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Conserved domains on  [gi|1490918183|gb|RLE47830|]
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hypothetical protein DRJ25_01440 [Candidatus Woesearchaeota archaeon]

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
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];
49-592 5.51e-178

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


:

Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 515.87  E-value: 5.51e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  49 YLFKEVIDAstrfstkaLLLSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHS 128
Cdd:COG1132    42 LLLGRIIDA--------LLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 129 THKTGSLISRIIRGGSAVERLTDVFVFNFAPLLFQFTIVAASLLFIGVIPALISFFVVVVFIAYSYFINNIQQKSNLQLN 208
Cdd:COG1132   114 RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQ 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 209 QAEDEEKANISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWFSVTRFIAE 288
Cdd:COG1132   194 EALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSG 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 289 DITIGTMVFLFTVFNNLFGPLFGFVHGMRNFYRSMADFQDLFKYAKIKNEIEDLPNAGKLKIVHGDIEFKNVSFKY-KKR 367
Cdd:COG1132   274 SLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYpGDR 353

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 368 KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFDDTIYNN 447
Cdd:COG1132   354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIREN 433

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 448 IAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEH 527
Cdd:COG1132   434 IRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEA 513

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 528 EIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLWNLQKGG 592
Cdd:COG1132   514 LIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
 
Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
49-592 5.51e-178

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 515.87  E-value: 5.51e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  49 YLFKEVIDAstrfstkaLLLSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHS 128
Cdd:COG1132    42 LLLGRIIDA--------LLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 129 THKTGSLISRIIRGGSAVERLTDVFVFNFAPLLFQFTIVAASLLFIGVIPALISFFVVVVFIAYSYFINNIQQKSNLQLN 208
Cdd:COG1132   114 RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQ 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 209 QAEDEEKANISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWFSVTRFIAE 288
Cdd:COG1132   194 EALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSG 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 289 DITIGTMVFLFTVFNNLFGPLFGFVHGMRNFYRSMADFQDLFKYAKIKNEIEDLPNAGKLKIVHGDIEFKNVSFKY-KKR 367
Cdd:COG1132   274 SLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYpGDR 353

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 368 KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFDDTIYNN 447
Cdd:COG1132   354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIREN 433

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 448 IAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEH 527
Cdd:COG1132   434 IRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEA 513

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 528 EIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLWNLQKGG 592
Cdd:COG1132   514 LIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 355-589 9.29e-122

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: 359.24  E-value: 9.29e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYK-KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIV 433
Cdd:cd03253     1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 PQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLV 513
Cdd:cd03253    81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183 514 LDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLWNLQ 589
Cdd:cd03253   161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 74-589 1.71e-106

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: 332.07  E-value: 1.71e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  74 ILTIILLVFLAITIFNSAgywlrmHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRII-RGGSAVERLTDV 152
Cdd:TIGR02203  58 LVVIGLAVLRGICSFVST------YLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITfDSEQVASAATDA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 153 F----------VFNFAPLLF---QFTIVaasllfIGVIPALISFFVVVVFIAYSYFINNIQqKSNLQLNQAEDEEKANIS 219
Cdd:TIGR02203 132 FivlvretltvIGLFIVLLYyswQLTLI------VVVMLPVLSILMRRVSKRLRRISKEIQ-NSMGQVTTVAEETLQGYR 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 220 DVftnidsiKYFGKE-------NRIKSIYRKFAVKTRNAllknwnyfrwldsGQLLILGIGLVLLVWFSVTRFIA----- 287
Cdd:TIGR02203 205 VV-------KLFGGQayetrrfDAVSNRNRRLAMKMTSA-------------GSISSPITQLIASLALAVVLFIAlfqaq 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 288 -EDITIGTMVFLFTVFNNLFGPLFGFVHGMRNFYRSMADFQDLFkyAKIKNEIEdlPNAGKLKI--VHGDIEFKNVSFKY 364
Cdd:TIGR02203 265 aGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLF--TLLDSPPE--KDTGTRAIerARGDVEFRNVTFRY 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 365 --KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFDD 442
Cdd:TIGR02203 341 pgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFND 420

