRREIPYLRRRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 445 SVVLQ-HPALFNDTVRANLT-----MGRERSD--QACWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIAR 516
Cdd:COG2884   82 GVVFQdFRLLPDRTVYENVAlplrvTGKSRKEirRRVREVLDLVGLSDKAKALPHEL-----------SGGEQQRVAIAR 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 517 MVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIA-HRLSAVKQAD-RVLVFDGGHIAEDG 583
Cdd:COG2884  151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkRVLELEDGRLVRDE 219
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
369-590 1.93e-29

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 122.05  E-value: 1.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEIGLETIRE----NV 444
Cdd:COG1129    5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSPRDaqaaGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 445 SVVLQHPALFND-TVRANLTMGRERS-----DqacWQAL--EIAQLDATVKaLPLGLDSVVGRSGVrfsgGQRQRLAIAR 516
Cdd:COG1129   82 AIIHQELNLVPNlSVAENIFLGREPRrggliD---WRAMrrRARELLARLG-LDIDPDTPVGDLSV----AQQQLVEIAR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 517 MVLAEPKVVILDEATSALDAA-TEyNLHQALARFLS-GRTTLIIAHRLSAVKQ-ADRVLVF-DGGHIAE----DGDHQQL 588
Cdd:COG1129  154 ALSRDARVLILDEPTASLTEReVE-RLFRIIRRLKAqGVAIIYISHRLDEVFEiADRVTVLrDGRLVGTgpvaELTEDEL 232


                 ..
gi 489309308 589 IA 590
Cdd:COG1129  233 VR 234
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 369-591 2.22e-29

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 116.77  E-value: 2.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGST--------QQEIGLETI 440
Cdd:PRK11264   4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidtarslsQQKGLIRQL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 441 RENVSVVLQHPALF-NDTVRANLTMG-----RERSDQACWQALEiaqLDATVkalplGLDSVVGRSGVRFSGGQRQRLAI 514
Cdd:PRK11264  84 RQHVGFVFQNFNLFpHRTVLENIIEGpvivkGEPKEEATARARE---LLAKV-----GLAGKETSYPRRLSGGQQQRVAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 515 ARMVLAEPKVVILDEATSALD---AATEYNLHQALARflSGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDpelVGEVLNTIRQLAQ--EKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKALFA 233


                 .
gi 489309308 591 D 591
Cdd:PRK11264 234 D 234
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 123-606 4.35e-29

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: 123.48  E-value: 4.35e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   123 RIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGILMWMHWKLAL----LILLF 198
Cdd:TIGR01271  959 RLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIaaipVAVIF 1038

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   199 NPLVIYaTVQLGKRvkhLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFlgrlgqraQEVRDFAVNSQWKSDASSRA 278
Cdd:TIGR01271 1039 IMLRAY-FLRTSQQ---LKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYF--------ETLFHKALNLHTANWFLYLS 1106

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   279 SGLLFQFGIDI-----FRAAAMLTVLFSDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAAGGALTRINELL-ARADEP 352
Cdd:TIGR01271 1107 TLRWFQMRIDIifvffFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIdLPQEEP 1186

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   353 QYAGGADPFTGRETVGIE---------------VRGLNFGYGEE--LVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLL 415
Cdd:TIGR01271 1187 RPSGGGGKYQLSTVLVIEnphaqkcwpsggqmdVQGLTAKYTEAgrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL 1266

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   416 GLYTPQaGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRERSDQACWQALEIAQLDATVKALPLGLDS 495
Cdd:TIGR01271 1267 RLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDF 1345

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   496 VVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFD 575
Cdd:TIGR01271 1346 VLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIE 1425

                          490       500       510
                   ....*....|....*....|....*....|.
gi 489309308   576 GGHIAEDGDHQQLIADGGLYAKLYGHLQQVR 606
Cdd:TIGR01271 1426 GSSVKQYDSIQKLLNETSLFKQAMSAADRLK 1456
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 369-580 6.25e-29

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 112.52  E-value: 6.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqqeigletirenvsvvl 448
Cdd:cd03216    1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG------------------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 qHPALFNDTVRAnltmgrersdqacwQALEIA---QLdatvkalplgldsvvgrsgvrfSGGQRQRLAIARMVLAEPKVV 525
Cdd:cd03216   62 -KEVSFASPRDA--------------RRAGIAmvyQL----------------------SVGERQMVEIARALARNARLL 104

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 526 ILDEATSALDAATEYNLHQALARFLS-GRTTLIIAHRLSAVKQ-ADRVLVFDGGHIA 580
Cdd:cd03216  105 ILDEPTAALTPAEVERLFKVIRRLRAqGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 369-597 8.17e-29

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 122.83  E-value: 8.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  369 IEVRGLNFGYGEEL---VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLY-----------TPQAGSI----RFGGS 430
Cdd:PTZ00265 1166 IEIMDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfkNEHTNDMtneqDYQGD 1245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  431 TQQEIGLETIRE--------------------------------------NV-SVVLQHPALFNDTVRANLTMGRERSD- 470
Cdd:PTZ00265 1246 EEQNVGMKNVNEfsltkeggsgedstvfknsgkilldgvdicdynlkdlrNLfSIVSQEPMLFNMSIYENIKFGKEDATr 1325

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  471 QACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALA--R 548
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiK 1405

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489309308  549 FLSGRTTLIIAHRLSAVKQADRVLVFD-----GGHIAEDGDHQQLI-ADGGLYAK 597
Cdd:PTZ00265 1406 DKADKTIITIAHRIASIKRSDKIVVFNnpdrtGSFVQAHGTHEELLsVQDGVYKK 1460
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
369-591 1.27e-28

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 114.42  E-value: 1.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG--STQQEIGLETIRENVSV 446
Cdd:PRK09493   2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkVNDPKVDERLIRQEAGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPALFND-TVRANLTMGRER-----SDQACWQALEiaqLDATVkalplGLDSVVGRSGVRFSGGQRQRLAIARMVLA 520
Cdd:PRK09493  82 VFQQFYLFPHlTALENVMFGPLRvrgasKEEAEKQARE---LLAKV-----GLAERAHHYPSELSGGQQQRVAIARALAV 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 521 EPKVVILDEATSALDAATEY---NLHQALARflSGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHevlKVMQDLAE--EGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 370-579 1.62e-28

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: 112.74  E-value: 1.62e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 370 EVRGLNFGYGEE-LVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGStqqEIGLETIRENVSVVL 448
Cdd:cd03226    1 RIENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERRKSIGYVM 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHP--ALFNDTVRANLTMGRERSDQACWQALEIAQ---LDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIARMVLAEPK 523
Cdd:cd03226   78 QDVdyQLFTDSVREELLLGLKELDAGNEQAETVLKdldLYALKERHPLSL-----------SGGQKQRLAIAAALLSGKD 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489309308 524 VVILDEATSALDAateYNLHQALARFLS----GRTTLIIAHRLS-AVKQADRVLVFDGGHI 579
Cdd:cd03226  147 LLIFDEPTSGLDY---KNMERVGELIRElaaqGKAVIVITHDYEfLAKVCDRVLLLANGAI 204
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 369-588 3.24e-28

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: 113.05  E-value: 3.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGE-ELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG---STQQEIGLETIRENV 444
Cdd:cd03256    1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdiNKLKGKALRQLRRQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 445 SVVLQHPALFND-TVRANLTMGR--ERSD-QACWQALEIAQLDATVKALP-LGLDSVVGRSGVRFSGGQRQRLAIARMVL 519
Cdd:cd03256   81 GMIFQQFNLIERlSVLENVLSGRlgRRSTwRSLFGLFPKEEKQRALAALErVGLLDKAYQRADQLSGGQQQRVAIARALM 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 520 AEPKVVILDEATSALDAATEYNLHQALARFLS--GRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQL 588
Cdd:cd03256  161 QQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDlAREYADRIVGLKDGRIVFDGPPAEL 232
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
369-590 3.25e-28

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 112.93  E-value: 3.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVldQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGS--TQQEIGletiRENVSV 446
Cdd:COG3840    2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdlTALPPA----ERPVSM 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPALFND-TVRANLTMGR---------ERSDQAcwQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIAR 516
Cdd:COG3840   76 LFQENNLFPHlTVAQNIGLGLrpglkltaeQRAQVE--QALERVGLAGLLDRLPGQL-----------SGGQRQRVALAR 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 517 MVLAEPKVVILDEATSALDAATEYNLHQaLARFLS---GRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:COG3840  143 CLVRKRPILLLDEPFSALDPALRQEMLD-LVDELCrerGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLD 219
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
369-583 3.48e-28

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 116.59  E-value: 3.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstQQEIGLETIRENVSVVL 448
Cdd:PRK09452  15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG--QDITHVPAENRHVNTVF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALF-NDTVRANLTMG-----------RERsdqaCWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIAR 516
Cdd:PRK09452  93 QSYALFpHMTVFENVAFGlrmqktpaaeiTPR----VMEALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIAR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 517 MVLAEPKVVILDEATSALDaateYNLHQ-------ALARFLsGRTTLIIAH-RLSAVKQADRVLVFDGGHIAEDG 583
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALD----YKLRKqmqnelkALQRKL-GITFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 321-591 3.96e-28

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: 118.63  E-value: 3.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 321 PVEQLL-NLQYAYyaaggalTRinELLAraDEPQyaGGADPFTGRETVGIEVRGLN---------FGYGEELV--LDQLN 388
Cdd:COG4172  240 PTAELFaAPQHPY-------TR--KLLA--AEPR--GDPRPVPPDAPPLLEARDLKvwfpikrglFRRTVGHVkaVDGVS 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 389 LNIAPGEKVAIVGASGGGKSTLVQLLLGLyTPQAGSIRFGG---STQQEIGLETIRENVSVVLQHP-ALFND--TVRANL 462
Cdd:COG4172  307 LTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGqdlDGLSRRALRPLRRRMQVVFQDPfGSLSPrmTVGQII 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 463 TMG----------RERSDQACwQALEIAQLDATVKAlplgldsvvgrsgvR----FSGGQRQRLAIAR-MVLaEPKVVIL 527
Cdd:COG4172  386 AEGlrvhgpglsaAERRARVA-EALEEVGLDPAARH--------------RypheFSGGQRQRIAIARaLIL-EPKLLVL 449

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 528 DEATSALDAATeynlhQA----LARFLSGR---TTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:COG4172  450 DEPTSALDVSV-----QAqildLLRDLQREhglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
369-588 5.14e-28

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 115.57  E-value: 5.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEIGLETIRE-NVSVV 447
Cdd:PRK10851   3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG---TDVSRLHARDrKVGFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALFND-TVRANLTMG------RERSDQA-----CWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIA 515
Cdd:PRK10851  80 FQHYALFRHmTVFDNIAFGltvlprRERPNAAaikakVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 516 RMVLAEPKVVILDEATSALDAATEY-------NLHQALaRFlsgrTTLIIAH-RLSAVKQADRVLVFDGGHIAEDGDHQQ 587
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKelrrwlrQLHEEL-KF----TSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQ 223


                 .
gi 489309308 588 L 588
Cdd:PRK10851 224 V 224
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
 101-342 5.29e-28

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: 113.68  E-value: 5.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 101 GALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGT 180
Cdd:cd18551   48 LQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 181 SGILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQE 260
Cdd:cd18551  128 VVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAER 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 261 VRDFAVNSQWKSDASSRASGLLFQfgidifraAAMLTVLF--------SDLSIGQMLAVFSYLWFMISPVEQLLNLQYAY 332
Cdd:cd18551  208 LYRAGLKAAKIEALIGPLMGLAVQ--------LALLVVLGvggarvasGALTVGTLVAFLLYLFQLITPLSQLSSFFTQL 279

                        250
                 ....*....|
gi 489309308 333 YAAGGALTRI 342
Cdd:cd18551  280 QKALGALERI 289
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 373-588 1.21e-27

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


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 112.21  E-value: 1.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  373 GLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEI---GLETIRENVSVVLQ 449
Cdd:TIGR02769  16 GLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  450 H-PALFNDTVRANLTMGR-----ERSDQACWQALEIAQLDAtvkalpLGLDS-VVGRSGVRFSGGQRQRLAIARMVLAEP 522
Cdd:TIGR02769  96 DsPSAVNPRMTVRQIIGEplrhlTSLDESEQKARIAELLDM------VGLRSeDADKLPRQLSGGQLQRINIARALAVKP 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308  523 KVVILDEATSALDAATEYNLHQALARF--LSGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQL 588
Cdd:TIGR02769 170 KLIVLDEAVSNLDMVLQAVILELLRKLqqAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQL 238
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 369-590 1.23e-27

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: 111.62  E-value: 1.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGE-ELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVV 447
Cdd:cd03295    1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALF-NDTVRANLTM-------GRERSDQACWQALEIAQLDatvkalPLGLdsvVGRSGVRFSGGQRQRLAIARMVL 519
Cdd:cd03295   81 IQQIGLFpHMTVEENIALvpkllkwPKEKIRERADELLALVGLD------PAEF---ADRYPHELSGGQQQRVGVARALA 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308 520 AEPKVVILDEATSALDAATEYNLHQALARF--LSGRTTLIIAHRL-SAVKQADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:cd03295  152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 369-601 3.14e-27

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 110.63  E-value: 3.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG------STQQeigLETIRe 442
Cdd:PRK13548   3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwSPAE---LARRR- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 443 nvSVVLQHPAL-FNDTVRANLTMGRE--RSDQACWQALEIAQLDATvkalplGLDSVVGRSGVRFSGGQRQRLAIARmVL 519
Cdd:PRK13548  79 --AVLPQHSSLsFPFTVEEVVAMGRAphGLSRAEDDALVAAALAQV------DLAHLAGRDYPQLSGGEQQRVQLAR-VL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 520 A-------EPKVVILDEATSALDAAteynlHQ----ALARFL---SGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGD 584
Cdd:PRK13548 150 AqlwepdgPPRWLLLDEPTSALDLA-----HQhhvlRLARQLaheRGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224

                        250
                 ....*....|....*..
gi 489309308 585 HQQLIADGGLyAKLYGH 601
Cdd:PRK13548 225 PAEVLTPETL-RRVYGA 240
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 369-577 3.22e-27

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: 109.52  E-value: 3.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLN--FGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG-STQQEIglETIRENVS 445
Cdd:cd03263    1 LQIRNLTktYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGySIRTDR--KAARQSLG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 446 VVLQHPALFND-TVRANLT-MGRERSdqacwqaLEIAQLDATVKAL--PLGLDSVVGRSGVRFSGGQRQRLAIARMVLAE 521
Cdd:cd03263   79 YCPQFDALFDElTVREHLRfYARLKG-------LPKSEIKEEVELLlrVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 522 PKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQ-ADRVLVFDGG 577
Cdd:cd03263  152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDG 208
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
 103-322 3.28e-27

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: 111.20  E-value: 3.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  103 LVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSG 182
Cdd:pfam00664  55 FILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGII 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  183 ILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLgrlgQRAQEVR 262
Cdd:pfam00664 135 VMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYEL----EKYDKAL 210

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308  263 DFAVNSQWKSDASSRASGLLFQFGIDIFRAAAML----TVLFSDLSIGQMLAVFSYLWFMISPV 322
Cdd:pfam00664 211 EEALKAGIKKAVANGLSFGITQFIGYLSYALALWfgayLVISGELSVGDLVAFLSLFAQLFGPL 274
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 369-588 3.54e-27

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 110.51  E-value: 3.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLY--TPQA---GSIRFGGS--TQQEIGLETIR 441
Cdd:COG1117   12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGArveGEILLDGEdiYDPDVDVVELR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 442 ENVSVVLQHPALFNDTVRANLTMG--------RERSDQACWQALEIAQLDATVKAlplGLDsvvgRSGVRFSGGQRQRLA 513
Cdd:COG1117   92 RRVGMVFQKPNPFPKSIYDNVAYGlrlhgiksKSELDEIVEESLRKAALWDEVKD---RLK----KSALGLSGGQQQRLC 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 514 IARmVLA-EPKVVILDEATSALD-AAT---EynlhqALARFLSGRTTLII-------AHRLSavkqaDRVLVFDGGHIAE 581
Cdd:COG1117  165 IAR-ALAvEPEVLLMDEPTSALDpISTakiE-----ELILELKKDYTIVIvthnmqqAARVS-----DYTAFFYLGELVE 233


                 ....*..
gi 489309308 582 DGDHQQL 588
Cdd:COG1117  234 FGPTEQI 240
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 369-584 3.91e-27

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 115.55  E-value: 3.91e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQ-----QEigLETIREN 443
Cdd:COG0488  316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKigyfdQH--QEELDPD 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 444 VSVVlqhpalfnDTVRANLTMGRERsdqacwqalEIAQLdatvkalpLG--------LDSVVGrsgvRFSGGQRQRLAIA 515
Cdd:COG0488  394 KTVL--------DELRDGAPGGTEQ---------EVRGY--------LGrflfsgddAFKPVG----VLSGGEKARLALA 444

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308 516 RMVLAEPKVVILDEATSALDAATEYNLHQALARFlSGrTTLIIAH-R--LSAVkqADRVLVFDGGHIAE-DGD 584
Cdd:COG0488  445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGG 513
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 369-583 4.41e-27

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 112.59  E-value: 4.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLN--FGYGEELV--LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEI------GLE 438
Cdd:PRK11153   2 IELKNISkvFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDG---QDLtalsekELR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 439 TIRENVSVVLQHpalFN----DTVRANLTMgrersdqacwqALEIAQLD-ATVKALPLGLDSVVGRSGVR------FSGG 507
Cdd:PRK11153  79 KARRQIGMIFQH---FNllssRTVFDNVAL-----------PLELAGTPkAEIKARVTELLELVGLSDKAdrypaqLSGG 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 508 QRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALA---RFLsGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDG 583
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKdinREL-GLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 369-572 5.88e-27

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 109.03  E-value: 5.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVL 448
Cdd:PRK10247   8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALFNDTVRANLTMGrersdqacWQALEIA-QLDATVKALP-LGL-DSVVGRSGVRFSGGQRQRLAIARMVLAEPKVV 525
Cdd:PRK10247  88 QTPTLFGDTVYDNLIFP--------WQIRNQQpDPAIFLDDLErFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489309308 526 ILDEATSALDAATEYNLHQALARFLS--GRTTLIIAHRLSAVKQADRVL 572
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVReqNIAVLWVTHDKDEINHADKVI 208
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 369-600 6.42e-27

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 109.76  E-value: 6.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGY-GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIG---LETIRENV 444
Cdd:COG3638    3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 445 SVVLQHPALFND-TVRANLTMGR--------------ERSDQAcwQALEIaqLDAtvkalpLGLDSVVGRSGVRFSGGQR 509
Cdd:COG3638   83 GMIFQQFNLVPRlSVLTNVLAGRlgrtstwrsllglfPPEDRE--RALEA--LER------VGLADKAYQRADQLSGGQQ 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 510 QRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLS--GRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQ 586
Cdd:COG3638  153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDlARRYADRIIGLRDGRVVFDGPPA 232

                        250
                 ....*....|....
gi 489309308 587 QLIADggLYAKLYG 600
Cdd:COG3638  233 ELTDA--VLREIYG 244
cbiO PRK13650
energy-coupling factor transporter ATPase;
369-593 6.43e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 110.59  E-value: 6.43e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYG---EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVS 445
Cdd:PRK13650   5 IEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 446 VVLQHP--ALFNDTVRANLTMGRERsdqacwQALEIAQLDATVK-ALPL-GLDSVVGRSGVRFSGGQRQRLAIARMVLAE 521
Cdd:PRK13650  85 MVFQNPdnQFVGATVEDDVAFGLEN------KGIPHEEMKERVNeALELvGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308 522 PKVVILDEATSALDAATEYNLHQALA--RFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGG 593
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKgiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 309-598 1.17e-26

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: 115.81  E-value: 1.17e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   309 LAVFSYLWFmisPVEQLLNLQYAYYAAGGALTRINELLARAD-EPQyAGGADPFTGRETVGIEVRGLNFGYGEEL--VLD 385
Cdd:TIGR00957  580 LALFNILRF---PLNILPMVISSIVQASVSLKRLRIFLSHEElEPD-SIERRTIKPGEGNSITVHNATFTWARDLppTLN 655

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   386 QLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGStqqeigletirenVSVVLQHPALFNDTVRANLTMG 465
Cdd:TIGR00957  656 GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFG 722

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   466 RERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQA 545
Cdd:TIGR00957  723 KALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308   546 L---ARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGGLYAKL 598
Cdd:TIGR00957  803 VigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
368-583 1.22e-26

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 111.66  E-value: 1.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 368 GIEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIglETIRENVSVV 447
Cdd:PRK11000   3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV--PPAERGVGMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALF-NDTVRANLTMG-------RERSDQACWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIARMVL 519
Cdd:PRK11000  81 FQSYALYpHLSVAENMSFGlklagakKEEINQRVNQVAEVLQLAHLLDRKPKAL-----------SGGQRQRVAIGRTLV 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 520 AEPKVVILDEATSALDAATEYN-------LHQALarflsGRTTLIIAH-RLSAVKQADRVLVFDGGHIAEDG 583
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQmrieisrLHKRL-----GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 371-582 1.40e-26

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 109.00  E-value: 1.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 371 VRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTqqeigLETIRENVSVVLQH 450
Cdd:PRK11247  15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP-----LAEAREDTRLMFQD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 451 PALFN-DTVRANLTMG-RERSDQACWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIARMVLAEPKVVILD 528
Cdd:PRK11247  90 ARLLPwKKVIDNVGLGlKGQWRDAALQALAAVGLADRANEWPAAL-----------SGGQKQRVALARALIHRPGLLLLD 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 529 EATSALDAATEYNLHQALARFLS--GRTTLIIAHRLS-AVKQADRVLVFDGGHIAED 582
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKIGLD 215
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
377-574 1.57e-26

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 106.93  E-value: 1.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 377 GYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQqeigletirenVSVVLQH---PAL 453
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGAR-----------VAYVPQRsevPDS 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 454 FNDTVRANLTMGRERsDQACWQALEIAQLDATVKALP-LGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATS 532
Cdd:NF040873  70 LPLTVRDLVAMGRWA-RRGLWRRLTRDDRAAVDDALErVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489309308 533 ALDAATEYNLHQALARFLS-GRTTLIIAHRLSAVKQADRVLVF 574
Cdd:NF040873 149 GLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 387-594 2.62e-26