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 443 TIYNNIAFSNPK-AKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSL 521
Cdd:TIGR02203 421 TIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSAL 500

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 522 DSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLWNLQ 589
Cdd:TIGR02203 501 DNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
286-592 1.66e-93

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 298.47  E-value: 1.66e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 286 IAEDITIGTMVFLFTVFNNLFGPLFGFVHGMRNFYRSMADFQDLFKYAKIKNEIEDlpnaGKLKI--VHGDIEFKNVSFK 363
Cdd:PRK11176  275 VMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDE----GKRVIerAKGDIEFRNVTFT 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 364 Y--KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFD 441
Cdd:PRK11176  351 YpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFN 430

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 442 DTIYNNIAF-SNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSS 520
Cdd:PRK11176  431 DTIANNIAYaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSA 510

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490918183 521 LDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLWNLQKGG 592
Cdd:PRK11176  511 LDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFGQ 582
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 370-519 6.82e-37

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 134.31  E-value: 6.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 370 FSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFDD-TIYNNI 448
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 449 AFSnpkAKRKDVFRAMKFAQLLKIVNNF--PKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATS 519
Cdd:pfam00005  81 RLG---LLLKGLSKREKDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
GguA NF040905
sugar ABC transporter ATP-binding protein;
368-568 4.12e-16

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 81.37  E-value: 4.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 368 KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNS--GAILIDGKnIKEFK--QESLRSELSIVPQECVLFDD- 442
Cdd:NF040905   15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGE-VCRFKdiRDSEALGIVIIHQELALIPYl 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 443 TIYNNIAFSNPKAKR-----KDVFRamKFAQLLKIVNnfpKKE--KTVVGERGVklsgGEKQRVSIARAILADKKVLVLD 515
Cdd:NF040905   94 SIAENIFLGNERAKRgvidwNETNR--RARELLAKVG---LDEspDTLVTDIGV----GKQQLVEIAKALSKDVKLLILD 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 516 EATSSL-DSETEHeiqadLQKLM-----EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQ 568
Cdd:NF040905  165 EPTAALnEEDSAA-----LLDLLlelkaQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
364-561 1.33e-12

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 66.49  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 364 YKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKnikefkqeslrSELSIVPQECVLfDDT 443
Cdd:NF040873    2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQRSEV-PDS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 444 IynniafsnP----------------------KAKRKDVFRAMKFAQLLKIvnnfpkkEKTVVGErgvkLSGGEKQRVSI 501
Cdd:NF040873   70 L--------PltvrdlvamgrwarrglwrrltRDDRAAVDDALERVGLADL-------AGRQLGE----LSGGQRQRALL 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 502 ARAILADKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMNADKIIVL 561
Cdd:NF040873  131 AQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 379-564 9.94e-10

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 57.38  E-value: 9.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  379 RNKKIALVGPSGSGKTTLIRLLFRLYDVNS-GAILIDGKNIKEFKQESLRselsivpqecvlfddtiynniafsnpkakr 457
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLL------------------------------ 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  458 kdvframkfaqllkivnnfpkkeKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQA------ 531
Cdd:smart00382  51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrl 107

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1490918183  532 DLQKLMEGRTSIIIAH-------RLSTIMNADKIIVLDKG 564
Cdd:smart00382 108 LLLLKSEKNLTVILTTndekdlgPALLRRRFDRRIVLLLI 147
GguA NF040905
sugar ABC transporter ATP-binding protein;
367-567 1.56e-08

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 57.49  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 367 RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLF-RLYDVN-SGAILIDGKNIkefkqeslrsELSIVPQEC------- 437
Cdd:NF040905  273 RKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgRSYGRNiSGTVFKDGKEV----------DVSTVSDAIdaglayv 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 438 ---------VLfDDTIYNNIAFSN-PKAKRKDVFRAMKfaqLLKIVNNFPKKEKT---VVGERGVKLSGGEKQRVSIARA 504
Cdd:NF040905  343 tedrkgyglNL-IDDIKRNITLANlGKVSRRGVIDENE---EIKVAEEYRKKMNIktpSVFQKVGNLSGGNQQKVVLSKW 418

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 505 ILADKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIV 567
Cdd:NF040905  419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINELAaEGKGVIVISSELPELLGmCDRIYVMNEGRIT 483
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
485-580 3.62e-06

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 49.35  E-value: 3.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 485 GERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMN-ADKIIVLD 562
Cdd:NF000106  139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGATVLLTTQYMEEAEQlAHELTVID 218

                          90
                  ....*....|....*...
gi 1490918183 563 KGKIVQQGTHNQLIKEKG 580
Cdd:NF000106  219 RGRVIADGKVDELKTKVG 236
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
355-400 5.69e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 39.72  E-value: 5.69e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLL 400
Cdd:NF033858    2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI 47
 
Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
49-592 5.51e-178

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 515.87  E-value: 5.51e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  49 YLFKEVIDAstrfstkaLLLSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHS 128
Cdd:COG1132    42 LLLGRIIDA--------LLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 129 THKTGSLISRIIRGGSAVERLTDVFVFNFAPLLFQFTIVAASLLFIGVIPALISFFVVVVFIAYSYFINNIQQKSNLQLN 208
Cdd:COG1132   114 RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQ 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 209 QAEDEEKANISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWFSVTRFIAE 288
Cdd:COG1132   194 EALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSG 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 289 DITIGTMVFLFTVFNNLFGPLFGFVHGMRNFYRSMADFQDLFKYAKIKNEIEDLPNAGKLKIVHGDIEFKNVSFKY-KKR 367
Cdd:COG1132   274 SLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYpGDR 353

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 368 KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFDDTIYNN 447
Cdd:COG1132   354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIREN 433

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 448 IAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEH 527
Cdd:COG1132   434 IRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEA 513

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 528 EIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLWNLQKGG 592
Cdd:COG1132   514 LIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 116-589 4.26e-160

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: 471.23  E-value: 4.26e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 116 FNHIIHLSYNFHSTHKTGSLiSRII-RGGSAVERLTDVFVFNFAPLLFQFTIVAASLLFI-GVIPALISFFVVVVFIAYS 193
Cdd:COG5265   118 FRHLHALSLRFHLERQTGGL-SRDIeRGTKGIEFLLRFLLFNILPTLLEIALVAGILLVKyDWWFALITLVTVVLYIAFT 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 194 YFINNIQQKSNLQLNQAEDEEKANISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIG 273
Cdd:COG5265   197 VVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALG 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 274 LVLLVWFSVTRFIAEDITIGTMVFLFTVFNNLFGPL--FGFVhgmrnfYR----SMADFQDLFKYAKIKNEIEDLPNAGK 347
Cdd:COG5265   277 LTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLnfLGFV------YReirqALADMERMFDLLDQPPEVADAPDAPP 350

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 348 LKIVHGDIEFKNVSFKY-KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESL 426
Cdd:COG5265   351 LVVGGGEVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL 430

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 427 RSELSIVPQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAIL 506
Cdd:COG5265   431 RAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLL 510

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 507 ADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLW 586
Cdd:COG5265   511 KNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMW 590


                  ...
gi 1490918183 587 NLQ 589
Cdd:COG5265   591 ARQ 593
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 67-589 2.10e-138

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: 418.85  E-value: 2.10e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  67 LLSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRI-----IR 141
Cdd:COG2274   187 LPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFrdvesIR 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 142 ggsavERLTDVFVFNFAPLLFQFTIVAAsLLFIGVIPALISFFVVVVFIAYSYFINNIQQKSNLQLNQAEDEEKANISDV 221
Cdd:COG2274   267 -----EFLTGSLLTALLDLLFVLIFLIV-LFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVET 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 222 FTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWFSVTRFIAEDITIGTMVFLFTV 301
Cdd:COG2274   341 LRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNIL 420