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


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 110.59  E-value: 2.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  387 LNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQE----IGLETIRENVSVVLQHPALFND-TVRAN 461
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHlSVRGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  462 LTMGRERSDQACWQALeiaqlDATVKALpLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYN 541
Cdd:TIGR02142  96 LRYGMKRARPSERRIS-----FERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308  542 LHQALARfLSGRT---TLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIADGGL 594
Cdd:TIGR02142 170 ILPYLER-LHAEFgipILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDL 225
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
386-590 2.76e-26

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 107.36  E-value: 2.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 386 QLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIglETIRENVSVVLQHPALFND-TVRANLTM 464
Cdd:PRK10771  17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT--PPSRRPVSMLFQENNLFSHlTVAQNIGL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 465 G-----RERSDQACwQALEIAQLdatvkalpLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATE 539
Cdd:PRK10771  95 GlnpglKLNAAQRE-KLHAIARQ--------MGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489309308 540 YNLHQALARFLSGR--TTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
 104-342 7.55e-26

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: 107.89  E-value: 7.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGI 183
Cdd:cd18552   54 LASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 184 LMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVRD 263
Cdd:cd18552  134 LFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRR 213

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 264 FAVNSQWKSDASSRASGLLFQFGIDIFRAAAMLTVLFSDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAAGGALTRI 342
Cdd:cd18552  214 LSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
 104-325 1.26e-25

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: 107.13  E-value: 1.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGI 183
Cdd:cd18542   54 VFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALII 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 184 LMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVRD 263
Cdd:cd18542  134 MFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRD 213

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 264 favnsqwKSDASSRASGLLFQFGIDIFRAAAMLTVLF-------SDLSIGQMLAVFSYLWFMISPVEQL 325
Cdd:cd18542  214 -------LNIKLAKLLAKYWPLMDFLSGLQIVLVLWVggylvinGEITLGELVAFISYLWMLIWPVRQL 275
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 380-592 1.46e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 107.03  E-value: 1.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 380 EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG----STQQEIGLETIRENVSVVLQHP--AL 453
Cdd:PRK13634  19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitAGKKNKKLKPLRKKVGIVFQFPehQL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 454 FNDTVRANLTMGRersdqacwQALEIAQLDATVKA---LPL-GLD-SVVGRSGVRFSGGQRQRLAIARmVLA-EPKVVIL 527
Cdd:PRK13634  99 FEETVEKDICFGP--------MNFGVSEEDAKQKAremIELvGLPeELLARSPFELSGGQMRRVAIAG-VLAmEPEVLVL 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308 528 DEATSALDAATE-------YNLHQAlarflSGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIADG 592
Cdd:PRK13634 170 DEPTAGLDPKGRkemmemfYKLHKE-----KGLTTVLVTHSMEdAARYADQIVVMHKGTVFLQGTPREIFADP 237
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 369-606 1.48e-25

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: 106.48  E-value: 1.48e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGE--ELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQaGSIRFGGSTQQEIGLETIRENVSV 446
Cdd:cd03289    3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPALFNDTVRANLTMGRERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVI 526
Cdd:cd03289   82 IPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 527 LDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGGLYAKLYGHLQQVR 606
Cdd:cd03289  162 LDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRLK 241
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 370-591 1.50e-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: 1.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 370 EVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEI-GLET---IRENVS 445
Cdd:COG0410    5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG---EDItGLPPhriARLGIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 446 VVLQHPALFND-TVRANLTMG-RERSDQAcwqalEIAQLDATVKAL-PLgLDSVVGRSGVRFSGGQRQRLAIARMVLAEP 522
Cdd:COG0410   82 YVPEGRRIFPSlTVEENLLLGaYARRDRA-----EVRADLERVYELfPR-LKERRRQRAGTLSGGEQQMLAIGRALMSRP 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 523 KVVILDEATSALDAATEYNLHQALARfL--SGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:COG0410  156 KLLLLDEPSLGLAPLIVEEIFEIIRR-LnrEGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLAD 226
cbiO PRK13644
energy-coupling factor transporter ATPase;
384-594 1.71e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 106.22  E-value: 1.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG-STQQEIGLETIRENVSVVLQHP--ALFNDTVRA 460
Cdd:PRK13644  18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKLQGIRKLVGIVFQNPetQFVGRTVEE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 461 NLTMGRErsdQACWQALEIAQLDATVKAlPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEY 540
Cdd:PRK13644  98 DLAFGPE---NLCLPPIEIRKRVDRALA-EIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 541 NLHQALARF-LSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADGGL 594
Cdd:PRK13644 174 AVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSL 228
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 369-574 1.72e-25

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 112.43  E-value: 1.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  369 IEVRGLNFGYGE----ELVLDqLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQ-QEIGLETIREN 443
Cdd:PTZ00265  383 IQFKNVRFHYDTrkdvEIYKD-LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNlKDINLKWWRSK 461

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  444 VSVVLQHPALFNDTVRANLTMG---------------------------RERSDQACWQALE--IAQLDAT--------- 485
Cdd:PTZ00265  462 IGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkRNSCRAKCAGDLNdmSNTTDSNeliemrkny 541

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  486 --------------------VKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYnLHQA 545
Cdd:PTZ00265  542 qtikdsevvdvskkvlihdfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY-LVQK 620

                         250       260       270
                  ....*....|....*....|....*....|..
gi 489309308  546 LARFLSG---RTTLIIAHRLSAVKQADRVLVF 574
Cdd:PTZ00265  621 TINNLKGnenRITIIIAHRLSTIRYANTIFVL 652
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
 102-342 3.59e-25

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: 105.65  E-value: 3.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 102 ALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTS 181
Cdd:cd18546   52 GWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIA 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 182 GILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEV 261
Cdd:cd18546  132 VVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDY 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 262 RDFAVNSQwksdassRASGLLFQFgIDIFRAAAMLTVLF--------SDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYY 333
Cdd:cd18546  212 RDARLRAQ-------RLVAIYFPG-VELLGNLATAAVLLvgawrvaaGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQ 283


                 ....*....
gi 489309308 334 AAGGALTRI 342
Cdd:cd18546  284 QARAALEKI 292
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
373-582 5.94e-25

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 104.38  E-value: 5.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 373 GLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG---STQQEIGLETIRENVSVVLQ 449
Cdd:PRK10419  17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplAKLNRAQRKAFRRDIQMVFQ 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 450 H-PALFN--DTVRANLtmgRE--RSDQACWQALEIAQLDATVKALPLGlDSVVGRSGVRFSGGQRQRLAIARMVLAEPKV 524
Cdd:PRK10419  97 DsISAVNprKTVREII---REplRHLLSLDKAERLARASEMLRAVDLD-DSVLDKRPPQLSGGQLQRVCLARALAVEPKL 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489309308 525 VILDEATSALDAATEYNLHQALARFL--SGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAED 582
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQqqFGTACLFITHDLRLVERfCQRVMVMDNGQIVET 233
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 370-592 6.41e-25

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


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 103.97  E-value: 6.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 370 EVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEI-GL---ETIRENVS 445
Cdd:COG0411    6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG---RDItGLpphRIARLGIA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 446 VVLQHPALFND-TVRANLTMGRERSDQACWQAL---------EIAQLDATVKAL--PLGLDSVVGRSGVRFSGGQRQRLA 513
Cdd:COG0411   83 RTFQNPRLFPElTVLENVLVAAHARLGRGLLAAllrlprarrEEREARERAEELleRVGLADRADEPAGNLSYGQQRRLE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 514 IARMVLAEPKVVILDEATSALDAAteynLHQALARFL------SGRTTLIIAHRLSAVKQ-ADRVLVFDGGhiaedgdhq 586
Cdd:COG0411  163 IARALATEPKLLLLDEPAAGLNPE----ETEELAELIrrlrdeRGITILLIEHDMDLVMGlADRIVVLDFG--------- 229


                 ....*.
gi 489309308 587 QLIADG 592
Cdd:COG0411  230 RVIAEG 235
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 369-583 6.65e-25

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: 102.66  E-value: 6.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGeKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGlETIRENVSVVL 448
Cdd:cd03264    1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPalfndTVRANLTmGRERSDQACW-----QALEIAQLDATVKALplGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPK 523
Cdd:cd03264   79 QEF-----GVYPNFT-VREFLDYIAWlkgipSKEVKARVDEVLELV--NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489309308 524 VVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDG 583
Cdd:cd03264  151 ILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 387-583 6.81e-25

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: 102.96  E-value: 6.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 387 LNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstQQEIGLETIRENVSVVLQHPALFND-TVRANLTMG 465
Cdd:cd03298   17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTAAPPADRPVSMLFQENNLFAHlTVEQNVGLG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 466 RERSDQacwqaLEIAQLDATVKALP-LGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQ 544
Cdd:cd03298   95 LSPGLK-----LTAEDRQAIEVALArVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489309308 545 ALA--RFLSGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDG 583
Cdd:cd03298  170 LVLdlHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 369-577 8.46e-25

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: 102.79  E-value: 8.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEEL-VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETI----REN 443
Cdd:cd03290    1 VQVTNGYFSWGSGLaTLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 444 VSVVLQHPALFNDTVRANLTMGRERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPK 523
Cdd:cd03290   81 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 524 VVILDEATSALDAATEYNLHQA-LARFLSG--RTTLIIAHRLSAVKQADRVLVFDGG 577
Cdd:cd03290  161 IVFLDDPFSALDIHLSDHLMQEgILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
369-590 8.88e-25

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 104.89  E-value: 8.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETiRENVSVVL 448
Cdd:PRK13537   8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVVP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALFND-TVRANLTM-GRE--RSDQACWQA----LEIAQL----DATVKALplgldsvvgrsgvrfSGGQRQRLAIAR 516
Cdd:PRK13537  87 QFDNLDPDfTVRENLLVfGRYfgLSAAAARALvpplLEFAKLenkaDAKVGEL---------------SGGMKRRLTLAR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308 517 MVLAEPKVVILDEATSALDAATEYNLHQALARFL-SGRTTLIIAHRL-SAVKQADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMeEAERLCDRLCVIEEGRKIAEGAPHALIE 227
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 386-584 9.52e-25

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


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 102.63  E-value: 9.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  386 QLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstQQEIGLETIRENVSVVLQHPALFND-TVRANLTM 464
Cdd:TIGR01277  16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND--QSHTGLAPYQRPVSMLFQENNLFAHlTVRQNIGL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  465 GRERSDQAcwQALEIAQLDATvkALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQ 544
Cdd:TIGR01277  94 GLHPGLKL--NAEQQEKVVDA--AQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 489309308  545 ALARFLSGR--TTLIIAHRLS-AVKQADRVLVFDGGHIAEDGD 584
Cdd:TIGR01277 170 LVKQLCSERqrTLLMVTHHLSdARAIASQIAVVSQGKIKVVSD 212
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 102-328 9.83e-25

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: 104.51  E-value: 9.83e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 102 ALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTS 181
Cdd:cd18563   56 SALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIG 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 182 GILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAgnrqgFflgrlGQRAQEV 261
Cdd:cd18563  136 VVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKA-----F-----GQEKREI 205

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 262 RDFAVNSQWKSDASSRAS----------GLLFQFGIDIFRAAAMLTVLFSDLSIGQMLAVFSYLWFMISPVEQLLNL 328
Cdd:cd18563  206 KRFDEANQELLDANIRAEklwatffpllTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRL 282
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 386-591 1.35e-24

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 105.57  E-value: 1.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 386 QLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG----STQQEIGLETIRENVSVVLQHPALFND-TVRA 460
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqDSARGIFLPPHRRRIGYVFQEARLFPHlSVRG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 461 NLTMGRERsdqaCWQALEIAQLDATVKALplGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEY 540
Cdd:COG4148   97 NLLYGRKR----APRAERRISFDEVVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 541 NLHQALARfLSGRT---TLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:COG4148  171 EILPYLER-LRDELdipILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 369-604 6.26e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 101.74  E-value: 6.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGY--GEElVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSV 446
Cdd:PRK13647   5 IEVEDLHFRYkdGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHP--ALFNDTV-------RANLTMGRERSDQACWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIARM 517
Cdd:PRK13647  84 VFQDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 518 VLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIA-HRLS-AVKQADRVLVFDGGHIAEDGD-----HQQLIA 590
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDkslltDEDIVE 232

                        250
                 ....*....|....*...
gi 489309308 591 DGGL----YAKLYGHLQQ 604
Cdd:PRK13647 233 QAGLrlplVAQIFEDLPE 250
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 385-591 1.39e-23

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 102.09  E-value: 1.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 385 DQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGST---QQEIGLETIRENVSVVLQHP-ALFNdtvrA 460
Cdd:PRK15079  38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDllgMKDDEWRAVRSDIQMIFQDPlASLN----P 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 461 NLTMGRERSD--QACWQALEIAQLDATVKALPLG---LDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALD 535
Cdd:PRK15079 114 RMTIGEIIAEplRTYHPKLSRQEVKDRVKAMMLKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 536 A---ATEYNLHQALARFLsGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:PRK15079 194 VsiqAQVVNLLQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 399-591 1.40e-23

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


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 101.80  E-value: 1.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  399 IVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLEtiRENVSVVLQHPALF-NDTVRANLTMG-------RERSD 470
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFpHMTVEENVAFGlkmrkvpRAEIK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  471 QACWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFL 550
Cdd:TIGR01187  79 PRVLEALRLVQLEEFADRKPHQL-----------SGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 489309308  551 S--GRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:TIGR01187 148 EqlGITFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 369-592 1.78e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 100.21  E-value: 1.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGY--GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSV 446
Cdd:PRK13648   8 IVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHP--ALFNDTVRANLTMGRE-----------RSDQACWQALEIAQLDATVKALplgldsvvgrsgvrfSGGQRQRLA 513
Cdd:PRK13648  88 VFQNPdnQFVGSIVKYDVAFGLEnhavpydemhrRVSEALKQVDMLERADYEPNAL---------------SGGQKQRVA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 514 IARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIA--HRLSAVKQADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232


                 .
gi 489309308 592 G 592
Cdd:PRK13648 233 A 233
cbiO PRK13641
energy-coupling factor transporter ATPase;
369-591 2.11e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 100.67  E-value: 2.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYG-----EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG----STQQEIGLET 439
Cdd:PRK13641   3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 440 IRENVSVVLQHP--ALFNDTVRANLTMGRER----SDQACWQALEIAQldatvkalPLGL-DSVVGRSGVRFSGGQRQRL 512
Cdd:PRK13641  83 LRKKVSLVFQFPeaQLFENTVLKDVEFGPKNfgfsEDEAKEKALKWLK--------KVGLsEDLISKSPFELSGGQMRRV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 513 AIARMVLAEPKVVILDEATSALDAATEYNLHQALARF-LSGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFS 234


                 .
gi 489309308 591 D 591
Cdd:PRK13641 235 D 235
cbiO PRK13642
energy-coupling factor transporter ATPase;
369-590 2.31e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 100.17  E-value: 2.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLN---LNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVS 445
Cdd:PRK13642   5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 446 VVLQHP--ALFNDTVRANLTMGRErsDQACWQALEIAQLDATVKALPLgLDSVVgRSGVRFSGGQRQRLAIARMVLAEPK 523
Cdd:PRK13642  85 MVFQNPdnQFVGATVEDDVAFGME--NQGIPREEMIKRVDEALLAVNM-LDFKT-REPARLSGGQKQRVAVAGIIALRPE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 524 VVILDEATSALDAATEYNLHQALARFLSGR--TTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
PTZ00243 PTZ00243
ABC transporter; Provisional
 383-603 2.83e-23

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 105.25  E-value: 2.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  383 VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGStqqeigletirenVSVVLQHPALFNDTVRANL 462
Cdd:PTZ00243  675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS-------------IAYVPQQAWIMNATVRGNI 741

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  463 TMGRERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAAT-EYN 541
Cdd:PTZ00243  742 LFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERV 821

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308  542 LHQALARFLSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDGDHQQLIADgGLYAKLYGHLQ 603
Cdd:PTZ00243  822 VEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRT-SLYATLAAELK 882
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 104-342 2.86e-23

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: 100.66  E-value: 2.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGI 183
Cdd:cd18564   69 LASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGV 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 184 LMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAgnrqgfflgrLGQRAQEVRD 263
Cdd:cd18564  149 MFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQA----------FGREEHEERR 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 264 FAVNSQWKSDASSRASGLLFQFG--IDIFRAAAMLTVLF--------SDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYY 333
Cdd:cd18564  219 FARENRKSLRAGLRAARLQALLSpvVDVLVAVGTALVLWfgawlvlaGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIA 298


                 ....*....
gi 489309308 334 AAGGALTRI 342
Cdd:cd18564  299 KASASAERV 307
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 370-592 3.96e-23

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


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 98.37  E-value: 3.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  370 EVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEI-GLET---IRENVS 445
Cdd:TIGR03410   2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDG---EDItKLPPherARAGIA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  446 VVLQHPALFND-TVRANLTMG---RERSDQacwqaleiaQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAE 521
Cdd:TIGR03410  79 YVPQGREIFPRlTVEENLLTGlaaLPRRSR---------KIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTR 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308  522 PKVVILDEATSALDAATEYNLHQALARFLS--GRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIADG 592
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAegGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDEDK 223
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 382-576 4.10e-23

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: 96.07  E-value: 4.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 382 LVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqqeigletiRENVSVVLQHPALFNDTVRan 461
Cdd:cd03223   15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFLPQRPYLPLGTLR-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 462 ltmgrersDQAC--WQAleiaqldatvkalplgldsvvgrsgvRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATE 539
Cdd:cd03223   82 --------EQLIypWDD--------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489309308 540 YNLHQALARFLsgrTTLI-IAHRLSAVKQADRVLVFDG 576
Cdd:cd03223  128 DRLYQLLKELG---ITVIsVGHRPSLWKFHDRVLDLDG 162
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
369-581 5.04e-23

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 98.78  E-value: 5.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYG----EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETirenv 444
Cdd:COG4525    4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR----- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 445 SVVLQHPALFN-DTVRANLTMG--------RERSDQAcwqaLEIAQLdatvkalpLGLDSVVGRSGVRFSGGQRQRLAIA 515
Cdd:COG4525   79 GVVFQKDALLPwLNVLDNVAFGlrlrgvpkAERRARA----EELLAL--------VGLADFARRRIWQLSGGMRQRVGIA 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489309308 516 RMVLAEPKVVILDEATSALDAATEYNLHQALARF--LSGRTTLIIAHRL-SAVKQADRVLVFDG--GHIAE 581
Cdd:COG4525  147 RALAADPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITHSVeEALFLATRLVVMSPgpGRIVE 217
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 369-591 5.63e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 99.78  E-value: 5.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEEL-----VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRF--------GGSTQQEI 435
Cdd:PRK13651   3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkKKTKEKEK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 436 GLET----------------IRENVSVVLQHP--ALFNDTVRAN-----LTMGRERSdqacwQALEIAQldatvKALPL- 491
Cdd:PRK13651  83 VLEKlviqktrfkkikkikeIRRRVGVVFQFAeyQLFEQTIEKDiifgpVSMGVSKE-----EAKKRAA-----KYIELv 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 492 GLD-SVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALD-AATE------YNLHQalarflSGRTTLIIAHRL- 562
Cdd:PRK13651 153 GLDeSYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKeileifDNLNK------QGKTIILVTHDLd 226

                        250       260
                 ....*....|....*....|....*....
gi 489309308 563 SAVKQADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:PRK13651 227 NVLEWTKRTIFFKDGKIIKDGDTYDILSD 255
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 370-584 6.46e-23

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 97.83  E-value: 6.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 370 EVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGL--YTPQAGSIRFGGstqQEI-GLET---IREN 443
Cdd:COG0396    2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDG---EDIlELSPderARAG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 444 VSVVLQHPALF-----NDTVRANLTMGRErsdqacwQALEIAQLDATVKAL--PLGLD-SVVGRS-GVRFSGGQRQRLAI 514
Cdd:COG0396   79 IFLAFQYPVEIpgvsvSNFLRTALNARRG-------EELSAREFLKLLKEKmkELGLDeDFLDRYvNEGFSGGEKKRNEI 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308 515 ARMVLAEPKVVILDEATSALDAATEYNLHQALARFLS-GRTTLIIAH--RLSAVKQADRVLVFDGGHIAEDGD 584
Cdd:COG0396  152 LQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 369-597 7.12e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 99.92  E-value: 7.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEE-----LVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFG--------------- 428
Cdd:PRK13631  22 LRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnhelit 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 429 GSTQQEI-GLETIRENVSVVLQHP--ALFNDTVRANLTMGRersdqacwQALEIAQLDATVKA----LPLGLD-SVVGRS 500
Cdd:PRK13631 102 NPYSKKIkNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGP--------VALGVKKSEAKKLAkfylNKMGLDdSYLERS 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 501 GVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQ-ALARFLSGRTTLIIAHRLSAVKQ-ADRVLVFDGGH 578
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQlILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGK 253

                        250
                 ....*....|....*....
gi 489309308 579 IAEDGDHQQLIADGGLYAK 597
Cdd:PRK13631 254 ILKTGTPYEIFTDQHIINS 272
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 384-583 1.38e-22

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


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 96.77  E-value: 1.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIrenvsVVLQHPALFN-DTVRANL 462
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  463 TMGRERSDQACWQALEIAQLDATVKALplGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNL 542
Cdd:TIGR01184  76 ALAVDRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 489309308  543 HQALARFL--SGRTTLIIAHRL-SAVKQADRVLVFDGGHIAEDG 583
Cdd:TIGR01184 154 QEELMQIWeeHRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
cbiO PRK13640
energy-coupling factor transporter ATPase;
369-583 1.68e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 97.95  E-value: 1.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGY--GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGS---IRFGGSTQQEIGLETIREN 443
Cdd:PRK13640   6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 444 VSVVLQHP------ALFNDTVR---ANLTMGRERSDQACWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAI 514
Cdd:PRK13640  86 VGIVFQNPdnqfvgATVGDDVAfglENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANL-----------SGGQKQRVAI 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 515 ARMVLAEPKVVILDEATSALDAATEYNLHQaLARFL---SGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDG 583
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILK-LIRKLkkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225
cbiO PRK13649
energy-coupling factor transporter ATPase;
368-591 1.92e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 97.51  E-value: 1.92e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 368 GIEVRGLNFGYG-----EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG----STQQEIGLE 438
Cdd:PRK13649   2 GINLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitSTSKNKDIK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 439 TIRENVSVVLQHP--ALFNDTVRANLTMGrersDQACWQALEIAQLDATVKALPLGLD-SVVGRSGVRFSGGQRQRLAIA 515
Cdd:PRK13649  82 QIRKKVGLVFQFPesQLFEETVLKDVAFG----PQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 516 RMVLAEPKVVILDEATSALDAATEY-------NLHQalarflSGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQ 587
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKelmtlfkKLHQ------SGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKD 231