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 302 FNNLFGPLFGFVHGMRNFYRSMADFQDLFKYAKIKNEIEDLPNAGKLKIVHGDIEFKNVSFKY--KKRKIFSDFNLKIPR 379
Cdd:COG2274   421 SGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYpgDSPPVLDNISLTIKP 500

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 380 NKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFDDTIYNNIAFSNPKAKRKD 459
Cdd:COG2274   501 GERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEE 580

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 460 VFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEG 539
Cdd:COG2274   581 IIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKG 660

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 1490918183 540 RTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLWNLQ 589
Cdd:COG2274   661 RTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 355-589 9.29e-122

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: 359.24  E-value: 9.29e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYK-KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIV 433
Cdd:cd03253     1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 PQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLV 513
Cdd:cd03253    81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183 514 LDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLWNLQ 589
Cdd:cd03253   161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 355-586 6.35e-112

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: 333.81  E-value: 6.35e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKY--KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSI 432
Cdd:cd03251     1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVL 512
Cdd:cd03251    81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490918183 513 VLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLW 586
Cdd:cd03251   161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 355-589 3.56e-107

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: 321.80  E-value: 3.56e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKR---KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELS 431
Cdd:cd03249     1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 432 IVPQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKV 511
Cdd:cd03249    81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 512 LVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLWNLQ 589
Cdd:cd03249   161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 74-589 1.71e-106

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: 332.07  E-value: 1.71e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  74 ILTIILLVFLAITIFNSAgywlrmHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRII-RGGSAVERLTDV 152
Cdd:TIGR02203  58 LVVIGLAVLRGICSFVST------YLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITfDSEQVASAATDA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 153 F----------VFNFAPLLF---QFTIVaasllfIGVIPALISFFVVVVFIAYSYFINNIQqKSNLQLNQAEDEEKANIS 219
Cdd:TIGR02203 132 FivlvretltvIGLFIVLLYyswQLTLI------VVVMLPVLSILMRRVSKRLRRISKEIQ-NSMGQVTTVAEETLQGYR 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 220 DVftnidsiKYFGKE-------NRIKSIYRKFAVKTRNAllknwnyfrwldsGQLLILGIGLVLLVWFSVTRFIA----- 287
Cdd:TIGR02203 205 VV-------KLFGGQayetrrfDAVSNRNRRLAMKMTSA-------------GSISSPITQLIASLALAVVLFIAlfqaq 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 288 -EDITIGTMVFLFTVFNNLFGPLFGFVHGMRNFYRSMADFQDLFkyAKIKNEIEdlPNAGKLKI--VHGDIEFKNVSFKY 364
Cdd:TIGR02203 265 aGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLF--TLLDSPPE--KDTGTRAIerARGDVEFRNVTFRY 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 365 --KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFDD 442
Cdd:TIGR02203 341 pgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFND 420

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 443 TIYNNIAFSNPK-AKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSL 521
Cdd:TIGR02203 421 TIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSAL 500

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 522 DSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLWNLQ 589
Cdd:TIGR02203 501 DNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
 16-589 2.38e-103

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


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 323.96  E-value: 2.38e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  16 LSVYWSLLKKYRFFFFGLLFLIFLLESTRVINKYLFKEVIDAStrFSTKAL-LLSNYTSILTIILLVfLAITIFnsagyw 94
Cdd:TIGR02204   6 LAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHG--FSKDSSgLLNRYFAFLLVVALV-LALGTA------ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  95 LRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRIIrggsaverlTDVfvfnfapLLFQfTIVAAS---- 170
Cdd:TIGR02204  77 ARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLT---------TDT-------TLLQ-SVIGSSlsma 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 171 ----LLFIGVI-------PALISFFVVVV-FIAY--SYFINNIQQKSNlqlnQAED---EEKANISDVFTNIDSIKYFGK 233
Cdd:TIGR02204 140 lrnaLMCIGGLimmfitsPKLTSLVLLAVpLVLLpiLLFGRRVRKLSR----ESQDriaDAGSYAGETLGAIRTVQAFGH 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 234 ENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWFSVTRFIAEDITIGTM---VFLFTVFNNLFGPLf 310
Cdd:TIGR02204 216 EDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLgqfVFYAVMVAGSIGTL- 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 311 GFVHGmrNFYRSMADFQDLFKYAKIKNEIEDLPNAGKLKI-VHGDIEFKNVSFKYKKR---KIFSDFNLKIPRNKKIALV 386
Cdd:TIGR02204 295 SEVWG--ELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVpLRGEIEFEQVNFAYPARpdqPALDGLNLTVRPGETVALV 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 387 GPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKF 466
Cdd:TIGR02204 373 GPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARA 452

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 467 AQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIA 546
Cdd:TIGR02204 453 AHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIA 532

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|...
gi 1490918183 547 HRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLWNLQ 589
Cdd:TIGR02204 533 HRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 353-580 1.28e-98

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: 299.53  E-value: 1.28e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 353 GDIEFKNVSFKY-KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELS 431
Cdd:cd03254     1 GEIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 432 IVPQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKV 511
Cdd:cd03254    81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 512 LVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKG 580
Cdd:cd03254   161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
286-592 1.66e-93

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 298.47  E-value: 1.66e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 286 IAEDITIGTMVFLFTVFNNLFGPLFGFVHGMRNFYRSMADFQDLFKYAKIKNEIEDlpnaGKLKI--VHGDIEFKNVSFK 363
Cdd:PRK11176  275 VMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDE----GKRVIerAKGDIEFRNVTFT 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 364 Y--KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFD 441
Cdd:PRK11176  351 YpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFN 430

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 442 DTIYNNIAF-SNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSS 520
Cdd:PRK11176  431 DTIANNIAYaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSA 510

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490918183 521 LDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLWNLQKGG 592
Cdd:PRK11176  511 LDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFGQ 582
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 68-580 1.78e-89

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: 287.42  E-value: 1.78e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  68 LSNYTSILTIILLVFLAITIFNsagyWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRIIRGgsaVE 147
Cdd:COG4988    54 LSALLPLLGLLLAVLLLRALLA----WLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEG---VE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 148 RLtDVFVFNFAPLLFQfTIVAASLLFIGVIPA--------LISFFVVVVFIAysyFINNIQQKsnlqLNQAEDEEKANIS 219
Cdd:COG4988   127 AL-DGYFARYLPQLFL-AALVPLLILVAVFPLdwlsglilLVTAPLIPLFMI---LVGKGAAK----ASRRQWRALARLS 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 220 DVFtnIDS------IKYFGKENR-IKSI------YRKFAVKT-RNALLknwnyfrwldSGqllilgiglvllvwfSVTRF 285
Cdd:COG4988   198 GHF--LDRlrglttLKLFGRAKAeAERIaeasedFRKRTMKVlRVAFL----------SS---------------AVLEF 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 286 IAediTIGT-MVFLFTVFNNLFGPLfGFVHG-------------MRNF-------YRSMADFQDLFKY-----AKIKNEI 339
Cdd:COG4988   251 FA---SLSIaLVAVYIGFRLLGGSL-TLFAAlfvlllapefflpLRDLgsfyharANGIAAAEKIFALldapePAAPAGT 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 340 EDLPNAGKLkivhgDIEFKNVSFKYKKRK-IFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNI 418
Cdd:COG4988   327 APLPAAGPP-----SIELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 419 KEFKQESLRSELSIVPQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQR 498
Cdd:COG4988   402 SDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQR 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 499 VSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKE 578
Cdd:COG4988   482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561


                  ..
gi 1490918183 579 KG 580
Cdd:COG4988   562 NG 563
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
50-585 1.59e-87