                 ....
gi 489309308 588 LIAD 591
Cdd:PRK13649 232 IFQD 235
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
366-589 2.18e-22

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 98.75  E-value: 2.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 366 TVGIEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGsTQQEIGLETIRENVS 445
Cdd:PRK13536  39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG-VPVPARARLARARIG 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 446 VVLQHPALFND-TVRANLT-------MGRERSDQACWQALEIAQLDAtvKAlplglDSVVGrsgvRFSGGQRQRLAIARM 517
Cdd:PRK13536 118 VVPQFDNLDLEfTVRENLLvfgryfgMSTREIEAVIPSLLEFARLES--KA-----DARVS----DLSGGMKRRLTLARA 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308 518 VLAEPKVVILDEATSALDAATEYNLHQALARFLS-GRTTLIIAHRL-SAVKQADRVLVFDGGHIAEDGDHQQLI 589
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMeEAERLCDRLCVLEAGRKIAEGRPHALI 260
cbiO PRK13643
energy-coupling factor transporter ATPase;
384-583 2.73e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 97.50  E-value: 2.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG----STQQEIGLETIRENVSVVLQHP--ALFNDT 457
Cdd:PRK13643  22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQKEIKPVRKKVGVVFQFPesQLFEET 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 458 VRANLTMG-------RERSDQACWQALEIAQLDATVKAlplgldsvvgRSGVRFSGGQRQRLAIARMVLAEPKVVILDEA 530
Cdd:PRK13643 102 VLKDVAFGpqnfgipKEKAEKIAAEKLEMVGLADEFWE----------KSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 531 TSALDAATEYNLHQALARF-LSGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDG 583
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 369-588 2.97e-22

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: 95.51  E-value: 2.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIR-FGGSTQQEIGleTIRENVSVV 447
Cdd:cd03265    1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvAGHDVVREPR--EVRRRIGIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALFND-TVRANLTM-------GRERSDQACWQALEIAQL----DATVKAlplgldsvvgrsgvrFSGGQRQRLAIA 515
Cdd:cd03265   79 FQDLSVDDElTGWENLYIharlygvPGAERRERIDELLDFVGLleaaDRLVKT---------------YSGGMRRRLEIA 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 516 RMVLAEPKVVILDEATSALDAAT-----EYnLHQALARFlsGRTTLIIAHRL-SAVKQADRVLVFDGGHIAEDGDHQQL 588
Cdd:cd03265  144 RSLVHRPEVLFLDEPTIGLDPQTrahvwEY-IEKLKEEF--GMTILLTTHYMeEAEQLCDRVAIIDHGRIIAEGTPEEL 219
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 372-591 3.11e-22

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 98.11  E-value: 3.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 372 RGLnFGyGEELV--LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG---STQQEIGLETIRENVSV 446
Cdd:PRK11308  19 RGL-FK-PERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdlLKADPEAQKLLRQKIQI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHP-ALFN--DTVRANLTmgrersdqacwQALEI-AQLDA---TVKALplgldSVVGRSGVR----------FSGGQR 509
Cdd:PRK11308  97 VFQNPyGSLNprKKVGQILE-----------EPLLInTSLSAaerREKAL-----AMMAKVGLRpehydryphmFSGGQR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 510 QRLAIARMVLAEPKVVILDEATSALDA---ATEYNLHQALARFLsGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDH 585
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVsvqAQVLNLMMDLQQEL-GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTK 239


                 ....*.
gi 489309308 586 QQLIAD 591
Cdd:PRK11308 240 EQIFNN 245
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 367-573 3.12e-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: 94.54  E-value: 3.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 367 VGIEVRGLNF------GYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQA--GSIRFGGstqQEIGLE 438
Cdd:cd03213    2 VTLSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLING---RPLDKR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 439 TIRENVSVVLQHpalfnDTVRANLTMgrersdqacWQALEIAqldATVKALplgldsvvgrsgvrfSGGQRQRLAIARMV 518
Cdd:cd03213   79 SFRKIIGYVPQD-----DILHPTLTV---------RETLMFA---AKLRGL---------------SGGERKRVSIALEL 126

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 519 LAEPKVVILDEATSALDAATEYNLHQALARF-LSGRTTLIIAHRLSA--VKQADRVLV 573
Cdd:cd03213  127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSSeiFELFDKLLL 184
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 369-573 3.46e-22

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 100.10  E-value: 3.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGsTQQEIG--LETIRENVSV 446
Cdd:COG3845    6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG-KPVRIRspRDAIALGIGM 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPALFND-TVRANLTMGRERSDqacWQALEIAQLDATVKA------LPLGLDSVVGRSGVrfsgGQRQRLAIARMVL 519
Cdd:COG3845   85 VHQHFMLVPNlTVAENIVLGLEPTK---GGRLDRKAARARIRElserygLDVDPDAKVEDLSV----GEQQRVEILKALY 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 520 AEPKVVILDEATSAL-DAATEyNLHQALARFLS-GRTTLIIAHRLSAVKQ-ADRVLV 573
Cdd:COG3845  158 RGARILILDEPTAVLtPQEAD-ELFEILRRLAAeGKSIIFITHKLREVMAiADRVTV 213
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 369-606 4.44e-22

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: 95.54  E-value: 4.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAG-SIR-FGgstqQEIGLETIRE---- 442
Cdd:COG1119    4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlFG----ERRGGEDVWElrkr 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 443 --NVSVVLQHPALFNDTVR------ANLTMGRersdqacWQALEIAQLDATVKALP-LGLDSVVGRSGVRFSGGQRQRLA 513
Cdd:COG1119   80 igLVSPALQLRFPRDETVLdvvlsgFFDSIGL-------YREPTDEQRERARELLElLGLAHLADRPFGTLSQGEQRRVL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 514 IARMVLAEPKVVILDEATSALDAATEYNLHQALARF-LSGRTTLI-IAHRLSAVKQA-DRVLVFDGGHIAEDGDHQQLIA 590
Cdd:COG1119  153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLT 232

                        250
                 ....*....|....*.
gi 489309308 591 DGGLyAKLYGHLQQVR 606
Cdd:COG1119  233 SENL-SEAFGLPVEVE 247
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 369-582 1.23e-21

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 94.04  E-value: 1.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLN--FGYGEELV--LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG---STQQEIGLETIR 441
Cdd:COG4181    9 IELRGLTktVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlFALDEDARARLR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 442 -ENVSVVLQH----PALfndTVRANLTM-----GRERSDQACWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQR 511
Cdd:COG4181   89 aRHVGFVFQSfqllPTL---TALENVMLplelaGRRDARARARALLERVGLGHRLDHYPAQL-----------SGGEQQR 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 512 LAIARMVLAEPKVVILDEATSALDAATE-------YNLHQALArflsgrTTLIIA-HRLSAVKQADRVLVFDGGHIAED 582
Cdd:COG4181  155 VALARAFATEPAILFADEPTGNLDAATGeqiidllFELNRERG------TTLVLVtHDPALAARCDRVLRLRAGRLVED 227
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 104-342 1.32e-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: 350020 [Multi-domain]  Cd Length: 289  Bit Score: 95.24  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGI 183
Cdd:cd18576   51 VFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVL 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 184 LMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVRD 263
Cdd:cd18576  131 LFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVK 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 264 FAVNsqwksdaSSRASGLLFQFGIDIFRAAAMLTVLFS-------DLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAAG 336
Cdd:cd18576  211 LALK-------RARIRALFSSFIIFLLFGAIVAVLWYGgrlvlagELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKAL 283


                 ....*.
gi 489309308 337 GALTRI 342
Cdd:cd18576  284 GASERV 289
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
369-588 1.36e-21

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 96.71  E-value: 1.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG------STQQeigletirE 442
Cdd:PRK11432   7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvthrSIQQ--------R 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 443 NVSVVLQHPALF-----NDTVRANLTM---GRERSDQACWQALEIAQLDatvkalplGLDSvvgrsgvRF----SGGQRQ 510
Cdd:PRK11432  79 DICMVFQSYALFphmslGENVGYGLKMlgvPKEERKQRVKEALELVDLA--------GFED-------RYvdqiSGGQQQ 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 511 RLAIARMVLAEPKVVILDEATSALDAateyNLHQAL---ARFLSGR---TTLIIAHRLS-AVKQADRVLVFDGGHIAEDG 583
Cdd:PRK11432 144 RVALARALILKPKVLLFDEPLSNLDA----NLRRSMrekIRELQQQfniTSLYVTHDQSeAFAVSDTVIVMNKGKIMQIG 219


                 ....*
gi 489309308 584 DHQQL 588
Cdd:PRK11432 220 SPQEL 224
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 371-579 1.81e-21

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 98.21  E-value: 1.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 371 VRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQ-----QEIGL---ETIRE 442
Cdd:COG0488    1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRigylpQEPPLdddLTVLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 443 NVSVVLQH-PALFNDTVRANLTMGRERSDQACWQALEIA-------QLDATVKAL--PLGLDSVVGRSGVR-FSGGQRQR 511
Cdd:COG0488   81 TVLDGDAElRALEAELEELEAKLAEPDEDLERLAELQEEfealggwEAEARAEEIlsGLGFPEEDLDRPVSeLSGGWRRR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308 512 LAIARMVLAEPKVVILDEATSALDA-ATEYnlhqaLARFLSGR--TTLIIAH-R--LSAVkqADRVLVFDGGHI 579
Cdd:COG0488  161 VALARALLSEPDLLLLDEPTNHLDLeSIEW-----LEEFLKNYpgTVLVVSHdRyfLDRV--ATRILELDRGKL 227
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 371-583 2.01e-21

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 94.22  E-value: 2.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 371 VRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETI---------R 441
Cdd:PRK11701   9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 442 ENVSVVLQHPAlfnDTVRANLT---------M-------GRERSDQACW-QALEIAQldATVKALPlgldsvvgrsgVRF 504
Cdd:PRK11701  89 TEWGFVHQHPR---DGLRMQVSaggnigerlMavgarhyGDIRATAGDWlERVEIDA--ARIDDLP-----------TTF 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 505 SGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLS--GRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAE 581
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVE 232


                 ..
gi 489309308 582 DG 583
Cdd:PRK11701 233 SG 234
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 364-591 2.05e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 94.53  E-value: 2.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 364 RETVGIEVRGLNFGYGEEL-VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGS--TQQEIGLETI 440
Cdd:PRK13636   1 MEDYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 441 RENVSVVLQHP--ALFNDTVRANLTMGrersdqacwqaleIAQLDATVKALPLGLDSVVGRSGVR---------FSGGQR 509
Cdd:PRK13636  81 RESVGMVFQDPdnQLFSASVYQDVSFG-------------AVNLKLPEDEVRKRVDNALKRTGIEhlkdkpthcLSFGQK 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 510 QRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLS--GRTTLIIAHRLSAVK-QADRVLVFDGGHIAEDGDHQ 586
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPK 227


                 ....*
gi 489309308 587 QLIAD 591
Cdd:PRK13636 228 EVFAE 232
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 369-582 2.31e-21

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 94.00  E-value: 2.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLN--FGYG---EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEI-GLETIR- 441
Cdd:COG1101    2 LELKNLSktFNPGtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG---KDVtKLPEYKr 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 442 -ENVSVVLQHPAL---FNDTVRANLTM----GRERSDQACWQALEIAQLDATVKALPLGL----DSVVGRsgvrFSGGQR 509
Cdd:COG1101   79 aKYIGRVFQDPMMgtaPSMTIEENLALayrrGKRRGLRRGLTKKRRELFRELLATLGLGLenrlDTKVGL----LSGGQR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 510 QRLAIARMVLAEPKVVILDEATSALDAAT-------------EYNLhqalarflsgrTTLIIAHRLS-AVKQADRVLVFD 575
Cdd:COG1101  155 QALSLLMATLTKPKLLLLDEHTAALDPKTaalvleltekiveENNL-----------TTLMVTHNMEqALDYGNRLIMMH 223


                 ....*..
gi 489309308 576 GGHIAED 582
Cdd:COG1101  224 EGRIILD 230
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 369-588 2.42e-21

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 93.69  E-value: 2.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLL--LGLYTPQ---AGSIRFGGSTQQEIGLET--IR 441
Cdd:PRK14239   6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTDTvdLR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 442 ENVSVVLQHPALFNDTVRANLTMG--------RERSDQACWQALEIAQLDATVKalplgldSVVGRSGVRFSGGQRQRLA 513
Cdd:PRK14239  86 KEIGMVFQQPNPFPMSIYENVVYGlrlkgikdKQVLDEAVEKSLKGASIWDEVK-------DRLHDSALGLSGGQQQRVC 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308 514 IARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRL-SAVKQADRVLVFDGGHIAEDGDHQQL 588
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqQASRISDRTGFFLDGDLIEYNDTKQM 234
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 104-342 2.75e-21

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: 94.47  E-value: 2.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGI 183
Cdd:cd18550   54 LLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVA 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 184 LMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDA--IQEVRAGNRQGFFLGRLGQRAQEV 261
Cdd:cd18550  134 MLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSREL 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 262 RDFAVNSQWKSDASSRASGLLFQFGIDIFRAAAMLTVLFSDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAAGGALTR 341
Cdd:cd18550  214 RDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFER 293


                 .
gi 489309308 342 I 342
Cdd:cd18550  294 I 294
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 369-583 2.78e-21

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 96.45  E-value: 2.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVL 448
Cdd:PRK09536   4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPAL-FNDTVRANLTMGR--ERSDQACWQALEIAQLDATVKAlpLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVV 525
Cdd:PRK09536  84 QDTSLsFEFDVRQVVEMGRtpHRSRFDTWTETDRAAVERAMER--TGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 526 ILDEATSALDAAteynlHQ----ALARFL--SGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDG 583
Cdd:PRK09536 162 LLDEPTASLDIN-----HQvrtlELVRRLvdDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
369-560 4.19e-21

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 93.23  E-value: 4.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETirenvSVVL 448
Cdd:PRK11248   2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALFN-DTVRANLTMGRERSDQACWQALEIAQldatvKALPL-GLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVI 526
Cdd:PRK11248  77 QNEGLLPwRNVQDNVAFGLQLAGVEKMQRLEIAH-----QMLKKvGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489309308 527 LDEATSALDAATEYNLHQALARFL--SGRTTLIIAH 560
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWqeTGKQVLLITH 187
cbiO PRK13646
energy-coupling factor transporter ATPase;
380-592 4.40e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 93.69  E-value: 4.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 380 EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGST----QQEIGLETIRENVSVVLQHP--AL 453
Cdd:PRK13646  19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIRPVRKRIGMVFQFPesQL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 454 FNDTVRANLTMGRERSDqacwQALEIAQLDATVKALPLGLD-SVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATS 532
Cdd:PRK13646  99 FEDTVEREIIFGPKNFK----MNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308 533 ALDAATEYNLHQALARFL--SGRTTLIIAHRLSAV-KQADRVLVFDGGHIAEDGDHQQLIADG 592
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
 101-325 7.06e-21

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: 93.22  E-value: 7.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 101 GALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGT 180
Cdd:cd18544   53 LSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGI 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 181 SGILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQE 260
Cdd:cd18544  133 LIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQE 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308 261 VRDFavnsqwkSDASSRASGLLFQFgIDIFRAAAMLTVLF--------SDLSIGQMLAVFSYLWFMISPVEQL 325
Cdd:cd18544  213 YRKA-------NLKSIKLFALFRPL-VELLSSLALALVLWygggqvlsGAVTLGVLYAFIQYIQRFFRPIRDL 277
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 383-577 1.05e-20

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: 92.61  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 383 VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqqeigletireNVSVVLQHPALFNDTVRANL 462
Cdd:cd03291   52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 463 TMGRERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNL 542
Cdd:cd03291  119 IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489309308 543 HQA-LARFLSGRTTLIIAHRLSAVKQADRVLVFDGG 577
Cdd:cd03291  199 FEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 388-590 1.28e-20

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: 91.94  E-value: 1.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 388 NLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEIG-------LETIRENVSVVLQHPALF-NDTVR 459
Cdd:cd03294   44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDG---QDIAamsrkelRELRRKKISMVFQSFALLpHRTVL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 460 ANLTMG--------RERSDQACwQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIARMVLAEPKVVILDEAT 531
Cdd:cd03294  121 ENVAFGlevqgvprAEREERAA-EALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 532 SALDAATEYNLHQALARFLS--GRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:cd03294  189 SALDPLIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 369-578 1.29e-20

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: 88.27  E-value: 1.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGgstqqeigletirenvsvvl 448
Cdd:cd03221    1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 qhpalfndtvranltmgrersdqacwQALEIAQLDatvkalplgldsvvgrsgvRFSGGQRQRLAIARMVLAEPKVVILD 528
Cdd:cd03221   61 --------------------------STVKIGYFE-------------------QLSGGEKMRLALAKLLLENPNLLLLD 95

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 529 EATSALDAATEynlhQALARFLSG--RTTLIIAH-R--LSAVkqADRVLVFDGGH 578
Cdd:cd03221   96 EPTNHLDLESI----EALEEALKEypGTVILVSHdRyfLDQV--ATKIIELEDGK 144
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
 104-342 1.33e-20

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: 92.24  E-value: 1.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGI 183
Cdd:cd18557   51 VFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLII 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 184 LMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVRD 263
Cdd:cd18557  131 LFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYR 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 264 FAVnsqwksdASSRASGlLFQFGIDIFRAAAMLTVLF--------SDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAA 335
Cdd:cd18557  211 LAR-------KKALANA-LFQGITSLLIYLSLLLVLWyggylvlsGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKA 282


                 ....*..
gi 489309308 336 GGALTRI 342
Cdd:cd18557  283 LGASERV 289
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 375-578 3.71e-20

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: 95.36  E-value: 3.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   375 NFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqqeigletireNVSVVLQHPALF 454
Cdd:TIGR01271  433 NFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIM 499

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   455 NDTVRANLTMGRERSDQACWQALEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSAL 534
Cdd:TIGR01271  500 PGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHL 579

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 489309308   535 DAATEYNLHQA-LARFLSGRTTLIIAHRLSAVKQADRVLVFDGGH 578
Cdd:TIGR01271  580 DVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGV 624
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
384-579 4.02e-20

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 92.24  E-value: 4.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIA---PGEKV-AIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGST----QQEIGLETIRENVSVVLQHPALF- 454
Cdd:PRK11144  10 LGDLCLTVNltlPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaEKGICLPPEKRRIGYVFQDARLFp 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 455 NDTVRANLTMGRERSDQAcwqaleiaQLDATVKALplGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSAL 534
Cdd:PRK11144  90 HYKVRGNLRYGMAKSMVA--------QFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489309308 535 DAATEYNLHQALARfLSGRTTLII---AHRLSAVKQ-ADRVLVFDGGHI 579
Cdd:PRK11144 160 DLPRKRELLPYLER-LAREINIPIlyvSHSLDEILRlADRVVVLEQGKV 207
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 369-584 4.54e-20

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: 88.74  E-value: 4.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGL--YTPQAGSIRFGGstqQEIgletirENVSV 446
Cdd:cd03217    1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKG---EDI------TDLPP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 vlqhpalfNDTVRANLTMgrersdqaCWQA-LEIAQLdaTVKALplgLDSVvgrsGVRFSGGQRQRLAIARMVLAEPKVV 525
Cdd:cd03217   72 --------EERARLGIFL--------AFQYpPEIPGV--KNADF---LRYV----NEGFSGGEKKRNEILQLLLLEPDLA 126

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 526 ILDEATSALDAATEYNLHQALARFLS-GRTTLIIAH--RLSAVKQADRVLVFDGGHIAEDGD 584
Cdd:cd03217  127 ILDEPDSGLDIDALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD 188
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 377-584 6.78e-20

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 89.37  E-value: 6.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 377 GYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRfggstqqeigletIRENVSVVLQ-----HP 451
Cdd:COG1134   35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE-------------VNGRVSALLElgagfHP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 452 ALfndTVRAN-----LTMGRERSdqacwqalEIAQLdatvkalplgLDSVVGRSGV---------RFSGGQRQRLAIARM 517
Cdd:COG1134  102 EL---TGRENiylngRLLGLSRK--------EIDEK----------FDEIVEFAELgdfidqpvkTYSSGMRARLAFAVA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 518 VLAEPKVVILDEATSALDAATeynLHQALARFL----SGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGD 584
Cdd:COG1134  161 TAVDPDILLVDEVLAVGDAAF---QKKCLARIRelreSGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
 100-328 8.77e-20

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: 90.16  E-value: 8.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 100 CGALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVG 179
Cdd:cd18547   56 LLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVG 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 180 TSGILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQ 259
Cdd:cd18547  136 TLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINE 215

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 260 EVRDFAVNSQWksdassrASGLL---------FQFGIDIFRAAAMltVLFSDLSIGQMLAVFSYLWFMISPVEQLLNL 328
Cdd:cd18547  216 ELYKASFKAQF-------YSGLLmpimnfinnLGYVLVAVVGGLL--VINGALTVGVIQAFLQYSRQFSQPINQISQQ 284
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 383-577 1.10e-19

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


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 88.26  E-value: 1.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 383 VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRF---GG------STQQEIgLETIRENVSVVLQH--- 450
Cdd:COG4778   26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGwvdlaqASPREI-LALRRRTIGYVSQFlrv 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 451 ----PALfnDTV-RANLTMGRERsDQACWQALEI-AQLDatvkaLPLGLDSVvgrSGVRFSGGQRQRLAIARMVLAEPKV 524
Cdd:COG4778  105 iprvSAL--DVVaEPLLERGVDR-EEARARARELlARLN-----LPERLWDL---PPATFSGGEQQRVNIARGFIADPPL 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 525 VILDEATSALDAAT-----EYnLHQALARflsGRTTLIIAHRLSAVKQ-ADRVLVFDGG 577
Cdd:COG4778  174 LLLDEPTASLDAANravvvEL-IEEAKAR---GTAIIGIFHDEEVREAvADRVVDVTPF 228
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 369-583 1.20e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 88.82  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQL---LLGLYtPQA---GSIRFGGSTQQEIGLETIRE 442
Cdd:PRK14247   4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELY-PEArvsGEVYLDGQDIFKMDVIELRR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 443 NVSVVLQHP-ALFNDTVRANLTMG---------RERSDQACWQALEIAQLDATVKALplgLDSVVGrsgvRFSGGQRQRL 512
Cdd:PRK14247  83 RVQMVFQIPnPIPNLSIFENVALGlklnrlvksKKELQERVRWALEKAQLWDEVKDR---LDAPAG----KLSGGQQQRL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 513 AIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAH-RLSAVKQADRVLVFDGGHIAEDG 583
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
378-591 1.28e-19