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 283.01  E-value: 1.59e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  50 LFKEVIDAstrfstkallLSNYTSIlTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHST 129
Cdd:PRK13657   41 LFGRIIDA----------ISGKGDI-FPLLAAWAGFGLFNIIAGVLVARHADRLAHRRRLAVLTEYFERIIQLPLAWHSQ 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 130 HKTGSLISRIIRGGSAVERL-TDVFVFNFAPLLFQFTIVAASLlFIGVIPALISFFVVVVFIAYSYFInnIQQKSNLQln 208
Cdd:PRK13657  110 RGSGRALHTLLRGTDALFGLwLEFMREHLATLVALVVLLPLAL-FMNWRLSLVLVVLGIVYTLITTLV--MRKTKDGQ-- 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 209 qAEDEEK-----ANISDVFTNIDSIKYFgkeNRIK---SIYRKFAvktrNALLK------NWnyfrW-LDSGqllilgig 273
Cdd:PRK13657  185 -AAVEEHyhdlfAHVSDAIGNVSVVQSY---NRIEaetQALRDIA----DNLLAaqmpvlSW----WaLASV-------- 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 274 lvllvwfsVTRfIAEDITI------GTM-----------VFLFTVFNNLfgpLFGFVHGMRNF----YRSMADFQDLFKY 332
Cdd:PRK13657  245 --------LNR-AASTITMlailvlGAAlvqkgqlrvgeVVAFVGFATL---LIGRLDQVVAFinqvFMAAPKLEEFFEV 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 333 AKIKNEIEDLPNAGKLKIVHGDIEFKNVSFKY-KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAI 411
Cdd:PRK13657  313 EDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 412 LIDGKNIKEFKQESLRSELSIVPQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKL 491
Cdd:PRK13657  393 LIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQL 472

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 492 SGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGT 571
Cdd:PRK13657  473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552

                         570
                  ....*....|....
gi 1490918183 572 HNQLIKEKGLYKKL 585
Cdd:PRK13657  553 FDELVARGGRFAAL 566
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 106-588 2.00e-84

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: 274.34  E-value: 2.00e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 106 RLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRIIrggSAVERLTDVFVFNFAPLLFQFTIVAASLLFIGVI-----PAL 180
Cdd:COG4987    85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLV---ADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFspalaLVL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 181 ISFFVVVVFIAySYFINNIQQKSNLQLNQAEDEEKANISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFR 260
Cdd:COG4987   162 ALGLLLAGLLL-PLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSA 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 261 WLDSGQLLILGIGLVLLVWFSVTRFIAEDITiGTM--VFLFTVFNnLFGPLFGFVHGMRNFYRSMADFQDLFKYAKIKNE 338
Cdd:COG4987   241 LAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLlaLLVLAALA-LFEALAPLPAAAQHLGRVRAAARRLNELLDAPPA 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 339 IEDlPNAGKLKIVHGDIEFKNVSFKY--KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGK 416
Cdd:COG4987   319 VTE-PAEPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGV 397

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 417 NIKEFKQESLRSELSIVPQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEK 496
Cdd:COG4987   398 DLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGER 477

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 497 QRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLI 576
Cdd:COG4987   478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELL 557

                         490
                  ....*....|..
gi 1490918183 577 KEKGLYKKLWNL 588
Cdd:COG4987   558 AQNGRYRQLYQR 569
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 355-565 1.42e-81

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: 253.46  E-value: 1.42e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKY--KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSI 432
Cdd:cd03228     1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQECVLFDDTIYNNIafsnpkakrkdvframkfaqllkivnnfpkkektvvgergvkLSGGEKQRVSIARAILADKKVL 512
Cdd:cd03228    81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 513 VLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGK 565
Cdd:cd03228   119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 355-589 2.22e-80

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: 252.79  E-value: 2.22e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYK--KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSI 432
Cdd:cd03252     1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVL 512
Cdd:cd03252    81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 513 VLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLWNLQ 589
Cdd:cd03252   161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 67-585 1.85e-77