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 88.87  E-value: 1.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 378 YGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEIG----------------LETIR 441
Cdd:PRK10619  15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNG---QTINlvrdkdgqlkvadknqLRLLR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 442 ENVSVVLQHPALFND-TVRANLTmgrersdQACWQALEIAQLDATVKAL----PLGLD-SVVGRSGVRFSGGQRQRLAIA 515
Cdd:PRK10619  92 TRLTMVFQHFNLWSHmTVLENVM-------EAPIQVLGLSKQEARERAVkylaKVGIDeRAQGKYPVHLSGGQQQRVSIA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 516 RMVLAEPKVVILDEATSALD---AATEYNLHQALARflSGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAE--EGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 368-538 1.40e-19

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 87.54  E-value: 1.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 368 GIEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQA---GSIRFGGstqQEI-GLETIREN 443
Cdd:COG4136    1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNG---RRLtALPAEQRR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 444 VSVVLQHPALF-NDTVRANL------TMGRERSDQACWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIAR 516
Cdd:COG4136   78 IGILFQDDLLFpHLSVGENLafalppTIGRAQRRARVEQALEEAGLAGFADRDPATL-----------SGGQRARVALLR 146

                        170       180
                 ....*....|....*....|..
gi 489309308 517 MVLAEPKVVILDEATSALDAAT 538
Cdd:COG4136  147 ALLAEPRALLLDEPFSKLDAAL 168
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
371-600 1.48e-19

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 88.89  E-value: 1.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 371 VRG--LNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVL 448
Cdd:PRK10253   8 LRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALFND-TVRANLTMGReRSDQACWQALEIAQLDATVKAL-PLGLDSVVGRSGVRFSGGQRQRLAIArMVLA-EPKVV 525
Cdd:PRK10253  88 QNATTPGDiTVQELVARGR-YPHQPLFTRWRKEDEEAVTKAMqATGITHLADQSVDTLSGGQRQRAWIA-MVLAqETAIM 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 526 ILDEATSALDAATEYNLHQALARF--LSGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIAdGGLYAKLYG 600
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT-AELIERIYG 242
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
380-583 2.08e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 88.61  E-value: 2.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 380 EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG-STQQEIGLETIRENVSVVLQHP--ALFND 456
Cdd:PRK13633  22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENLWDIRNKAGMVFQNPdnQIVAT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 457 TVRANLTMGRERSDQacwQALEI-AQLDATVKAlplgldsvVGRSGVR------FSGGQRQRLAIARMVLAEPKVVILDE 529
Cdd:PRK13633 102 IVEEDVAFGPENLGI---PPEEIrERVDESLKK--------VGMYEYRrhaphlLSGGQKQRVAIAGILAMRPECIIFDE 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308 530 ATSALDAATEYNLHQALARF--LSGRTTLIIAHRLSAVKQADRVLVFDGGHIAEDG 583
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEG 226
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 380-580 2.25e-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: 87.33  E-value: 2.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 380 EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLlglytpqAGSIRFGGSTQQEIGL-------ETIRENVSVVLQ--- 449
Cdd:cd03234   19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAI-------SGRVEGGGTTSGQILFngqprkpDQFQKCVAYVRQddi 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 450 -HPALfndTVR------ANLTMGRERSDQacwqalEIAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEP 522
Cdd:cd03234   92 lLPGL---TVRetltytAILRLPRKSSDA------IRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDP 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489309308 523 KVVILDEATSALDAATEYNLHQALARFL-SGRTTLIIAH--RLSAVKQADRVLVFDGGHIA 580
Cdd:cd03234  163 KVLILDEPTSGLDSFTALNLVSTLSQLArRNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 104-349 2.26e-19

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: 88.75  E-value: 2.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGI 183
Cdd:cd18778   55 LLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAII 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 184 LMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVRd 263
Cdd:cd18778  135 LFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYR- 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 264 favnsqwksDASSRASGL--LFQFGIDIFRAAAMLTVLF--------SDLSIGQMLAVFSYLWFMISPVEQllnlqyayy 333
Cdd:cd18778  214 ---------KAQLRAMKLwaIFHPLMEFLTSLGTVLVLGfggrlvlaGELTIGDLVAFLLYLGLFYEPITS--------- 275

                        250
                 ....*....|....*.
gi 489309308 334 aaggaLTRINELLARA 349
Cdd:cd18778  276 -----LHGLNEMLQRA 286
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 369-591 2.34e-19

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: 91.67  E-value: 2.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLN--FGYGEEL--VLDQLNLNIAPGEKVAIVGASGGGKS----TLVQLLLGLYTPQAGSIRFGG---STQQEIGL 437
Cdd:COG4172    7 LSVEDLSvaFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGqdlLGLSEREL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 438 ETIREN-VSVVLQHP--ALfN----------DTVRANLTMGRERSDQACWQALE---IAQLDATVKALPLgldsvvgrsg 501
Cdd:COG4172   87 RRIRGNrIAMIFQEPmtSL-NplhtigkqiaEVLRLHRGLSGAAARARALELLErvgIPDPERRLDAYPH---------- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 502 vRFSGGQRQRLAIArMVLA-EPKVVILDEATSALDAATeynlhQA--------LARFLsGRTTLIIAHRLSAVKQ-ADRV 571
Cdd:COG4172  156 -QLSGGQRQRVMIA-MALAnEPDLLIADEPTTALDVTV-----QAqildllkdLQREL-GMALLLITHDLGVVRRfADRV 227

                        250       260
                 ....*....|....*....|
gi 489309308 572 LVFDGGHIAEDGDHQQLIAD 591
Cdd:COG4172  228 AVMRQGEIVEQGPTAELFAA 247
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 351-590 2.78e-19

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 91.31  E-value: 2.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 351 EPQyaGGADPFTGRETVGIEVRGLNFGY-----------GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYT 419
Cdd:PRK15134 260 EPS--GDPVPLPEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 420 PQaGSIRFGGSTQQEIG---LETIRENVSVVLQHPalfNDTVRANLTMGR--ERSDQACWQALEIAQLDATVKAL--PLG 492
Cdd:PRK15134 338 SQ-GEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP---NSSLNPRLNVLQiiEEGLRVHQPTLSAAQREQQVIAVmeEVG 413

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 493 LDSVV-GRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLhQALARFLSGRTTL---IIAHRLSAVKQ- 567
Cdd:PRK15134 414 LDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQI-LALLKSLQQKHQLaylFISHDLHVVRAl 492

                        250       260
                 ....*....|....*....|...
gi 489309308 568 ADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:PRK15134 493 CHQVIVLRQGEVVEQGDCERVFA 515
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
383-579 3.35e-19

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 86.79  E-value: 3.35e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 383 VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIG----LETIRENVSVVLQHPALFND-T 457
Cdd:PRK11629  24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakAELRNQKLGFIYQFHHLLPDfT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 458 VRANLTM----GRERSDQACWQALEIAQldatvkalPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSA 533
Cdd:PRK11629 104 ALENVAMplliGKKKPAEINSRALEMLA--------AVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489309308 534 LDAATEYNLHQALARF--LSGRTTLIIAHRLSAVKQADRVLVFDGGHI 579
Cdd:PRK11629 176 LDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
369-582 3.50e-19

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 91.71  E-value: 3.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGY--GEEL--VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETI---- 440
Cdd:PRK10535   5 LELKDIRRSYpsGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 441 RENVSVVLQHPALFndtvrANLTMGRERSDQACWQALEIAQLDATVKAL--PLGLDSVVGRSGVRFSGGQRQRLAIARMV 518
Cdd:PRK10535  85 REHFGFIFQRYHLL-----SHLTAAQNVEVPAVYAGLERKQRLLRAQELlqRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 519 LAEPKVVILDEATSALDAATEYN----LHQALARflsGRTTLIIAHRLSAVKQADRVLVFDGGHIAED 582
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEvmaiLHQLRDR---GHTVIIVTHDPQVAAQAERVIEIRDGEIVRN 224
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 269-595 3.66e-19

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: 92.38  E-value: 3.66e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   269 QWKSDASSRASGLLFQFGIDifraaamLTVLFSDLSIGQMLAvfsylWFMI--------SPVEQLLNLQYAYYAAGG--- 337
Cdd:TIGR01257  820 QWSNIGNSPLEGDEFSFLLS-------MKMMLLDAALYGLLA-----WYLDqvfpgdygTPLPWYFLLQESYWLGGEgcs 887

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   338 -----ALTRINELLARADEPQYAGGA-DPFTGRE----TVGIEVRGLN--FGYGEELVLDQLNLNIAPGEKVAIVGASGG 405
Cdd:TIGR01257  888 treerALEKTEPLTEEMEDPEHPEGInDSFFERElpglVPGVCVKNLVkiFEPSGRPAVDRLNITFYENQITAFLGHNGA 967

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   406 GKSTLVQLLLGLYTPQAGSIRFGGStQQEIGLETIRENVSVVLQHPALFNDTVRANLTMGRERSDQACWqalEIAQLDAT 485
Cdd:TIGR01257  968 GKTTTLSILTGLLPPTSGTVLVGGK-DIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSW---EEAQLEME 1043

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   486 VKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSav 565
Cdd:TIGR01257 1044 AMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD-- 1121

                          330       340       350
                   ....*....|....*....|....*....|
gi 489309308   566 kQADRVlvfdgghiaedGDHQQLIADGGLY 595
Cdd:TIGR01257 1122 -EADLL-----------GDRIAIISQGRLY 1139
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
369-588 5.41e-19

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 89.12  E-value: 5.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstQQEIGLETIRENVSVVL 448
Cdd:PRK11607  20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--VDLSHVPPYQRPINMMF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALF-NDTVRANLTMGRERSDQAcwqALEIAQLDATVKALpLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVIL 527
Cdd:PRK11607  98 QSYALFpHMTVEQNIAFGLKQDKLP---KAEIASRVNEMLGL-VHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308 528 DEATSALDAATEYNLHQALARFLS--GRTTLIIAH-RLSAVKQADRVLVFDGGHIAEDGDHQQL 588
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 368-567 5.72e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 87.01  E-value: 5.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 368 GIEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQA-----GSIRFGGST--QQEIGLETI 440
Cdd:PRK14258   7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNiyERRVNLNRL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 441 RENVSVVLQHPALFNDTVRANLTMG--------RERSDQACWQALEIAQLDATVKalplgldSVVGRSGVRFSGGQRQRL 512
Cdd:PRK14258  87 RRQVSMVHPKPNLFPMSVYDNVAYGvkivgwrpKLEIDDIVESALKDADLWDEIK-------HKIHKSALDLSGGQQQRL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 513 AIARMVLAEPKVVILDEATSALDAATEYNLHQAL--ARFLSGRTTLIIAHRLSAVKQ 567
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSR 216
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
 383-584 7.10e-19

FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273907 [Multi-domain]  Cd Length: 243  Bit Score: 86.16  E-value: 7.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  383 VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLG--LYTPQAGSIRFGGSTQQEIGLETI-RENVSVVLQHP-------- 451
Cdd:TIGR01978  15 ILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDLLELEPDERaRAGLFLAFQYPeeipgvsn 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  452 ALFndtVRANLTMGRERSDQACWQALEIAQLDATVKALpLGLD-SVVGRS-GVRFSGGQRQRLAIARMVLAEPKVVILDE 529
Cdd:TIGR01978  95 LEF---LRSALNARRSARGEEPLDLLDFEKLLKEKLAL-LDMDeEFLNRSvNEGFSGGEKKRNEILQMALLEPKLAILDE 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308  530 ATSALDAATEYNLHQALARFLS-GRTTLIIAH--RLSAVKQADRVLVFDGGHIAEDGD 584
Cdd:TIGR01978 171 IDSGLDIDALKIVAEGINRLREpDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSGD 228
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 369-591 7.68e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 87.06  E-value: 7.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGE-ELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGST--QQEIGLETIRENVS 445
Cdd:PRK13639   2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikYDKKSLLEVRKTVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 446 VVLQHP--ALFNDTVRA-------NLTMGRERSDQACWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIAR 516
Cdd:PRK13639  82 IVFQNPddQLFAPTVEEdvafgplNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIAG 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 517 MVLAEPKVVILDEATSALD---AATEYNLHQALARflSGRTTLIIAHRLSAV-KQADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDpmgASQIMKLLYDLNK--EGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSD 227
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 358-571 9.74e-19

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 86.37  E-value: 9.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 358 ADPFTGRETVgIEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLL--LGLYTPQA---GSIRFGGST- 431
Cdd:PRK14243   1 TSTLNGTETV-LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGFrveGKVTFHGKNl 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 432 -QQEIGLETIRENVSVVLQHPALFNDTVRANLTMG------RERSDQACWQALEIAQLDATVKalplgldSVVGRSGVRF 504
Cdd:PRK14243  80 yAPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGaringyKGDMDELVERSLRQAALWDEVK-------DKLKQSGLSL 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 505 SGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLsavKQADRV 571
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM---QQAARV 216
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 369-559 1.01e-18

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: 85.15  E-value: 1.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELV-LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG---STQQEIGLETIRENV 444
Cdd:cd03292    1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvSDLRGRAIPYLRRKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 445 SVVLQHPALFND-TVRANLTMGRERSDQA--CWQ-----ALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIAR 516
Cdd:cd03292   81 GVVFQDFRLLPDrNVYENVAFALEVTGVPprEIRkrvpaALELVGLSHKHRALPAEL-----------SGGEQQRVAIAR 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489309308 517 MVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIA 559
Cdd:cd03292  150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 369-561 1.76e-18

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 84.16  E-value: 1.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEIGLETIREnVSVVL 448
Cdd:PRK13539   3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAE-ACHYL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QH-----PALfndTVRANLTMgrersdqacWQAL---EIAQLDATVKAlpLGLDSVVGRSGVRFSGGQRQRLAIARMVLA 520
Cdd:PRK13539  79 GHrnamkPAL---TVAENLEF---------WAAFlggEELDIAAALEA--VGLAPLAHLPFGYLSAGQKRRVALARLLVS 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489309308 521 EPKVVILDEATSALDAATEynlhqalARFLSgrttLIIAHR 561
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAV-------ALFAE----LIRAHL 174
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
369-583 1.91e-18

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 85.45  E-value: 1.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVL 448
Cdd:PRK11231   3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALFND-TVRANLTMGR-----------ERSDQACWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIAr 516
Cdd:PRK11231  83 QHHLTPEGiTVRELVAYGRspwlslwgrlsAEDNARVNQAMEQTRINHLADRRLTDL-----------SGGQRQRAFLA- 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 517 MVLAE-PKVVILDEATSALDAAteynlHQA----LARFLS--GRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDG 583
Cdd:PRK11231 151 MVLAQdTPVVLLDEPTTYLDIN-----HQVelmrLMRELNtqGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQG 220
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 369-577 2.44e-18

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 85.04  E-value: 2.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEI-GLETIRENVSVV 447
Cdd:PRK11300   6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARMGVVRT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALFND-TVRANL------------------TMGRERSDQacwQALEIAQ--LDAtvkalpLGLDSVVGRSGVRFSG 506
Cdd:PRK11300  86 FQHVRLFREmTVIENLlvaqhqqlktglfsgllkTPAFRRAES---EALDRAAtwLER------VGLLEHANRQAGNLAY 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308 507 GQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALA--RFLSGRTTLIIAHRLSAVKQ-ADRVLVFDGG 577
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQG 230
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 369-583 2.51e-18

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: 83.96  E-value: 2.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEE----LVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLEtIRENV 444
Cdd:cd03266    2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 445 SVVLQHPALFND-TVRANLT-MGRersdqacWQALEIAQLDATVKALP--LGLDSVVGRSGVRFSGGQRQRLAIARMVLA 520
Cdd:cd03266   81 GFVSDSTGLYDRlTARENLEyFAG-------LYGLKGDELTARLEELAdrLGMEELLDRRVGGFSTGMRQKVAIARALVH 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 521 EPKVVILDEATSALDAATEYNLHQALARFLS-GRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDG 583
Cdd:cd03266  154 DPPVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 121-590 2.56e-18

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 88.49  E-value: 2.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 121 VYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVD-KFVgeTLSRFLVAMLTLVGTSGILMWMHWKLALLILLFN 199
Cdd:PRK10522  80 VYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITiAFV--RLPELVQGIILTLGSAAYLAWLSPKMLLVTAIWM 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 200 PLVIYATVQLGKRV-KHLKKL-ENDstsrftQALTETLDAIQEVR---AGNRQgfflgrlgqRAQEV--RDFAVNSQWKS 272
Cdd:PRK10522 158 AVTIWGGFVLVARVyKHMATLrETE------DKLYNDYQTVLEGRkelTLNRE---------RAEYVfeNEYEPDAQEYR 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 273 DASSRAsgllfqfgiDIFRAAA-------ML----TVLFSDLSIG----QMLAVFSY-LWFMISPVEQLLNLQYAYYAAG 336
Cdd:PRK10522 223 HHIIRA---------DTFHLSAvnwsnimMLgaigLVFYMANSLGwadtNVAATYSLtLLFLRTPLLSAVGALPTLLSAQ 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 337 GALTRINELLARADEPQYAGGAdPFTGRETvgIEVRGLNFGYGEE-LVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLL 415
Cdd:PRK10522 294 VAFNKLNKLALAPYKAEFPRPQ-AFPDWQT--LELRNVTFAYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLT 370

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 416 GLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQHPALFNDTVRANltmGRERSDQACWQALEIAQLDATVKalplgLDS 495
Cdd:PRK10522 371 GLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPE---GKPANPALVEKWLERLKMAHKLE-----LED 442

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 496 vvGR-SGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFL--SGRTTLIIAHRLSAVKQADRVL 572
Cdd:PRK10522 443 --GRiSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLqeMGKTIFAISHDDHYFIHADRLL 520

                        490
                 ....*....|....*....
gi 489309308 573 VFDGGHIAE-DGDHQQLIA 590
Cdd:PRK10522 521 EMRNGQLSElTGEERDAAS 539
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 369-588 3.10e-18

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 85.24  E-value: 3.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGY-GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVV 447
Cdd:PRK13652   4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHP--ALFNDTVRANLTMGrersdqACWQALEIAQLDATVKAL--PLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPK 523
Cdd:PRK13652  84 FQNPddQIFSPTVEQDIAFG------PINLGLDEETVAHRVSSAlhMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 524 VVILDEATSALDAATEYNLHQALARFLS--GRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQL 588
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 372-583 3.63e-18

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: 83.74  E-value: 3.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 372 RGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIrfggstqqeigleTIRENVSVVLQ-- 449
Cdd:cd03220   26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-------------TVRGRVSSLLGlg 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 450 ---HPALfndTVRANLT-----MGRERSD-----QACWQALEIAQ-LDATVKalplgldsvvgrsgvRFSGGQRQRLAIA 515
Cdd:cd03220   93 ggfNPEL---TGRENIYlngrlLGLSRKEidekiDEIIEFSELGDfIDLPVK---------------TYSSGMKARLAFA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 516 RMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIA-HRLSAVKQ-ADRVLVFDGGHIAEDG 583
Cdd:cd03220  155 IATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 369-591 4.53e-18

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: 83.75  E-value: 4.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEIGLETI----RENV 444
Cdd:cd03218    1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG---QDITKLPMhkraRLGI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 445 SVVLQHPALFND-TVRANLTMgrersdqacwqALEIAQLDAT-----VKAL--PLGLDSVVGRSGVRFSGGQRQRLAIAR 516
Cdd:cd03218   78 GYLPQEASIFRKlTVEENILA-----------VLEIRGLSKKereekLEELleEFHITHLRKSKASSLSGGERRRVEIAR 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 517 MVLAEPKVVILDEATSALDAATEYNLhQALARFLSGRT--TLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:cd03218  147 ALATNPKFLLLDEPFAGVDPIAVQDI-QKIIKILKDRGigVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAAN 223
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 369-537 4.65e-18

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: 82.79  E-value: 4.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEigLETIRENVSVVL 448
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE--QRDEPHENILYL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  449 QH-PALFND-TVRANLTMGRE---RSDQACWQALEIAqldatvkalplGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPK 523
Cdd:TIGR01189  79 GHlPGLKPElSALENLHFWAAihgGAQRTIEDALAAV-----------GLTGFEDLPAAQLSAGQQRRLALARLWLSRRP 147

                         170
                  ....*....|....
gi 489309308  524 VVILDEATSALDAA 537
Cdd:TIGR01189 148 LWILDEPTTALDKA 161
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 369-575 4.93e-18

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: 82.93  E-value: 4.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGlETIRENVSVVL 448
Cdd:cd03231    1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR-DSIARGLLYLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALFND-TVRANLT-MGRERSDQACWQALEIAQLDAtVKALPLGldsvvgrsgvRFSGGQRQRLAIARMVLAEPKVVI 526
Cdd:cd03231   80 HAPGIKTTlSVLENLRfWHADHSDEQVEEALARVGLNG-FEDRPVA----------QLSAGQQRRVALARLLLSGRPLWI 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489309308 527 LDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLSAVKQADRVLVFD 575
Cdd:cd03231  149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELD 197
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 378-583 7.52e-18

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: 83.15  E-value: 7.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 378 YGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGST--QQEIGLetiRENVSVVL-QHPALF 454
Cdd:cd03267   31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwKRRKKF---LRRIGVVFgQKTQLW 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 455 ND-TVRANLTMGRERSDqacwqaLEIAQLDATVKALP--LGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEAT 531
Cdd:cd03267  108 WDlPVIDSFYLLAAIYD------LPPARFKKRLDELSelLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 532 SALDAATEYNLHQALARF--LSGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDG 583
Cdd:cd03267  182 IGLDVVAQENIRNFLKEYnrERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
369-588 1.45e-17

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 82.89  E-value: 1.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGS---TQQEIGLETIRENVS 445
Cdd:PRK11831   8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipAMSRSRLYTVRKRMS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 446 VVLQHPALFND-TVRANLTMG-RERSdqacwqALEIAQLDATV--KALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAE 521
Cdd:PRK11831  88 MLFQSGALFTDmNVFDNVAYPlREHT------QLPAPLLHSTVmmKLEAVGLRGAAKLMPSELSGGMARRAALARAIALE 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 522 PKVVILDEATSALDAATE-------YNLHQALarflsGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQL 588
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMgvlvkliSELNSAL-----GVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
383-579 1.51e-17

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 84.51  E-value: 1.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 383 VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEigLETIRENVSVVLQHPALF-NDTVRAN 461
Cdd:PRK11650  19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE--LEPADRDIAMVFQNYALYpHMSVREN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 462 LTMG-----------RERSDQACwQALEIAQLdatvkalplgLDsvvgRSGVRFSGGQRQRLAIARMVLAEPKVVILDEA 530
Cdd:PRK11650  97 MAYGlkirgmpkaeiEERVAEAA-RILELEPL----------LD----RKPRELSGGQRQRVAMGRAIVREPAVFLFDEP 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 531 TSALDAATEYN-------LHQALarflsGRTTLIIAH-RLSAVKQADRVLVFDGGHI 579
Cdd:PRK11650 162 LSNLDAKLRVQmrleiqrLHRRL-----KTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
378-591 2.19e-17

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 81.85  E-value: 2.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 378 YGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGS--TQQEIGlETIRENVSVVLQHPALFN 455
Cdd:PRK11614  15 YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKdiTDWQTA-KIMREAVAIVPEGRRVFS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 456 D-TVRANLTMGRERSDQACWQaleiAQLDATVKALPLGLDSVVGRSGVrFSGGQRQRLAIARMVLAEPKVVILDEATSAL 534
Cdd:PRK11614  94 RmTVEENLAMGGFFAERDQFQ----ERIKWVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 535 DAATEYNLHQALARFLS-GRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:PRK11614 169 APIIIQQIFDTIEQLREqGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLAN 227
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 369-589 3.46e-17

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 81.67  E-value: 3.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEIGLETIRE---NVS 445
Cdd:COG4604    2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDG---LDVATTPSRElakRLA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 446 VVLQHPAlFND--TVRANLTMGR-----ERSDQACWQALE--IAQLDATvkalPLG---LDSVvgrsgvrfSGGQRQRLA 513
Cdd:COG4604   79 ILRQENH-INSrlTVRELVAFGRfpyskGRLTAEDREIIDeaIAYLDLE----DLAdryLDEL--------SGGQRQRAF 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 514 IArMVLA-EPKVVILDEATSALDAATEYNLHQALARFL--SGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLI 589
Cdd:COG4604  146 IA-MVLAqDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDINfASCYADHIVAMKDGRVVAQGTPEEII 224
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
369-605 3.73e-17

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 81.60  E-value: 3.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGS---IRFGGSTQQEIG-----LETI 440
Cdd:PRK09984   5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQREGrlardIRKS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 441 RENVSVVLQHPALFND-TVRANLTMGRERSD---QACWQALEIAQLDATVKALP-LGLDSVVGRSGVRFSGGQRQRLAIA 515
Cdd:PRK09984  85 RANTGYIFQQFNLVNRlSVLENVLIGALGSTpfwRTCFSWFTREQKQRALQALTrVGMVHFAHQRVSTLSGGQQQRVAIA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 516 RMVLAEPKVVILDEATSALDAATEYNLHQALARF--LSGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLiaDG 592
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF--DN 242

                        250
                 ....*....|...
gi 489309308 593 GLYAKLYGHLQQV 605
Cdd:PRK09984 243 ERFDHLYRSINRV 255
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 384-589 3.83e-17

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 84.67  E-value: 3.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRF--------GGSTQQEIGLETIRENVSVVlqhPALfn 455
Cdd:PRK10762  20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgkevtfnGPKSSQEAGIGIIHQELNLI---PQL-- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 456 dTVRANLTMGRE------RSDqacWQALeIAQLDATVKALPLGLDS--VVGrsgvRFSGGQRQRLAIARMVLAEPKVVIL 527
Cdd:PRK10762  95 -TIAENIFLGREfvnrfgRID---WKKM-YAEADKLLARLNLRFSSdkLVG----ELSIGEQQMVEIAKVLSFESKVIIM 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308 528 DEATSAL-DAATEynlhqALARFL-----SGRTTLIIAHRLSAVKQ-ADRVLVF-DGGHIAE----DGDHQQLI 589
Cdd:PRK10762 166 DEPTDALtDTETE-----SLFRVIrelksQGRGIVYISHRLKEIFEiCDDVTVFrDGQFIAErevaDLTEDSLI 234
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 374-590 4.41e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 81.68  E-value: 4.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 374 LNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTP-----QAGSIRFGG-STQQEIGLETIRENVSVV 447
Cdd:PRK14271  27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGrSIFNYRDVLEFRRRVGML 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALFNDTVRANLTMGRERSDQACWQALE-IAQLDATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVI 526
Cdd:PRK14271 107 FQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRgVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL 186

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 527 LDEATSALDAATEYNLHQALARFLSGRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
369-560 6.43e-17

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 79.46  E-value: 6.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqqeiglETIRENVSVVL 448
Cdd:PRK13538   2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG--------EPIRRQRDEYH 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 Q------HPALFND--TVRANLT----MGRERSDQACWQALEIAQL----DATVKALplgldsvvgrsgvrfSGGQRQRL 512
Cdd:PRK13538  74 QdllylgHQPGIKTelTALENLRfyqrLHGPGDDEALWEALAQVGLagfeDVPVRQL---------------SAGQQRRV 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489309308 513 AIARMVLAEPKVVILDEATSALDAateynlhQALARFlsgrTTLIIAH 560
Cdd:PRK13538 139 ALARLWLTRAPLWILDEPFTAIDK-------QGVARL----EALLAQH 175
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
 104-342 9.55e-17

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: 80.97  E-value: 9.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGI 183
Cdd:cd18545   55 VASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVII 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 184 LMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVRD 263
Cdd:cd18545  135 MFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRK 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 264 FAVNSQWKSDassrasglLFQFGIDIFRAAAMLTVLF--------SDLSIGQMLAVFSYLWFMISPVEQLLNLQYAYYAA 335
Cdd:cd18545  215 ANMRAVRLNA--------LFWPLVELISALGTALVYWyggklvlgGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSA 286


                 ....*..
gi 489309308 336 GGALTRI 342
Cdd:cd18545  287 MASAERI 293
cbiO PRK13645
energy-coupling factor transporter ATPase;
384-598 1.49e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 80.44  E-value: 1.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFG-----GSTQQEIGLETIRENVSVVLQHP--ALFND 456
Cdd:PRK13645  27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipANLKKIKEVKRLRKEIGLVFQFPeyQLFQE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 457 TVRANLTMGR----ERSDQACWQALEIAQLdatvKALPlglDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATS 532
Cdd:PRK13645 107 TIEKDIAFGPvnlgENKQEAYKKVPELLKL----VQLP---EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 533 ALDAATEYNLHQALARFLS--GRTTLIIAHRLSAV-KQADRVLVFDGGHIAEDGDHQQLIADGGLYAKL 598
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFSNQELLTKI 248
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 384-583 1.83e-16

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 82.98  E-value: 1.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGS---TQQEIGLETIRENVSVVLQHPALFNDTvra 460
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYASLDP--- 416

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 461 nltmgRERSDQACWQALEIAQL---DATVKALPLGLDSV------VGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEAT 531
Cdd:PRK10261 417 -----RQTVGDSIMEPLRVHGLlpgKAAAARVAWLLERVgllpehAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308 532 SALDAATE---YNLHQALARFLsGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDG 583
Cdd:PRK10261 492 SALDVSIRgqiINLLLDLQRDF-GIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
369-580 2.50e-16

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 82.14  E-value: 2.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIREN-VSVV 447
Cdd:PRK09700   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGII 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQHPALFND-TVRANLTMGRERSDQAC------WQALEI-AQLDATVKALPLGLDSVVGrsgvRFSGGQRQRLAIARMVL 519
Cdd:PRK09700  86 YQELSVIDElTVLENLYIGRHLTKKVCgvniidWREMRVrAAMMLLRVGLKVDLDEKVA----NLSISHKQMLEIAKTLM 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308 520 AEPKVVILDEATSAL-DAATEYNLhqALARFLSGRTTLI--IAHRLSAVKQ-ADRVLVF-DGGHIA 580
Cdd:PRK09700 162 LDAKVIIMDEPTSSLtNKEVDYLF--LIMNQLRKEGTAIvyISHKLAEIRRiCDRYTVMkDGSSVC 225
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 384-591 3.18e-16

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: 81.77  E-value: 3.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGS--IRFG--------------GSTQQEIGLetirenvsvV 447
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGdewvdmtkpgpdgrGRAKRYIGI---------L 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  448 LQHPALF-NDTVRANLT--MGRERSDqacwqalEIAQLDATVKALPLGLD-----SVVGRSGVRFSGGQRQRLAIARMVL 519
Cdd:TIGR03269 371 HQEYDLYpHRTVLDNLTeaIGLELPD-------ELARMKAVITLKMVGFDeekaeEILDKYPDELSEGERHRVALAQVLI 443

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308  520 AEPKVVILDEATSALDAATEYNLHQAL--ARFLSGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:TIGR03269 444 KEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 369-560 3.48e-16

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 81.91  E-value: 3.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGgstqqeiglETIRenVSVVL 448
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG---------ETVK--LAYVD 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  449 QhpalFNDTVRANLTMGRERSDqacwqALEIaqldatvkaLPLGLDSVVGRSGV-RF--------------SGGQRQRLA 513
Cdd:TIGR03719 392 Q----SRDALDPNKTVWEEISG-----GLDI---------IKLGKREIPSRAYVgRFnfkgsdqqkkvgqlSGGERNRVH 453

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 489309308  514 IARMVLAEPKVVILDEATSALDAATEYNLHQALARFlsGRTTLIIAH 560
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISH 498
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
 104-329 3.76e-16

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: 79.41  E-value: 3.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLvTDLDTVDKFVGETLSRFLVAMLTLVGTSGI 183
Cdd:cd18570   57 LLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGII 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 184 LMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQR----AQ 259
Cdd:cd18570  136 LFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKfsklLK 215

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 260 EVRDFAVNSQWKSDASSRASGLlfqFGIDIFRAAAMLtVLFSDLSIGQMLAVFSYLWFMISPVEQLLNLQ 329
Cdd:cd18570  216 KSFKLGKLSNLQSSIKGLISLI---GSLLILWIGSYL-VIKGQLSLGQLIAFNALLGYFLGPIENLINLQ 281
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 393-595 4.02e-16

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 81.63  E-value: 4.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  393 PGEKVAIVGASGGGKSTLVQLLLGLYTP---QAGSIRFGGstqQEIGLETIRENVSVVLQH----PALfndTVRANLT-M 464
Cdd:TIGR00955  50 PGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNG---MPIDAKEMRAISAYVQQDdlfiPTL---TVREHLMfQ 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  465 GRERSDQACWQALEIAQLDATVKALPLG--LDSVVGRSGVR--FSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEY 540
Cdd:TIGR00955 124 AHLRMPRRVTKKEKRERVDEVLQALGLRkcANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489309308  541 NLHQALARF-LSGRTTLIIAHRLSA--VKQADRVLVFDGGHIAEDGDHQQLI---ADGGLY 595
Cdd:TIGR00955 204 SVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVpffSDLGHP 264
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
377-589 6.84e-16

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 80.08  E-value: 6.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 377 GYGEELVLDQLNLN---------IAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRE----N 443
Cdd:PRK10070  28 GLSKEQILEKTGLSlgvkdaslaIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkK 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 444 VSVVLQHPALF-NDTVRANLTMGRERSDQACWQALEIAqLDATVKalpLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEP 522
Cdd:PRK10070 108 IAMVFQSFALMpHMTVLDNTAFGMELAGINAEERREKA-LDALRQ---VGLENYAHSYPDELSGGMRQRVGLARALAINP 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 523 KVVILDEATSALDAATEYNLHQALARFLSG--RTTLIIAHRL-SAVKQADRVLVFDGGHIAEDGDHQQLI 589
Cdd:PRK10070 184 DILLMDEAFSALDPLIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 369-583 9.84e-16

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 80.09  E-value: 9.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQ--------QEIGLeti 440
Cdd:PRK15439  12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltpakaHQLGI--- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 441 renvSVVLQHPALF-NDTVRANLTMG--RERSDQACWQALeIAQLDATvkalpLGLDSVVGRSGVrfsgGQRQRLAIARM 517
Cdd:PRK15439  89 ----YLVPQEPLLFpNLSVKENILFGlpKRQASMQKMKQL-LAALGCQ-----LDLDSSAGSLEV----ADRQIVEILRG 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 518 VLAEPKVVILDEATSALDAATEYNLHQALARFLS-GRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDG 583
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETERLFSRIRELLAqGVGIVFISHKLPEIRQlADRISVMRDGTIALSG 222
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 383-590 1.69e-15

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 79.36  E-value: 1.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 383 VLDQLNLNIAPGEKVAIVGASGGGKS-TLVQLLLGLYTPQA----GSIRFGGST---QQEIGLETIREN-VSVVLQHPAL 453
Cdd:PRK15134  24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESllhASEQTLRGVRGNkIAMIFQEPMV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 454 -FN--DTVRANLT--------MGRE--RSDQ-ACWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIARMVL 519
Cdd:PRK15134 104 sLNplHTLEKQLYevlslhrgMRREaaRGEIlNCLDRVGIRQAAKRLTDYPHQL-----------SGGERQRVMIAMALL 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308 520 AEPKVVILDEATSALDAATEYNLHQALARFLS--GRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 370-579 1.91e-15

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: 74.78  E-value: 1.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 370 EVRGLNFGygeeLVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEIGLETIRENVS---- 445
Cdd:cd03215    6 EVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG---KPVTRRSPRDAIRagia 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 446 ----------VVLQHPalfndtVRANLTMGRersdqacwqaleiaqldatvkalplgldsvvgrsgvRFSGGQRQRLAIA 515
Cdd:cd03215   79 yvpedrkregLVLDLS------VAENIALSS------------------------------------LLSGGNQQKVVLA 116

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308 516 RMVLAEPKVVILDEATSALDAATEYNLHQALARFLS-GRTTLIIAHRLSAVKQ-ADRVLVFDGGHI 579
Cdd:cd03215  117 RWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADaGKAVLLISSELDELLGlCDRILVMYEGRI 182
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
373-594 2.08e-15

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 76.58  E-value: 2.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 373 GLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGST--QQEIGLETIRENVSVVLQH 450
Cdd:PRK13638   6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldYSKRGLLALRQQVATVFQD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 451 P--ALFNDTVRANLTMGrersdqacWQALEIAQLDATVK---ALPLgldsvVGRSGVR------FSGGQRQRLAIARMVL 519
Cdd:PRK13638  86 PeqQIFYTDIDSDIAFS--------LRNLGVPEAEITRRvdeALTL-----VDAQHFRhqpiqcLSHGQKKRVAIAGALV 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 520 AEPKVVILDEATSALDAATEYNLHQALARFLS-GRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIADGGL 594
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAqGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTEA 229
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
 100-348 2.17e-15

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: 77.49  E-value: 2.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 100 CGALVFNVLQARLFARLAKDIVYRIRVRLIERLKR--ISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTL 177
Cdd:cd18578   63 IVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRqdIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTL 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 178 VGTSGILMWMHWKLALLILLFNPLVIYATVqlgKRVKHLKKLENDSTSRFTQA---LTETLDAIQEVRAGNRQGFFLGRL 254
Cdd:cd18578  143 VAGLIIAFVYGWKLALVGLATVPLLLLAGY---LRMRLLSGFEEKNKKAYEESskiASEAVSNIRTVASLTLEDYFLEKY 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 255 GQRAQEVRDFAVNsqwksdaSSRASGLLF---QFGIDIFRAAAML--TVLFSD--LSIGQMLAVFSYLWFMISPVEQLLN 327
Cdd:cd18578  220 EEALEEPLKKGLR-------RALISGLGFglsQSLTFFAYALAFWygGRLVANgeYTFEQFFIVFMALIFGAQSAGQAFS 292

                        250       260
                 ....*....|....*....|.
gi 489309308 328 LQYAYYAAGGALTRINELLAR 348
Cdd:cd18578  293 FAPDIAKAKAAAARIFRLLDR 313
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 112-308 2.80e-15

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: 76.75  E-value: 2.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 112 LFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGILMWMHWKL 191
Cdd:cd18575   59 LVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKL 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 192 ALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVRDFAVnsqwk 271
Cdd:cd18575  139 TLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAAL----- 213

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 489309308 272 sdASSRASGLLFQFGIdIFRAAAMLTVLF---SDLSIGQM 308
Cdd:cd18575  214 --RRIRARALLTALVI-FLVFGAIVFVLWlgaHDVLAGRM 250
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
 100-325 3.35e-15

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: 76.37  E-value: 3.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 100 CGALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGeTLSRFLVAMLTLVG 179
Cdd:cd18543   50 VAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 180 TSGILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQ 259
Cdd:cd18543  129 GLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAAR 208

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308 260 EVRdfavnsqwksDASSRASGLL--FQFGIDIFRAAAMLTVLF--------SDLSIGQMLAVFSYLWFMISPVEQL 325
Cdd:cd18543  209 RLR----------ATRLRAARLRarFWPLLEALPELGLAAVLAlggwlvanGSLTLGTLVAFSAYLTMLVWPVRML 274
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 377-591 3.96e-15

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 78.67  E-value: 3.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 377 GYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGS------IRFGGSTQQEigLETIRENVSvVLQH 450
Cdd:PRK10636 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEiglakgIKLGYFAQHQ--LEFLRADES-PLQH 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 451 PALFNDtvranltmgrersdqacwQALEiAQLDATVKALPLGLDSVVGRSGvRFSGGQRQRLAIARMVLAEPKVVILDEA 530
Cdd:PRK10636 398 LARLAP------------------QELE-QKLRDYLGGFGFQGDKVTEETR-RFSGGEKARLVLALIVWQRPNLLLLDEP 457

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308 531 TSALDAATEYNLHQALARFLSGrtTLIIAHRLSAVKQA--DRVLVFDGGHIAEDG---DHQQLIAD 591
Cdd:PRK10636 458 TNHLDLDMRQALTEALIDFEGA--LVVVSHDRHLLRSTtdDLYLVHDGKVEPFDGdleDYQQWLSD 521
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
379-579 4.73e-15

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 74.53  E-value: 4.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 379 GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG---STQQEIGLETIRENVSVVLQ-HPALF 454
Cdd:PRK10908  13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdiTRLKNREVPFLRRQIGMIFQdHHLLM 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 455 NDTVRANLTM-----GRERSD--QACWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRLAIARMVLAEPKVVIL 527
Cdd:PRK10908  93 DRTVYDNVAIpliiaGASGDDirRRVSAALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVLLA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489309308 528 DEATSALDAATEYNLHQALARF-LSGRTTLIIAHRLSAVKQAD-RVLVFDGGHI 579
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 365-582 5.56e-15

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 74.22  E-value: 5.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 365 ETVGIEVRGLnfgygEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFggstqqEIGLETIRENV 444
Cdd:COG2401   32 EAFGVELRVV-----ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV------DVPDNQFGREA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 445 SVVLQHPAL--FNDTVRANLTMGreRSDQACWQaleiaqldATVKALplgldsvvgrsgvrfSGGQRQRLAIARMVLAEP 522
Cdd:COG2401  101 SLIDAIGRKgdFKDAVELLNAVG--LSDAVLWL--------RRFKEL---------------STGQKFRFRLALLLAERP 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 523 KVVILDEATSALDAATEYNLHQALARFL--SGRTTLIIAHRLSAVK--QADRVLVFD-GGHIAED 582
Cdd:COG2401  156 KLLVIDEFCSHLDRQTAKRVARNLQKLArrAGITLVVATHHYDVIDdlQPDLLIFVGyGGVPEEK 220
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 360-595 9.15e-15

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 76.99  E-value: 9.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 360 PFTGRETVgIEVRGLNF-GYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEIGLE 438
Cdd:COG3845  250 PAEPGEVV-LEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG---EDITGL 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 439 TIRE----NVSVV----LQHpALFND-TVRANLTMGRERSDQAC------WQALE------IAQLDatVKAlPlGLDSVV 497
Cdd:COG3845  326 SPRErrrlGVAYIpedrLGR-GLVPDmSVAENLILGRYRRPPFSrggfldRKAIRafaeelIEEFD--VRT-P-GPDTPA 400

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 498 GrsgvRFSGGQRQRLAIARMVLAEPKVVILDEATSALD-AATEYnLHQAL--ARfLSGRTTLIIAHRLSAVKQ-ADRVLV 573
Cdd:COG3845  401 R----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDvGAIEF-IHQRLleLR-DAGAAVLLISEDLDEILAlSDRIAV 474

                        250       260
                 ....*....|....*....|....*..
gi 489309308 574 FDGGHI-----AEDGDHQQLiadgGLY 595
Cdd:COG3845  475 MYEGRIvgevpAAEATREEI----GLL 497
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 384-582 1.16e-14

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 76.89  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYtPQA---GSIRFGGSTQQEIGL-ETIRENVSVVLQHPALFND-TV 458
Cdd:PRK13549  21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIrDTERAGIAIIHQELALVKElSV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 459 RANLTMGRE-----RSD-----QACWQALEIAQLDATVkALPLGldsvvgrsgvRFSGGQRQRLAIARMVLAEPKVVILD 528
Cdd:PRK13549 100 LENIFLGNEitpggIMDydamyLRAQKLLAQLKLDINP-ATPVG----------NLGLGQQQLVEIAKALNKQARLLILD 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 529 EATSALDAA-TEYNLHqaLARFLS--GRTTLIIAHRLSAVKQ-ADRVLVF-DGGHIAED 582
Cdd:PRK13549 169 EPTASLTESeTAVLLD--IIRDLKahGIACIYISHKLNEVKAiSDTICVIrDGRHIGTR 225
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 369-580 1.36e-14

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: 76.40  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYtPQA---GSIRFGGSTQQEIGL-ETIRENV 444
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIrDTERAGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  445 SVVLQHPALFND-TVRANLTMGRE------RSDQA-----CWQALEIAQLDATVKALPLGldsvvgrsgvRFSGGQRQRL 512
Cdd:TIGR02633  81 VIIHQELTLVPElSVAENIFLGNEitlpggRMAYNamylrAKNLLRELQLDADNVTRPVG----------DYGGGQQQLV 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308  513 AIARMVLAEPKVVILDEATSALDAAtEYNLHQALARFLS--GRTTLIIAHRLSAVKQ-ADRVLVF-DGGHIA 580
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEK-ETEILLDIIRDLKahGVACVYISHKLNEVKAvCDTICVIrDGQHVA 221
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 390-576 1.66e-14

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 73.60  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 390 NIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIrfggstqqeiglETIRENVSVVLQH-PALFNDTVRANLtmgRER 468
Cdd:cd03237   21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI------------EIELDTVSYKPQYiKADYEGTVRDLL---SSI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 469 SDQACWQAL---EIAQldatvkalPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQA 545
Cdd:cd03237   86 TKDFYTHPYfktEIAK--------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489309308 546 LARFL--SGRTTLIIAHR-LSAVKQADRVLVFDG 576
Cdd:cd03237  158 IRRFAenNEKTAFVVEHDiIMIDYLADRLIVFEG 191
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 387-588 1.68e-14

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 74.76  E-value: 1.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 387 LNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQ---AGSIRFGGS---TQQEIGLETIR-ENVSVVLQHPAL-FNDTV 458
Cdd:PRK09473  35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGReilNLPEKELNKLRaEQISMIFQDPMTsLNPYM 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 459 R-----ANLTMGRERSDQAcwQALE--IAQLDAtVKaLPlgldsvVGRSGVR-----FSGGQRQRLAIARMVLAEPKVVI 526
Cdd:PRK09473 115 RvgeqlMEVLMLHKGMSKA--EAFEesVRMLDA-VK-MP------EARKRMKmypheFSGGMRQRVMIAMALLCRPKLLI 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 527 LDEATSALDA---ATEYNLHQALARFLSgrTTLI-IAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQL 588
Cdd:PRK09473 185 ADEPTTALDVtvqAQIMTLLNELKREFN--TAIImITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV 249
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 369-571 2.59e-14

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 72.95  E-value: 2.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQL---LLGLyTPQA---GSIRFGGST--QQEIGLETI 440
Cdd:PRK14267   5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLEL-NEEArveGEVRLFGRNiySPDVDPIEV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 441 RENVSVVLQHPALF-NDTVRANLTMG---------RERSDQACWQALEIAQLDATVKalplglDSVVGRSGvRFSGGQRQ 510
Cdd:PRK14267  84 RREVGMVFQYPNPFpHLTIYDNVAIGvklnglvksKKELDERVEWALKKAALWDEVK------DRLNDYPS-NLSGGQRQ 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489309308 511 RLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIAHrlsAVKQADRV 571
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH---SPAQAARV 214
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 391-576 2.61e-14

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 75.98  E-value: 2.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 391 IAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRfggstqqeiglETIRenVSVVLQH-PALFNDTVRANLTMGRERS 469
Cdd:COG1245  363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-----------EDLK--ISYKPQYiSPDYDGTVEEFLRSANTDD 429

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 470 DQACWQALEIAQldatvkalPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARF 549
Cdd:COG1245  430 FGSSYYKTEIIK--------PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF 501

                        170       180       190
                 ....*....|....*....|....*....|
gi 489309308 550 L--SGRTTLIIAHRLSAVKQ-ADRVLVFDG 576
Cdd:COG1245  502 AenRGKTAMVVDHDIYLIDYiSDRLMVFEG 531
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 369-584 2.90e-14

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 72.75  E-value: 2.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLG--LYTPQAGSIRFGGSTQQEIGLEtIRENVSV 446
Cdd:CHL00131   8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPE-ERAHLGI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VL--QHPALFN-----DTVRANLTMGRERSDQACWQALEIAQLdaTVKALPL-GLDSVVGRSGVR--FSGGQRQRLAIAR 516
Cdd:CHL00131  87 FLafQYPIEIPgvsnaDFLRLAYNSKRKFQGLPELDPLEFLEI--INEKLKLvGMDPSFLSRNVNegFSGGEKKRNEILQ 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489309308 517 MVLAEPKVVILDEATSALDAATEYNLHQALARFL-SGRTTLIIAH--RLSAVKQADRVLVFDGGHIAEDGD 584
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 368-584 2.90e-14

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 72.81  E-value: 2.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 368 GIEVRGLNFGYGEELVlDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTP----QAGSIRFGGstqQEIGLETIR-E 442
Cdd:PRK10418   4 QIELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDG---KPVAPCALRgR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 443 NVSVVLQHP-ALFN--DTVRAN-----LTMGRERSDQACWQALEIAQLDATvkalplglDSVVGRSGVRFSGGQRQRLAI 514
Cdd:PRK10418  80 KIATIMQNPrSAFNplHTMHTHaretcLALGKPADDATLTAALEAVGLENA--------ARVLKLYPFEMSGGMLQRMMI 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308 515 ARMVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRT--TLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGD 584
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGD 224
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 384-595 4.75e-14

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 73.58  E-value: 4.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGST--QQEIGLetiRENVSVVL-Q-------HPAL 453
Cdd:COG4586   38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfKRRKEF---ARRIGVVFgQrsqlwwdLPAI 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 454 fnDTVRANLTMGRersdqacwqaLEIAQLDATVKALP--LGLDSVVGRSgVR-FSGGQRQRLAIARMVLAEPKVVILDEA 530
Cdd:COG4586  115 --DSFRLLKAIYR----------IPDAEYKKRLDELVelLDLGELLDTP-VRqLSLGQRMRCELAAALLHRPKILFLDEP 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 531 TSALDAATEYNLHQALARFLSGR-TTLIIA-HRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIADGGLY 595
Cdd:COG4586  182 TIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPY 249
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 369-577 4.91e-14

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: 71.16  E-value: 4.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQ------------EIG 436
Cdd:cd03269    1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiaarnrigylpeERG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 437 L---ETIRENVSVVLQHPALFNDTVRANLTMGRERSDQACWQALEIAQLdatvkalplgldsvvgrsgvrfSGGQRQRLA 513
Cdd:cd03269   81 LypkMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEEL----------------------SKGNQQKVQ 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 514 IARMVLAEPKVVILDEATSALDAATEYNLHQA---LARflSGRTTLIIAHRLSAVKQ-ADRVLVFDGG 577
Cdd:cd03269  139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVireLAR--AGKTVILSTHQMELVEElCDRVLLLNKG 204
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
384-590 4.91e-14

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 74.95  E-value: 4.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQ--------EIGLETIRENVSVVlqhPALfn 455
Cdd:PRK11288  20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfasttaalAAGVAIIYQELHLV---PEM-- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 456 dTVRANLTMGR--------ERSDQACWQALEIAQLDATVK-ALPLGldsvvgrsgvRFSGGQRQRLAIARMVLAEPKVVI 526
Cdd:PRK11288  95 -TVAENLYLGQlphkggivNRRLLNYEAREQLEHLGVDIDpDTPLK----------YLSIGQRQMVEIAKALARNARVIA 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 527 LDEATSALDAATEYNLHQALARFLS-GRTTLIIAHRLSAVKQ-ADRVLVF-DGGHIA-----EDGDHQQLIA 590
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAeGRVILYVSHRMEEIFAlCDAITVFkDGRYVAtfddmAQVDRDQLVQ 235
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 381-576 1.28e-13

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: 74.01  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  381 ELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGL--------YTPQAGSIrFGGSTQQEIGLETIRENVSvvlqHPA 452
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKL-FYVPQRPYMTLGTLRDQII----YPD 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  453 LFNDTVRanltmgRERSDQACWQALEIAQLDATVKAlPLGLDSVVGRSGVrFSGGQRQRLAIARMVLAEPKVVILDEATS 532
Cdd:TIGR00954 540 SSEDMKR------RGLSDKDLEQILDNVQLTHILER-EGGWSAVQDWMDV-LSGGEKQRIAMARLFYHKPQFAILDECTS 611

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 489309308  533 ALDAATEYNLHQALARFlsGRTTLIIAHRLSAVKQADRVLVFDG 576
Cdd:TIGR00954 612 AVSVDVEGYMYRLCREF--GITLFSVSHRKSLWKYHEYLLYMDG 653
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 369-585 1.37e-13

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 70.98  E-value: 1.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGL--YTPQAGSIRFGGSTQQEIGLET-IRENVS 445
Cdd:PRK09580   2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDrAGEGIF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 446 VVLQHPA--------LFNDTvraNLTMGRERSDQACWQALEIAQL-DATVKALPLGLDSVVGRSGVRFSGGQRQRLAIAR 516
Cdd:PRK09580  82 MAFQYPVeipgvsnqFFLQT---ALNAVRSYRGQEPLDRFDFQDLmEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQ 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 517 MVLAEPKVVILDEATSALDAATEYNLHQALARFLSGRTTLIIA---HRLSAVKQADRVLVFDGGHIAEDGDH 585
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDF 230
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 104-263 1.86e-13

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: 71.44  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGI 183
Cdd:cd18565   69 LFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAI 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 184 LMWMHWKLALLILLFNPLVIYATVQLGKRV--KHLKKLEndSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEV 261
Cdd:cd18565  149 LFYLNWQLALVALLPVPLIIAGTYWFQRRIepRYRAVRE--AVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEY 226


                 ..
gi 489309308 262 RD 263
Cdd:cd18565  227 RD 228
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
391-576 2.04e-13

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 72.92  E-value: 2.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 391 IAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIrfggstqqeigLETIRenVSVVLQH-PALFNDTVRANLTMGRERS 469
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-----------DPELK--ISYKPQYiKPDYDGTVEDLLRSITDDL 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 470 DQACWQAlEIAQldatvkalPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARF 549
Cdd:PRK13409 429 GSSYYKS-EIIK--------PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRI 499

                        170       180       190
                 ....*....|....*....|....*....|
gi 489309308 550 L--SGRTTLIIAHRLSAVKQ-ADRVLVFDG 576
Cdd:PRK13409 500 AeeREATALVVDHDIYMIDYiSDRLMVFEG 529
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 369-569 3.07e-13

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 68.82  E-value: 3.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEiGLETIRENVSVVL 448
Cdd:PRK13540   2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHPALF-NDTVRANLTMGRERSDqacwQALEIAQLdATVKALPLGLDSVVGrsgvRFSGGQRQRLAIARMVLAEPKVVIL 527
Cdd:PRK13540  81 HRSGINpYLTLRENCLYDIHFSP----GAVGITEL-CRLFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAKLWLL 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489309308 528 DEATSALDA-ATEYNLHQALARFLSGRTTLIIAHRLSAVKQAD 569
Cdd:PRK13540 152 DEPLVALDElSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 368-591 3.44e-13

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 69.29  E-value: 3.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 368 GIEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEIGLETI----REN 443
Cdd:COG1137    3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG---EDITHLPMhkraRLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 444 VSVVLQHPALFND-TVRANLTMgrersdqacwqALEIAQLDAT-----VKAL--PLGLDSVVGRSGVRFSGGQRQRLAIA 515
Cdd:COG1137   80 IGYLPQEASIFRKlTVEDNILA-----------VLELRKLSKKereerLEELleEFGITHLRKSKAYSLSGGERRRVEIA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 516 RMVLAEPKVVILDEATSALD--AATEYnlhQALARFLSGR--TTLIIAHR----LSAVkqaDRVLVFDGGHIAEDGDHQQ 587
Cdd:COG1137  149 RALATNPKFILLDEPFAGVDpiAVADI---QKIIRHLKERgiGVLITDHNvretLGIC---DRAYIISEGKVLAEGTPEE 222


                 ....
gi 489309308 588 LIAD 591
Cdd:COG1137  223 ILNN 226
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 369-560 4.79e-13

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 71.69  E-value: 4.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGgstqqeiglETIRenVSVVL 448
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG---------ETVK--LAYVD 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 449 QHpalfndtvRANLTmgrerSDQACWQalEIAQldatvkalplGLDSV-VGRSGV-------RF--------------SG 506
Cdd:PRK11819 394 QS--------RDALD-----PNKTVWE--EISG----------GLDIIkVGNREIpsrayvgRFnfkggdqqkkvgvlSG 448

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489309308 507 GQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFlSGrTTLIIAH 560
Cdd:PRK11819 449 GERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEF-PG-CAVVISH 500
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 369-590 6.13e-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: 71.37  E-value: 6.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGL--YTPQAGSIRF------------------- 427
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskvge 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  428 -----GGS-TQQEIGL--------ETIRENVSVVLQHP-ALF-NDTVRANLTMGRE----RSDQACWQALE-IAQLDATV 486
Cdd:TIGR03269  81 pcpvcGGTlEPEEVDFwnlsdklrRRIRKRIAIMLQRTfALYgDDTVLDNVLEALEeigyEGKEAVGRAVDlIEMVQLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  487 KALPLGLDsvvgrsgvrFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFL--SGRTTLIIAHRLSA 564
Cdd:TIGR03269 161 RITHIARD---------LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEV 231

                         250       260
                  ....*....|....*....|....*..
gi 489309308  565 VKQ-ADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:TIGR03269 232 IEDlSDKAIWLENGEIKEEGTPDEVVA 258
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 387-592 6.50e-13

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 68.81  E-value: 6.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 387 LNLNIAPGEKVAIVGASGGGKSTLVQLLLGLyTPQAGSIRFGG-STQQEIGLETIRENVSVVLQHPALFNDTVranltmg 465
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGqPLEAWSAAELARHRAYLSQQQTPPFAMPV------- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 466 rersdqacWQALEI-----AQLDATVKALP-----LGLDSVVGRSGVRFSGG--QRQRLA-----IARMVLAEPKVVILD 528
Cdd:PRK03695  87 --------FQYLTLhqpdkTRTEAVASALNevaeaLGLDDKLGRSVNQLSGGewQRVRLAavvlqVWPDINPAGQLLLLD 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308 529 EATSALDAATEYNLHQALARFLS-GRTTLIIAHRLS-AVKQADRVLVFDGGhiaedgdhqQLIADG 592
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCQqGIAVVMSSHDLNhTLRHADRVWLLKQG---------KLLASG 215
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 383-560 7.22e-13

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 71.12  E-value: 7.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  383 VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFG-----GSTQQEIGLE---TIRENVSVVLQH-PAL 453
Cdd:TIGR03719  20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpgikvGYLPQEPQLDptkTVRENVEEGVAEiKDA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  454 FN--DTVRANLT------------MGRERSDQACWQALEI-AQLDATVKAL--PLGlDSVVGRsgvrFSGGQRQRLAIAR 516
Cdd:TIGR03719 100 LDrfNEISAKYAepdadfdklaaeQAELQEIIDAADAWDLdSQLEIAMDALrcPPW-DADVTK----LSGGERRRVALCR 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 489309308  517 MVLAEPKVVILDEATSALDAATEYNLHQALARFlSGrTTLIIAH 560
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTH 216
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
 100-312 7.80e-13

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: 69.43  E-value: 7.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 100 CGALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVG 179
Cdd:cd18577   58 IGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIA 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 180 TSGILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQ 259
Cdd:cd18577  138 GFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALE 217

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308 260 EVRDFAVnsqWKSDASSRASGLLFqFGIDIFRAAAML--TVLFSD--LSIGQMLAVF 312
Cdd:cd18577  218 KARKAGI---KKGLVSGLGLGLLF-FIIFAMYALAFWygSRLVRDgeISPGDVLTVF 270
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
 120-336 2.11e-12

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: 68.25  E-value: 2.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 120 IVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGILMWMHWKLALLILLFN 199
Cdd:cd18549   73 IETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALL 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 200 PLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFflgrlgqraqEVRDFAVNSQWKSDASSRA- 278
Cdd:cd18549  153 PLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEY----------EIEKFDEGNDRFLESKKKAy 222

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 279 -SGLLFQFGIDIFRAAAMLTVLF--------SDLSIGQMLAVFSYLWFMISPVEQLLNL--QYAYYAAG 336
Cdd:cd18549  223 kAMAYFFSGMNFFTNLLNLVVLVaggyfiikGEITLGDLVAFLLYVNVFIKPIRRLVNFteQYQKGMAG 291
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
370-580 3.14e-12

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 68.89  E-value: 3.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 370 EVRGLNFGYgeelVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG------STQQEI-------- 435
Cdd:COG1129  258 EVEGLSVGG----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpvrirSPRDAIragiayvp 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 436 ------GL---ETIRENVSVvlqhPALFNDTVRANLTMGRERSDqacwqALE-IAQLDatVKALplGLDSVVGRsgvrFS 505
Cdd:COG1129  334 edrkgeGLvldLSIRENITL----ASLDRLSRGGLLDRRRERAL-----AEEyIKRLR--IKTP--SPEQPVGN----LS 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 506 GGQRQRLAIARMVLAEPKVVILDEATSALD--AATE-YNLHQALARflSGRTTLII------AHRLSavkqaDRVLVFDG 576
Cdd:COG1129  397 GGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAEiYRLIRELAA--EGKAVIVIsselpeLLGLS-----DRILVMRE 469


                 ....
gi 489309308 577 GHIA 580
Cdd:COG1129  470 GRIV 473
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 370-587 3.41e-12

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 69.21  E-value: 3.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 370 EVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGgsTQQEIGL-----------E 438
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG--TKLEVAYfdqhraeldpeK 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 439 TIRENVSVVLQhpalfndTVRANltmGRERSDQACWQALEIAQLDAT--VKALplgldsvvgrsgvrfSGGQRQRLAIAR 516
Cdd:PRK11147 399 TVMDNLAEGKQ-------EVMVN---GRPRHVLGYLQDFLFHPKRAMtpVKAL---------------SGGERNRLLLAR 453

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 517 MVLAEPKVVILDEATSALDAATEYNLHQALARFlSGrTTLIIAHrlsavkqaDRVLV---------FDG-GHIAE----- 581
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVETLELLEELLDSY-QG-TVLLVSH--------DRQFVdntvtecwiFEGnGKIGRyvggy 523


                 ....*..
gi 489309308 582 -DGDHQQ 587
Cdd:PRK11147 524 hDARQQQ 530
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
 104-325 4.38e-12

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: 67.05  E-value: 4.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGI 183
Cdd:cd18541   55 IFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVM 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 184 LMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVRD 263
Cdd:cd18541  135 MFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVE 214

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 264 favnsqwKSDASSRASGLLFQFgIDIFRAAAMLTVLF--------SDLSIGQMLAVFSYLWFMISPVEQL 325
Cdd:cd18541  215 -------KNLRLARVDALFFPL-IGLLIGLSFLIVLWyggrlvirGTITLGDLVAFNSYLGMLIWPMMAL 276
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
 115-327 4.47e-12

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: 67.06  E-value: 4.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 115 RLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGILMWMHWKLALL 194
Cdd:cd18554   72 WIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFV 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 195 ILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRA-----------GNRQGFFLGR-LGQRAQEVR 262
Cdd:cd18554  152 SLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSfalekheqkqfDKRNGHFLTRaLKHTRWNAK 231

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308 263 DFA-VNSqwksdassrasglLFQFGIDIFRAAAMLTVLFSDLSIGQMLAVFSYLWFMISPVEQLLN 327
Cdd:cd18554  232 TFSaVNT-------------ITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVN 284
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 387-580 7.00e-12

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 68.15  E-value: 7.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 387 LNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG------STQQEI--------------GL---ETIREN 443
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGkeinalSTAQRLarglvylpedrqssGLyldAPLAWN 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 444 VSVVLQH-PALFNDTVRANLTMGRERsdqacwQALEI--AQLDATVKALplgldsvvgrsgvrfSGGQRQRLAIARMVLA 520
Cdd:PRK15439 362 VCALTHNrRGFWIKPARENAVLERYR------RALNIkfNHAEQAARTL---------------SGGNQQKVLIAKCLEA 420

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308 521 EPKVVILDEATSALDAATEYNLHQaLARFLSGRTT--LIIAHRLSAVKQ-ADRVLVFDGGHIA 580
Cdd:PRK15439 421 SPQLLIVDEPTRGVDVSARNDIYQ-LIRSIAAQNVavLFISSDLEEIEQmADRVLVMHQGEIS 482
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 369-557 7.60e-12

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 67.99  E-value: 7.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGgstqqeigletirENVSV-- 446
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS-------------ENANIgy 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 -VLQHPALFNDTVraNLT--MGRERSDQACWQALEiaqldATVKALPLGLDSvVGRSGVRFSGGQRQRLAIARMVLAEPK 523
Cdd:PRK15064 387 yAQDHAYDFENDL--TLFdwMSQWRQEGDDEQAVR-----GTLGRLLFSQDD-IKKSVKVLSGGEKGRMLFGKLMMQKPN 458

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489309308 524 VVILDEATSALDAATEYNLHQALARFlsgRTTLI 557
Cdd:PRK15064 459 VLVMDEPTNHMDMESIESLNMALEKY---EGTLI 489
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
 120-337 1.06e-11

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: 66.00  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 120 IVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGILMWMHWKLALLILLFN 199
Cdd:cd18573   72 IVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVV 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 200 PLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVRDFAvnsqwKSDAssRAS 279
Cdd:cd18573  152 PPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLA-----KKEA--LAS 224

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 280 GLLF---QFGIDifraAAMLTVLF--------SDLSIGQMLAvfsylwFMIspveqllnlqYAYYAAGG 337
Cdd:cd18573  225 GLFFgstGFSGN----LSLLSVLYyggslvasGELTVGDLTS------FLM----------YAVYVGSS 273
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 377-579 1.17e-11

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: 64.21  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 377 GYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLL---LGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQ--HP 451
Cdd:cd03233   16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEdvHF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 452 ALFndTVRanltmgrersdqacwQALEIAqldatvkALPLGLDSVVGrsgvrFSGGQRQRLAIARMVLAEPKVVILDEAT 531
Cdd:cd03233   96 PTL--TVR---------------ETLDFA-------LRCKGNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNST 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489309308 532 SALDAATEYNLHQALaRFLS---GRTTLIIAHRLS--AVKQADRVLVFDGGHI 579
Cdd:cd03233  147 RGLDSSTALEILKCI-RTMAdvlKTTTFVSLYQASdeIYDLFDKVLVLYEGRQ 198
GguA NF040905
sugar ABC transporter ATP-binding protein;
384-579 1.40e-11

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 67.12  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYtPQA---GSIRFGGSTQQeigLETIR--ENVSVVLQH------PA 452
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVCR---FKDIRdsEALGIVIIHqelaliPY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 453 LfndTVRANLTMGRERSDQAC--WQA--LEIAQLDATVkalplGL----DSVVGRSGVrfsgGQRQRLAIARMVLAEPKV 524
Cdd:NF040905  93 L---SIAENIFLGNERAKRGVidWNEtnRRARELLAKV-----GLdespDTLVTDIGV----GKQQLVEIAKALSKDVKL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 525 VILDEATSALDAATEYNLHQALARFLS-GRTTLIIAHRLSAVKQ-ADRVLVF-DGGHI 579
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAqGITSIIISHKLNEIRRvADSITVLrDGRTI 218
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
371-600 1.98e-11

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 64.81  E-value: 1.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 371 VRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQH 450
Cdd:PRK10575  14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 451 -PALFNDTVRANLTMGRERSDQACWQaLEIAQLDATVKALPL-GLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILD 528
Cdd:PRK10575  94 lPAAEGMTVRELVAIGRYPWHGALGR-FGAADREKVEEAISLvGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 529 EATSALDAAteynlHQ----ALARFLS---GRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDGDHQQLIaDGGLYAKLYG 600
Cdd:PRK10575 173 EPTSALDIA-----HQvdvlALVHRLSqerGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM-RGETLEQIYG 246
PLN03211 PLN03211
ABC transporter G-25; Provisional
 380-577 2.29e-11

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 66.83  E-value: 2.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 380 EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLlglytpqAGSIR---FGGSTQQEIGLET--IRENVSVVLQHPALF 454
Cdd:PLN03211  80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQgnnFTGTILANNRKPTkqILKRTGFVTQDDILY 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 455 -NDTVRANLTM-GRERSDQACWQALEIAQLDATVKALPLGL--DSVVGRSGVR-FSGGQRQRLAIARMVLAEPKVVILDE 529
Cdd:PLN03211 153 pHLTVRETLVFcSLLRLPKSLTKQEKILVAESVISELGLTKceNTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDE 232

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489309308 530 ATSALDAATEYNLHQALARFLS-GRTTLIIAHRLSA-VKQA-DRVLVFDGG 577
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQkGKTIVTSMHQPSSrVYQMfDSVLVLSEG 283
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 384-534 2.38e-11

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 66.29  E-value: 2.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqQEIGLETIRE----NVSVVLQHPALFND-TV 458
Cdd:PRK10982  14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFKSSKEalenGISMVHQELNLVLQrSV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 459 RANLTMGRE-------------RSDQACWQALEIaQLDATVKALPLgldsvvgrsgvrfSGGQRQRLAIARMVLAEPKVV 525
Cdd:PRK10982  91 MDNMWLGRYptkgmfvdqdkmyRDTKAIFDELDI-DIDPRAKVATL-------------SVSQMQMIEIAKAFSYNAKIV 156


                 ....*....
gi 489309308 526 ILDEATSAL 534
Cdd:PRK10982 157 IMDEPTSSL 165
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 371-588 2.86e-11

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 66.42  E-value: 2.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 371 VRGLNFGYGEEL----VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG-------------STQQ 433
Cdd:PRK10261  15 VENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvielSEQS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 434 EIGLETIR-ENVSVVLQHPAL-----------FNDTVRANLTMGRERSDQACWQALEIAQLDATvkalplglDSVVGRSG 501
Cdd:PRK10261  95 AAQMRHVRgADMAMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVEAKRMLDQVRIPEA--------QTILSRYP 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 502 VRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQaLARFLSGRTTL---IIAHRLSAVKQ-ADRVLVFDGG 577
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ-LIKVLQKEMSMgviFITHDMGVVAEiADRVLVMYQG 245

                        250
                 ....*....|.
gi 489309308 578 HIAEDGDHQQL 588
Cdd:PRK10261 246 EAVETGSVEQI 256
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
 100-327 7.72e-11

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: 63.33  E-value: 7.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 100 CGALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVG 179
Cdd:cd18572   47 VLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVG 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 180 TSGILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAgnrqgfflgrLGQRAQ 259
Cdd:cd18572  127 GLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRS----------FATEER 196

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 260 EVRDFAVNSQ-WKSDASSRAS-GLLFQFGIDIFRAAAMLTVLF--------SDLSIGQMLAVFSYLWFMISPVEQLLN 327
Cdd:cd18572  197 EARRYERALDkALKLSVRQALaYAGYVAVNTLLQNGTQVLVLFygghlvlsGRMSAGQLVTFMLYQQQLGEAFQSLGD 274
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 383-560 1.67e-10

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 63.60  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 383 VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFG-----GSTQQEIGLE---TIRENVSVVLQH--PA 452
Cdd:PRK11819  22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApgikvGYLPQEPQLDpekTVRENVEEGVAEvkAA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 453 L--FNDtVRANLTMGRERSD-----QACWQA-------------LEIAqLDAtvkalpLGL---DSVVGRsgvrFSGGQR 509
Cdd:PRK11819 102 LdrFNE-IYAAYAEPDADFDalaaeQGELQEiidaadawdldsqLEIA-MDA------LRCppwDAKVTK----LSGGER 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489309308 510 QRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFlSGrTTLIIAH 560
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY-PG-TVVAVTH 218
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
368-606 2.04e-10

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 62.83  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 368 GIEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGG--KSTLVQLLLGlytPQAGS--IRFGGSTQQEIGLE-TIRE 442
Cdd:NF000106  13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRrpWRF*TWCANRRALRrTIG* 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 443 NVSVVLQHPALFNDtvRANLTM-GRErsdqacwqaLEIAQLDATVKALPL----GLDSVVGRSGVRFSGGQRQRLAIARM 517
Cdd:NF000106  90 HRPVR*GRRESFSG--RENLYMiGR*---------LDLSRKDARARADELlerfSLTEAAGRAAAKYSGGMRRRLDLAAS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 518 VLAEPKVVILDEATSALDAATEYNLHQALARFL-SGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQliadggLY 595
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDE------LK 232

                        250
                 ....*....|.
gi 489309308 596 AKLYGHLQQVR 606
Cdd:NF000106 233 TKVGGRTLQIR 243
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 380-588 2.09e-10

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 61.60  E-value: 2.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 380 EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLL---LGLYTPQA---GSIRFGGSTQQEIGLETIRENVSVVLQHPAL 453
Cdd:PRK14246  22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlIEIYDSKIkvdGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 454 F-NDTVRANLTMgrERSDQACWQALEIAQL-DATVKALPL--GLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDE 529
Cdd:PRK14246 102 FpHLSIYDNIAY--PLKSHGIKEKREIKKIvEECLRKVGLwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 530 ATSALDAATEYNLHQALARFLSGRTTLIIAHR-LSAVKQADRVLVFDGGHIAEDGDHQQL 588
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVEWGSSNEI 239
hmuV PRK13547
heme ABC transporter ATP-binding protein;
383-583 2.12e-10

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 61.77  E-value: 2.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 383 VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQA--------GSIRFGGSTQQEIGLETIRENVSVVLQ--HPA 452
Cdd:PRK13547  16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQPA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 453 lFNDTVRANLTMGR-----------ERSDQACWQALEIAqldatvkalplGLDSVVGRSGVRFSGGQRQRLAIARmVLAE 521
Cdd:PRK13547  96 -FAFSAREIVLLGRypharragaltHRDGEIAWQALALA-----------GATALVGRDVTTLSGGELARVQFAR-VLAQ 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308 522 ----------PKVVILDEATSALDAATEYNLH---QALARFLSgRTTLIIAHRLS-AVKQADRVLVFDGGHIAEDG 583
Cdd:PRK13547 163 lwpphdaaqpPRYLLLDEPTAALDLAHQHRLLdtvRRLARDWN-LGVLAIVHDPNlAARHADRIAMLADGAIVAHG 237
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
 101-322 3.19e-10

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: 61.26  E-value: 3.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 101 GALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGt 180
Cdd:cd18548   51 LGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIG- 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 181 sGILM--WMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRA 258
Cdd:cd18548  130 -AIIMafRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKAN 208

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 259 QEVRDFAVNSQwksdassRASGLL---FQFGIDIfraaAMLTVLF--------SDLSIGQMLAVFSYLWFMISPV 322
Cdd:cd18548  209 DDLTDTSLKAG-------RLMALLnplMMLIMNL----AIVAILWfgghlinaGSLQVGDLVAFINYLMQILMSL 272
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 369-538 3.57e-10

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 60.56  E-value: 3.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLN--FGYGEEL--VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG---STQQEIGLETIR 441
Cdd:PRK10584   7 VEVHHLKksVGQGEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplHQMDEEARAKLR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 442 -ENVSVVLQH-------PALFNDTVRANLTMGRER-SDQACWQALEIAQLDATVKALPLGLdsvvgrsgvrfSGGQRQRL 512
Cdd:PRK10584  87 aKHVGFVFQSfmliptlNALENVELPALLRGESSRqSRNGAKALLEQLGLGKRLDHLPAQL-----------SGGEQQRV 155

                        170       180
                 ....*....|....*....|....*.
gi 489309308 513 AIARMVLAEPKVVILDEATSALDAAT 538
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQT 181
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 392-563 4.77e-10

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


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 60.46  E-value: 4.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 392 APGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIR-----------FGGSTQQEIgLETIRE-NVSVVL------QHPAL 453
Cdd:cd03236   24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELQNY-FTKLLEgDVKVIVkpqyvdLIPKA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 454 FNDTVRANLtmgrERSDqacwqalEIAQLDATVKALplGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSA 533
Cdd:cd03236  103 VKGKVGELL----KKKD-------ERGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169

                        170       180       190
                 ....*....|....*....|....*....|.
gi 489309308 534 LDAATEYNLHQALARFLS-GRTTLIIAHRLS 563
Cdd:cd03236  170 LDIKQRLNAARLIRELAEdDNYVLVVEHDLA 200
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
 123-287 4.92e-10

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: 60.95  E-value: 4.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 123 RIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGILMWMHWKLALLILLFNPLV 202
Cdd:cd18589   70 RLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLL 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 203 IYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRA-GNRQG---FFLGRLGQRAQ----EVRDFAVNSqWksda 274
Cdd:cd18589  150 LLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSfANEEGeaqRYRQRLQKTYRlnkkEAAAYAVSM-W---- 224

                        170
                 ....*....|...
gi 489309308 275 SSRASGLLFQFGI 287
Cdd:cd18589  225 TSSFSGLALKVGI 237
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
393-562 5.26e-10

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 62.13  E-value: 5.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 393 PGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSI-----------RFGGSTQQEIgLETIREN-VSVVL------QHPALF 454
Cdd:PRK13409  98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkRFRGTELQNY-FKKLYNGeIKVVHkpqyvdLIPKVF 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 455 NDTVRANLtmgrERSDqacwqalEIAQLDATVKALplGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSAL 534
Cdd:PRK13409 177 KGKVRELL----KKVD-------ERGKLDEVVERL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243

                        170       180
                 ....*....|....*....|....*...
gi 489309308 535 DAATEYNLHQALARFLSGRTTLIIAHRL 562
Cdd:PRK13409 244 DIRQRLNVARLIRELAEGKYVLVVEHDL 271
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 379-584 7.17e-10

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 62.43  E-value: 7.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   379 GEELV-LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTpqAGSI------------------RFGGSTQQEIGLE- 438
Cdd:TIGR00956  773 KEKRViLNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT--TGVItggdrlvngrpldssfqrSIGYVQQQDLHLPt 850

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   439 -TIRENV--SVVLQHPAlfndtvranlTMGRERSDQACWQALEIAQLDATVkalplglDSVVGRSGVRFSGGQRQRLAIA 515
Cdd:TIGR00956  851 sTVRESLrfSAYLRQPK----------SVSKSEKMEYVEEVIKLLEMESYA-------DAVVGVPGEGLNVEQRKRLTIG 913

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308   516 RMVLAEPKVVI-LDEATSALDAATEYNLHQaLARFLS--GRTTLIIAHRLSAV--KQADRVLVFD-GGHIAEDGD 584
Cdd:TIGR00956  914 VELVAKPKLLLfLDEPTSGLDSQTAWSICK-LMRKLAdhGQAILCTIHQPSAIlfEEFDRLLLLQkGGQTVYFGD 987
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 384-582 8.23e-10

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: 61.38  E-value: 8.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQ-AGSIRFGGStQQEIG--LETIRENVSVVLQ----HPALFND 456
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGK-PVDIRnpAQAIRAGIAMVPEdrkrHGIVPIL 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  457 TVRANLTM-------GRERSDQACWQAL---EIAQLdaTVKA----LPLGldsvvgrsgvRFSGGQRQRLAIARMVLAEP 522
Cdd:TIGR02633 355 GVGKNITLsvlksfcFKMRIDAAAELQIigsAIQRL--KVKTaspfLPIG----------RLSGGNQQKAVLAKMLLTNP 422

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308  523 KVVILDEATSALDAATEYNLHQ---ALARflSGRTTLIIAHRLSAV-KQADRVLVFDGGHIAED 582
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKlinQLAQ--EGVAIIVVSSELAEVlGLSDRVLVIGEGKLKGD 484
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
387-590 8.67e-10

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 59.80  E-value: 8.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 387 LNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGStQQEIGLETIR-ENVSVVLQHPA-----------LF 454
Cdd:PRK15112  32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH-PLHFGDYSYRsQRIRMIFQDPStslnprqrisqIL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 455 NDTVRANLTMGRERSDQACWQAL-EIAQLDATVKALPLGLDSvvgrsgvrfsgGQRQRLAIARMVLAEPKVVILDEATSA 533
Cdd:PRK15112 111 DFPLRLNTDLEPEQREKQIIETLrQVGLLPDHASYYPHMLAP-----------GQKQRLGLARALILRPKVIIADEALAS 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489309308 534 LDAATE---YNLHQALARfLSGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIA 590
Cdd:PRK15112 180 LDMSMRsqlINLMLELQE-KQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
 101-342 8.81e-10

Six-transmembrane helical domain 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: 350002 [Multi-domain]  Cd Length: 312  Bit Score: 60.37  E-value: 8.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 101 GALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGT 180
Cdd:cd18558   71 IVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 181 SGILMWMHWKLALLILLFNPL-----VIYATVQLGKRVKHLKKLENDStsrftQALTETLDAIQEVRAGNRQGFFLGRLG 255
Cdd:cd18558  151 FIIGFIRGWKLTLVILAISPVlglsaVVWAKILSGFTDKEKKAYAKAG-----AVAEEVLEAFRTVIAFGGQQKEETRYA 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 256 QRAQEVRDFAVNSQWKSDASSRASGLLFQFGIDI-FRAAAMLtVLFSDLSIGQMLAV-FSYLWFMISPVEQLLNLQyAYY 333
Cdd:cd18558  226 QNLEIAKRNGIKKAITFNISMGAAFLLIYASYALaFWYGTYL-VTQQEYSIGEVLTVfFSVLIGAFSAGQQVPSIE-AFA 303


                 ....*....
gi 489309308 334 AAGGALTRI 342
Cdd:cd18558  304 NARGAAYHI 312
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 378-591 1.71e-09

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 58.75  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 378 YGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFggsTQQEIGL----ETIRENVSVVLQHPAL 453
Cdd:PRK10895  13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIII---DDEDISLlplhARARRGIGYLPQEASI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 454 FND-----------TVRANLTMgRERSDQA--CWQALEIAQLDATVkalplgldsvvgrsGVRFSGGQRQRLAIARMVLA 520
Cdd:PRK10895  90 FRRlsvydnlmavlQIRDDLSA-EQREDRAneLMEEFHIEHLRDSM--------------GQSLSGGERRRVEIARALAA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489309308 521 EPKVVILDEATSALDAATEYNLHQALARFL-SGRTTLIIAHRL-SAVKQADRVLVFDGGHIAEDGDHQQLIAD 591
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQD 227
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 343-569 2.21e-09

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 60.03  E-value: 2.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 343 NELLARADEPQyaggADPFTGRETVGIEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYtPQA 422
Cdd:PRK10938 239 GVQLPEPDEPS----ARHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQG 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 423 GS---IRFG-----GST----QQEIGLetirenVSVVLQHPALFNDTVRANLTMGRERSdQACWQALEIAQLDATVKALP 490
Cdd:PRK10938 314 YSndlTLFGrrrgsGETiwdiKKHIGY------VSSSLHLDYRVSTSVRNVILSGFFDS-IGIYQAVSDRQQKLAQQWLD 386

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 491 -LGLDSVVGRSGVR-FSGGQrQRLA-IARMVLAEPKVVILDEATSALDAATEynlhQALARFL-----SGRTTLI----- 557
Cdd:PRK10938 387 iLGIDKRTADAPFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNR----QLVRRFVdvlisEGETQLLfvshh 461

                        250
                 ....*....|....*....
gi 489309308 558 -------IAHRLSAVKQAD 569
Cdd:PRK10938 462 aedapacITHRLEFVPDGD 480
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 378-579 2.22e-09

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 58.59  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 378 YGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFG-----GSTQQEIGLE-TIRENVSVVLQhp 451
Cdd:PRK09544  14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNgklriGYVPQKLYLDtTLPLTVNRFLR-- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 452 alfndtvranLTMGRERSDqaCWQALEIAQLDATVKAlPLGldsvvgrsgvRFSGGQRQRLAIARMVLAEPKVVILDEAT 531
Cdd:PRK09544  92 ----------LRPGTKKED--ILPALKRVQAGHLIDA-PMQ----------KLSGGETQRVLLARALLNRPQLLVLDEPT 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489309308 532 SALDAATE---YNLHQALARFLsGRTTLIIAHRLSAV-KQADRVLVFDgGHI 579
Cdd:PRK09544 149 QGVDVNGQvalYDLIDQLRREL-DCAVLMVSHDLHLVmAKTDEVLCLN-HHI 198
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
360-535 2.73e-09

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 60.14  E-value: 2.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 360 PFTGRETVGIEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIR-FGgstqQEI--- 435
Cdd:NF033858 258 PADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlFG----QPVdag 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 436 GLETiRENVSVVLQHPALFND-TVRANLT-------MGRERSDQACWQALE----IAQLDATVKALPLGLdsvvgrsgvr 503
Cdd:NF033858 334 DIAT-RRRVGYMSQAFSLYGElTVRQNLElharlfhLPAAEIAARVAEMLErfdlADVADALPDSLPLGI---------- 402

                        170       180       190
                 ....*....|....*....|....*....|..
gi 489309308 504 fsggqRQRLAIARMVLAEPKVVILDEATSALD 535
Cdd:NF033858 403 -----RQRLSLAVAVIHKPELLILDEPTSGVD 429
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 384-599 4.63e-09

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 59.13  E-value: 4.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQ----------QEIGLETIRenvsvvlqhpal 453
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAliaissglngQLTGIENIE------------ 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 454 fndtvRANLTMG--RERSDQACWQALEIAQ----LDATVKAlplgldsvvgrsgvrFSGGQRQRLAIARMVLAEPKVVIL 527
Cdd:PRK13545 108 -----LKGLMMGltKEKIKEIIPEIIEFADigkfIYQPVKT---------------YSSGMKSRLGFAISVHINPDILVI 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308 528 DEATSALDAATEYNLHQALARFL-SGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQLIADGGLYAKLY 599
Cdd:PRK13545 168 DEALSVGDQTFTKKCLDKMNEFKeQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKY 241
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 391-579 8.43e-09

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 58.97  E-value: 8.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   391 IAPGEKVAIVGASGGGKSTLVQLLL----GLYTPQAGSIRFGGSTQQEIgLETIRENVSVVLQhpalfNDTVRANLTMGr 466
Cdd:TIGR00956   84 IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAE-----TDVHFPHLTVG- 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   467 ersdqacwQALEIAQLDATVKALPLGL-----------------------DSVVGRSGVR-FSGGQRQRLAIARMVLAEP 522
Cdd:TIGR00956  157 --------ETLDFAARCKTPQNRPDGVsreeyakhiadvymatyglshtrNTKVGNDFVRgVSGGERKRVSIAEASLGGA 228

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308   523 KVVILDEATSALDAATEYNLHQAL---ARFLSGrTTLIIAHRLS--AVKQADRVLVFDGGHI 579
Cdd:TIGR00956  229 KIQCWDNATRGLDSATALEFIRALktsANILDT-TPLVAIYQCSqdAYELFDKVIVLYEGYQ 289
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 384-577 9.45e-09

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: 55.33  E-value: 9.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLL-----LGLYTpqaGSIRFGGstqQEIGlETIRENVSVVLQHPALF-NDT 457
Cdd:cd03232   23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVIT---GEILING---RPLD-KNFQRSTGYVEQQDVHSpNLT 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 458 VRanltmgrersdqacwQALEIAqldatvkALPLGLdsvvgrsgvrfSGGQRQRLAIARMVLAEPKVVILDEATSALDAA 537
Cdd:cd03232   96 VR---------------EALRFS-------ALLRGL-----------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489309308 538 TEYNLHQALARF-LSGRTTLIIAHRLSAV--KQADRVLVFDGG 577
Cdd:cd03232  143 AAYNIVRFLKKLaDSGQAILCTIHQPSASifEKFDRLLLLKRG 185
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
373-535 1.34e-08

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 55.63  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 373 GLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG--STQQEigletiRENVSVVLQH 450
Cdd:PRK13543  16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktATRGD------RSRFMAYLGH 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 451 -PALFND-TVRANLTM-----GReRSDQACWQALEIAQLDATVKALplgldsvvgrsgVR-FSGGQRQRLAIARMVLAEP 522
Cdd:PRK13543  90 lPGLKADlSTLENLHFlcglhGR-RAKQMPGSALAIVGLAGYEDTL------------VRqLSAGQKKRLALARLWLSPA 156

                        170
                 ....*....|...
gi 489309308 523 KVVILDEATSALD 535
Cdd:PRK13543 157 PLWLLDEPYANLD 169
PLN03140 PLN03140
ABC transporter G family member; Provisional
 393-536 1.40e-08

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 57.93  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  393 PGEKVAIVGASGGGKSTLVQLLLGLYTPQ--AGSIRFGGSTQQEIGLETIR--------ENVSVVLQHPALFNDTVRANL 462
Cdd:PLN03140  905 PGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETFARISgyceqndiHSPQVTVRESLIYSAFLRLPK 984

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308  463 TMGRERSDQACWQALEIAQLDaTVKalplglDSVVGRSGVR-FSGGQRQRLAIARMVLAEPKVVILDEATSALDA 536
Cdd:PLN03140  985 EVSKEEKMMFVDEVMELVELD-NLK------DAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 394-582 1.80e-08

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 57.25  E-value: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 394 GEKVAIVGASGGGKSTLVQLLLGLYTpqagsirfgGSTQQEIGLEtireNVSVVLQHPAlfnDTVRANLTM---GRERS- 469
Cdd:PRK13549 288 GEILGIAGLVGAGRTELVQCLFGAYP---------GRWEGEIFID----GKPVKIRNPQ---QAIAQGIAMvpeDRKRDg 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 470 ----------------DQACW-----QALEIAQLDATVKALPLGLDSVVGRSGvRFSGGQRQRLAIARMVLAEPKVVILD 528
Cdd:PRK13549 352 ivpvmgvgknitlaalDRFTGgsridDAAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILD 430

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 529 EATSALD--AATE-YNLHQALARflSGRTTLIIAHRLSAV-KQADRVLVFDGGHIAED 582
Cdd:PRK13549 431 EPTRGIDvgAKYEiYKLINQLVQ--QGVAIIVISSELPEVlGLSDRVLVMHEGKLKGD 486
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
 104-342 2.51e-08

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: 55.67  E-value: 2.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLvTDLDTVDKFVGetlSRFLVAMLTL--VGTS 181
Cdd:cd18566   57 LLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLT---GQALLALLDLpfVLIF 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 182 GILMW-MHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAgnrqgfflgrLGQRAQE 260
Cdd:cd18566  133 LGLIWyLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKA----------MAMEPQM 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 261 VRDFAVNSQWKSDASSRAS--GLLFQFGIDIFRAAAMLTVLF--------SDLSIGQMLAVFSYLWFMISPVEQLLNLQY 330
Cdd:cd18566  203 LRRYERLQANAAYAGFKVAkiNAVAQTLGQLFSQVSMVAVVAfgallvinGDLTVGALIACTMLSGRVLQPLQRAFGLWT 282

                        250
                 ....*....|..
gi 489309308 331 AYYAAGGALTRI 342
Cdd:cd18566  283 RFQQVRVAVRRL 294
PLN03073 PLN03073
ABC transporter F family; Provisional
 375-560 2.54e-08

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 57.18  E-value: 2.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 375 NFGY-GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIrfggstqqeigLETIRENVSVVLQHPAL 453
Cdd:PLN03073 515 SFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------FRSAKVRMAVFSQHHVD 583

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 454 FND-TVRANLTMGRersdqaCWQALEIAQLDATvkalpLGLDSVVGRSGVR----FSGGQRQRLAIARMVLAEPKVVILD 528
Cdd:PLN03073 584 GLDlSSNPLLYMMR------CFPGVPEQKLRAH-----LGSFGVTGNLALQpmytLSGGQKSRVAFAKITFKKPHILLLD 652

                        170       180       190
                 ....*....|....*....|....*....|..
gi 489309308 529 EATSALDAATEYNLHQALARFLSGrtTLIIAH 560
Cdd:PLN03073 653 EPSNHLDLDAVEALIQGLVLFQGG--VLMVSH 682
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 101-325 3.59e-08

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: 55.18  E-value: 3.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 101 GALVFNVLQARLFARLA----KDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDldtVDKfVGETLSRFLV---- 172
Cdd:cd18540   50 GLILIQALSVFLFIRLAgkieMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSD---TQR-LGEIISWGLVdlvw 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 173 AMLTLVGTSGILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAgnrqgfflg 252
Cdd:cd18540  126 GITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKT--------- 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 253 rLGQRAQEVRDFAVNSQWKSDASSRA---SGLLF---QFGIDIFRAAAMLT----VLFSDLSIGQMLAVFSYLWFMISPV 322
Cdd:cd18540  197 -LVREEKNLREFKELTEEMRRASVRAarlSALFLpivLFLGSIATALVLWYggilVLAGAITIGTLVAFISYATQFFEPI 275


                 ...
gi 489309308 323 EQL 325
Cdd:cd18540  276 QQL 278
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 393-575 5.12e-08

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: 52.38  E-value: 5.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   393 PGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFggstqqeIGLETIRENVSVVLQHPalfndtvranltmgrersdqa 472
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLDQLLLI--------------------- 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   473 cwqaleiaqldatvkalplgldsVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFL-- 550
Cdd:smart00382  53 -----------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109

                          170       180       190
                   ....*....|....*....|....*....|
gi 489309308   551 -----SGRTTLIIAHRLSAVKQADRVLVFD 575
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPALLRRRFD 139
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 393-535 5.70e-08

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 55.56  E-value: 5.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 393 PGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSI-----------RFGGSTQQEIgLETIREN---VSVVLQH----PALF 454
Cdd:COG1245   98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGTELQDY-FKKLANGeikVAHKPQYvdliPKVF 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 455 NDTVRANLTMGRERSDqacwqALEIAQLdatvkalpLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSAL 534
Cdd:COG1245  177 KGTVRELLEKVDERGK-----LDELAEK--------LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243


                 .
gi 489309308 535 D 535
Cdd:COG1245  244 D 244
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 379-535 7.00e-08

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 55.56  E-value: 7.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 379 GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQE-IGLETirenvsVVLQHPALfnDT 457
Cdd:PRK10636  12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAwVNQET------PALPQPAL--EY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 458 V----------RANLTMGRERSDQACWQALEiAQLDA----TVKALPLGLDSVVGRSGVR-------FSGGQRQRLAIAR 516
Cdd:PRK10636  84 VidgdreyrqlEAQLHDANERNDGHAIATIH-GKLDAidawTIRSRAASLLHGLGFSNEQlerpvsdFSGGWRMRLNLAQ 162

                        170
                 ....*....|....*....
gi 489309308 517 MVLAEPKVVILDEATSALD 535
Cdd:PRK10636 163 ALICRSDLLLLDEPTNHLD 181
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 382-598 9.51e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 55.02  E-value: 9.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 382 LVLDQLNLNiaPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIGLETIRENVSVVLQhpalfndtvRAN 461
Cdd:PRK10938  19 LQLPSLTLN--AGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQ---------RNN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 462 LTMGRERSDQACWQALEIAQLDATVKAL------PLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALD 535
Cdd:PRK10938  88 TDMLSPGEDDTGRTTAEIIQDEVKDPARceqlaqQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 536 AATEYNLHQALARFLSGRTTLI-IAHRLSAV-KQADRVLVFDGGHIAEDGDHQQLIADgGLYAKL 598
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITLVlVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQQ-ALVAQL 231
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 384-583 1.91e-07

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


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 51.17  E-value: 1.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLllglytpqagsirfGGSTQQEIGLETIRENVSvvlQHPALFNDTVRANLT 463
Cdd:cd03238   11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNE--------------GLYASGKARLISFLPKFS---RNKLIFIDQLQFLID 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 464 MGrersdqacwqaleiaqldatVKALPLGldsvvgRSGVRFSGGQRQRLAIARMVLAEPK--VVILDEATSALDAATEYN 541
Cdd:cd03238   74 VG--------------------LGYLTLG------QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQ 127

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489309308 542 LHQALARFLS-GRTTLIIAHRLSAVKQADRVLVF------DGGHIAEDG 583
Cdd:cd03238  128 LLEVIKGLIDlGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
 104-243 2.17e-07

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: 53.02  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGI 183
Cdd:cd18780   57 IATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVF 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 184 LMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRA 243
Cdd:cd18780  137 MFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRS 196
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 505-590 2.19e-07

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 53.85  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 505 SGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFLS-GRTTLIIAHRLSAV-KQADRVLVFDGGHI--- 579
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVlGMSDRILVMHEGRIsge 476

                         90
                 ....*....|...
gi 489309308 580 --AEDGDHQQLIA 590
Cdd:PRK10762 477 ftREQATQEKLMA 489
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
 104-310 4.51e-07

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: 51.82  E-value: 4.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLvTDLDTVDKF-VGETLSRFLVAMLtLVGTSG 182
Cdd:cd18782   57 VLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFlTGTALTTLLDVLF-SVIYIA 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 183 ILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQR-AQEV 261
Cdd:cd18782  135 VLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRyARSL 214

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489309308 262 -RDFAVNSQwkSDASSRASGLLFQFGIDIFRAAAMLTVLFSDLSIGQMLA 310
Cdd:cd18782  215 gEGFKLTVL--GTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIA 262
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 384-583 4.54e-07

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 52.05  E-value: 4.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYT-P---QAGSIRFGGSTQQEIGLETIRE----NVSVVLQHPAlfn 455
Cdd:PRK11022  23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEKERRNlvgaEVAMIFQDPM--- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 456 DTVRANLTMGRErsdqaCWQALEIAQ--LDATVKALPLGLDSVVG------RSGV---RFSGGQRQRLAIARMVLAEPKV 524
Cdd:PRK11022 100 TSLNPCYTVGFQ-----IMEAIKVHQggNKKTRRQRAIDLLNQVGipdpasRLDVyphQLSGGMSQRVMIAMAIACRPKL 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 525 VILDEATSALDAATEYNLHQALARFLSGRTT--LIIAHRLSAVKQ-ADRVLVFDGGHIAEDG 583
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVAEaAHKIIVMYAGQVVETG 236
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
394-567 9.26e-07

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 50.65  E-value: 9.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 394 GEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIR-FGGSTQQeigleTIREN-VSVVLQH-------PALFNDTVranlTM 464
Cdd:PRK15056  33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISiLGQPTRQ-----ALQKNlVAYVPQSeevdwsfPVLVEDVV----MM 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 465 GRerSDQACWQALEIAQLDATVKALPLGLDSVVGRSGV--RFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNL 542
Cdd:PRK15056 104 GR--YGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQigELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181

                        170       180
                 ....*....|....*....|....*..
gi 489309308 543 hQALARFL--SGRTTLIIAHRLSAVKQ 567
Cdd:PRK15056 182 -ISLLRELrdEGKTMLVSTHNLGSVTE 207
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 384-562 1.14e-06

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: 51.94  E-value: 1.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGstqqeiglETIRENVSVVLQH----PALfnDTVR 459
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG--------KSILTNISDVHQNmgycPQF--DAID 2024

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308   460 ANLTmGRER----SDQACWQALEIAQLdATVKALPLGLDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALD 535
Cdd:TIGR01257 2025 DLLT-GREHlylyARLRGVPAEEIEKV-ANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102

                          170       180
                   ....*....|....*....|....*...
gi 489309308   536 AATEYNLHQALARFL-SGRTTLIIAHRL 562
Cdd:TIGR01257 2103 PQARRMLWNTIVSIIrEGRAVVLTSHSM 2130
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 491-572 5.55e-06

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 49.83  E-value: 5.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  491 LGLDSV-VGRSGVRFSGGQRQRLAIARMVLA---EPKVVILDEATSALDAateYNLHQALARFLS----GRTTLIIAHRL 562
Cdd:PRK00635  796 LGLDYLpLGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHT---HDIKALIYVLQSlthqGHTVVIIEHNM 872

                          90
                  ....*....|
gi 489309308  563 SAVKQADRVL 572
Cdd:PRK00635  873 HVVKVADYVL 882
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
 384-592 7.16e-06

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


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 47.99  E-value: 7.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 384 LDQLNLNIAPGEKVAIVGASGGGKSTLVQ--LLLGLYTPQAGSIRFGGSTQQEIGLETIrENVSVVLQHP---------- 451
Cdd:cd03271   11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtLYPALARRLHLKKEQPGNHDRIEGLEHI-DKVIVIDQSPigrtprsnpa 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 452 -------------------ALFNDTVRANLTMGRERSD---QACWQALE----IAQLDATVKAL-PLGLDSV-VGRSGVR 503
Cdd:cd03271   90 tytgvfdeirelfcevckgKRYNRETLEVRYKGKSIADvldMTVEEALEffenIPKIARKLQTLcDVGLGYIkLGQPATT 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 504 FSGGQRQRLAIARMvLAEPK----VVILDEATSALDAATEYNLHQALARFLS-GRTTLIIAHRLSAVKQADRVLvfDGGh 578
Cdd:cd03271  170 LSGGEAQRIKLAKE-LSKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWII--DLG- 245

                        250
                 ....*....|....*
gi 489309308 579 iAEDGDH-QQLIADG 592
Cdd:cd03271  246 -PEGGDGgGQVVASG 259
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 377-538 8.76e-06

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 48.79  E-value: 8.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 377 GYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGST-----QQ-----EIGleTIRENVSV 446
Cdd:PRK11147  12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLivarlQQdpprnVEG--TVYDFVAE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 447 VLQHPA-LFNDTVRANLTMGRERSDQ-----ACWQA-LEIA---QLDATVKAL--PLGLDSVVGRSGVrfSGGQRQRLAI 514
Cdd:PRK11147  90 GIEEQAeYLKRYHDISHLVETDPSEKnlnelAKLQEqLDHHnlwQLENRINEVlaQLGLDPDAALSSL--SGGWLRKAAL 167

                        170       180
                 ....*....|....*....|....
gi 489309308 515 ARMVLAEPKVVILDEATSALDAAT 538
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIET 191
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
383-590 1.58e-05

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 47.49  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 383 VLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGL----YTPQAGSIRFggstqQEIGL---------ETIRENVSVVLQ 449
Cdd:PRK15093  22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRF-----DDIDLlrlsprerrKLVGHNVSMIFQ 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 450 HPALFNDTVRanlTMGRERSdQAC---------WQ--------ALE------IAQLDATVKALPLGLdsvvgrsgvrfSG 506
Cdd:PRK15093  97 EPQSCLDPSE---RVGRQLM-QNIpgwtykgrwWQrfgwrkrrAIEllhrvgIKDHKDAMRSFPYEL-----------TE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 507 GQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARF--LSGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDG 583
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnqNNNTTILLISHDLQMLSQwADKINVLYCGQTVETA 241


                 ....*..
gi 489309308 584 DHQQLIA 590
Cdd:PRK15093 242 PSKELVT 248
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 502-576 2.84e-05

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 44.87  E-value: 2.84e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489309308 502 VRFSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQALARFL--SGRTTLIIAHRLSAVKQ-ADRVLVFDG 576
Cdd:cd03222   70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDLAVLDYlSDRIHVFEG 147
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
394-581 4.58e-05

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 46.32  E-value: 4.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 394 GEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGG----------STQQEIGLET-------------IRENVSVVlqh 450
Cdd:PRK09700 289 GEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdisprspldAVKKGMAYITesrrdngffpnfsIAQNMAIS--- 365

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 451 PALFNDTVRANLTMGRERSDQacwQALEIAQLDATVKAlplgldSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEA 530
Cdd:PRK09700 366 RSLKDGGYKGAMGLFHEVDEQ---RTAENQRELLALKC------HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489309308 531 TSALDAATE---YNLHQALARflSGRTTLIIAHRLSAVKQA-DRVLVFDGGHIAE 581
Cdd:PRK09700 437 TRGIDVGAKaeiYKVMRQLAD--DGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 380-568 6.58e-05

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 44.09  E-value: 6.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 380 EELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGSTQQEIG---LETIRENVSVVLQHpalfnd 456
Cdd:PRK13541  12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpyCTYIGHNLGLKLEM------ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 457 TVRANLTMGRERSDQAcwqaleiAQLDATVKALPLglDSVVGRSGVRFSGGQRQRLAIARMVLAEPKVVILDEATSALDA 536
Cdd:PRK13541  86 TVFENLKFWSEIYNSA-------ETLYAAIHYFKL--HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489309308 537 ATE---YNLHQALARflSGRTTLIIAHRLSAVKQA 568
Cdd:PRK13541 157 ENRdllNNLIVMKAN--SGGIVLLSSHLESSIKSA 189
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
388-587 1.03e-04

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 45.29  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 388 NLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIRFGGST---------------------QQE--IGLETIRENV 444
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPidirsprdairagimlcpedrKAEgiIPVHSVADNI 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 445 svvlqhpalfndtvraNLTMGRERSDQACW--QALEIAQLDATVKALPLGLDSvvGRSGVRF-SGGQRQRLAIARMvLAE 521
Cdd:PRK11288 353 ----------------NISARRHHLRAGCLinNRWEAENADRFIRSLNIKTPS--REQLIMNlSGGNQQKAILGRW-LSE 413

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489309308 522 P-KVVILDEATSALD--AATE-YNLHQALARflSGRTTLIIAHRLSAVKQ-ADRVLVFDGGHIAEDGDHQQ 587
Cdd:PRK11288 414 DmKVILLDEPTRGIDvgAKHEiYNVIYELAA--QGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
 103-328 1.15e-04

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: 44.47  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 103 LVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTsG 182
Cdd:cd18568   56 ILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYL-G 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 183 ILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEvr 262
Cdd:cd18568  135 LMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAK-- 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489309308 263 dfAVNSQWK----SDASSRASGLLFQFG-IDIFRAAAMLtVLFSDLSIGQMLAvFSYLWFM-ISPVEQLLNL 328
Cdd:cd18568  213 --ALNTRFRgqklSIVLQLISSLINHLGtIAVLWYGAYL-VISGQLTIGQLVA-FNMLFGSvINPLLALVGL 280
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
369-535 1.50e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 44.73  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 369 IEVRGLNFGYGEELVLDQLNLNIAPGEKVAIVGASGGGKSTLVQLLLGLYTPQAGSIR-FGGSTQQEIGLETIRENVSVV 447
Cdd:NF033858   2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGDMADARHRRAVCPRIAYM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 448 LQ------HPALfndTVRANLT-MGR-------ERsdqacwqALEIAQL-DATvkalplGLDSVVGRSGVRFSGGQRQRL 512
Cdd:NF033858  82 PQglgknlYPTL---SVFENLDfFGRlfgqdaaER-------RRRIDELlRAT------GLAPFADRPAGKLSGGMKQKL 145

                        170       180
                 ....*....|....*....|...
gi 489309308 513 AIARMVLAEPKVVILDEATSALD 535
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVD 168
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 491-592 1.88e-04

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: 44.62  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308  491 LGLDSV-VGRSGVRFSGGQRQRLAIARMVLAE---PKVVILDEATSALDAATEYNLHQALARFLS-GRTTLIIAHRLSAV 565
Cdd:TIGR00630 816 VGLGYIrLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDkGNTVVVIEHNLDVI 895

                          90       100
                  ....*....|....*....|....*...
gi 489309308  566 KQADRVLvfDGGhiAEDGDH-QQLIADG 592
Cdd:TIGR00630 896 KTADYII--DLG--PEGGDGgGTVVASG 919
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
 123-242 2.79e-04

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: 43.07  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 123 RIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGILMWMHWKLALLILLFNPLV 202
Cdd:cd18784   70 RIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLI 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489309308 203 IYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVR 242
Cdd:cd18784  150 AIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVR 189
PLN03140 PLN03140
ABC transporter G family member; Provisional
 483-546 3.42e-04

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 43.68  E-value: 3.42e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489309308  483 DATVKALPLGL--DSVVGRSGVR-FSGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQAL 546
Cdd:PLN03140  313 DYTLKILGLDIckDTIVGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCL 379
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
 103-238 6.24e-04

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: 42.11  E-value: 6.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 103 LVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLvTDLDTVDKFVGETLSRFLVAMLTLVGTSG 182
Cdd:cd18555   56 GLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLI 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489309308 183 ILMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAI 238
Cdd:cd18555  135 YMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGI 190
ABC_6TM_AarD_CydD cd18584
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ...
 104-203 6.59e-04

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: 42.01  E-value: 6.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFvgetLSRFLVAM-LTLVGTSG 182
Cdd:cd18584   52 LLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDALDGY----FARYLPQLvLAAIVPLL 127

                         90       100
                 ....*....|....*....|....
gi 489309308 183 IL---MWMHWKLALLILLFNPLVI 203
Cdd:cd18584  128 ILvavFPLDWVSALILLVTAPLIP 151
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 379-572 7.38e-04

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 40.42  E-value: 7.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 379 GEELVLDQLNLNIAPGEKVAIVGASGGGKSTLV-QLLLGLytpqagsirfggstqqeigletirenvsvvlqhpalfndT 457
Cdd:cd03227    6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILdAIGLAL---------------------------------------G 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 458 VRANLTMGRERSDQACWQALEIAQLDATVKALplgldsvvgrsgvrfSGGQRQRLAIA-RMVLAEPK---VVILDEATSA 533
Cdd:cd03227   47 GAQSATRRRSGVKAGCIVAAVSAELIFTRLQL---------------SGGEKELSALAlILALASLKprpLYILDEIDRG 111

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 489309308 534 LDAATEYNLHQALARFL-SGRTTLIIAHRLSAVKQADRVL 572
Cdd:cd03227  112 LDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 505-580 1.03e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 42.02  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 505 SGGQRQRLAIARMVLAEPKVVILDEATSALDAATEYNLHQ---ALARflSGRTTLIIAHRL-SAVKQADRVLVFDGGHIA 580
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQliaELAK--KDKGIIIISSEMpELLGITDRILVMSNGLVA 470
PLN03073 PLN03073
ABC transporter F family; Provisional
 504-535 1.17e-03

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 41.77  E-value: 1.17e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 489309308 504 FSGGQRQRLAIARMVLAEPKVVILDEATSALD 535
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
ABC_6TM_AarD_CydDC_like cd18561
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ...
 104-262 1.18e-03

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: 41.11  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 104 VFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVGTSGI 183
Cdd:cd18561   51 ALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIY 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489309308 184 LMWMHWKLALLILLFNPLVIYATVQLGKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFLGRLGQRAQEVR 262
Cdd:cd18561  131 LFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLR 209
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
 100-251 6.90e-03

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: 39.02  E-value: 6.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489309308 100 CGALVFNVLQARLFARLAKDIVYRIRVRLIERLKRISLSEYESLGSGTVTTHLVTDLDTVDKFVGETLSRFLVAMLTLVG 179
Cdd:cd18580   50 LASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLG 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489309308 180 TSGILMWMHWKLALLILLFnpLVIYATVQL--GKRVKHLKKLENDSTSRFTQALTETLDAIQEVRAGNRQGFFL 251
Cdd:cd18580  130 SLIVIAIVSPYFLIVLPPL--LVVYYLLQRyyLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFI 201
 
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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