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


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 259.49  E-value: 1.85e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  67 LLSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRI------- 139
Cdd:TIGR03796 185 LVQGRQDWLRPLLLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVqlndqva 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 140 -IRGGSAVERLTDVF-VFNFAPLLFQFTIVaasLLFIGVIPALISFFVVvvfiaysYFINNIQQKSNLQLNQaeDEEKAn 217
Cdd:TIGR03796 265 eFLSGQLATTALDAVmLVFYALLMLLYDPV---LTLIGIAFAAINVLAL-------QLVSRRRVDANRRLQQ--DAGKL- 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 218 ISDVFT---NIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWFSVTRFIAEDITIGT 294
Cdd:TIGR03796 332 TGVAISglqSIETLKASGLESDFFSRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSLNSALILVVGGLRVMEGQLTIGM 411

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 295 MVFLFTVFNNLFGP---LFGFVHGMRNFYRSMADFQDLFKYA---KIKNEIEDLPNAGKLKIVHGDIEFKNVSFKYK--K 366
Cdd:TIGR03796 412 LVAFQSLMSSFLEPvnnLVGFGGTLQELEGDLNRLDDVLRNPvdpLLEEPEGSAATSEPPRRLSGYVELRNITFGYSplE 491

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 367 RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFDDTIYN 446
Cdd:TIGR03796 492 PPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRD 571

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 447 NIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETE 526
Cdd:TIGR03796 572 NLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETE 651

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 527 HEIQADLQKlmEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKL 585
Cdd:TIGR03796 652 KIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
 50-592 1.52e-70

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


Pssm-ID: 130260 [Multi-domain]  Cd Length: 585  Bit Score: 238.25  E-value: 1.52e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  50 LFKEVIDAstrfstkallLSNYTSIlTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHST 129
Cdd:TIGR01192  41 LFGRIIDA----------ISSKSDV-LPTLALWAGFGVFNTIAYVLVAREADRLAHGRRATLLTEAFGRIISMPLSWHQQ 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 130 HKTGSLISRIIRggsAVERLTDVFvfnfapLLFQFTIVAASLLFIGVIPAL------ISFFVVVVFIAYSYFINNIQQKS 203
Cdd:TIGR01192 110 RGTSNALHTLLR---ATETLFGLW------LEFMRQHLATFVALFLLIPTAfamdwrLSIVLMVLGILYILIAKLVMQRT 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 204 nlQLNQAEDEEK-----ANISDVFTNIDSIKYFgkeNRIKSIYRKFAVKTRNALLKNWNYFRW--LDSGQLLILGIGLVL 276
Cdd:TIGR01192 181 --KNGQAAVEHHyhnvfKHVSDSISNVSVVHSY---NRIEAETSALKQFTNNLLSAQYPVLDWwaLASGLNRMASTISMM 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 277 LVWFSVTRFIAE-DITIGTmVFLFTVFNNLfgpLFGFVHGMRNF----YRSMADFQDLFKYAKIKNEIEDLPNAGKLKIV 351
Cdd:TIGR01192 256 CILVIGTVLVIKgELSVGE-VIAFIGFANL---LIGRLDQMSGFitqiFEARAKLEDFFDLEDSVFQREEPADAPELPNV 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 352 HGDIEFKNVSFKY--KKRKIFsDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSE 429
Cdd:TIGR01192 332 KGAVEFRHITFEFanSSQGVF-DVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKS 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 430 LSIVPQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADK 509
Cdd:TIGR01192 411 IATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNA 490

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 510 KVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLwnLQ 589
Cdd:TIGR01192 491 PILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKL--LR 568


                  ...
gi 1490918183 590 KGG 592
Cdd:TIGR01192 569 RSG 571
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 70-587 1.62e-70

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: 240.80  E-value: 1.62e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  70 NYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRIIRGGSAVERL 149
Cdd:TIGR01193 190 KMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDAL 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 150 TDVFVFNFAPLLFqFTIVAASLLFIGVIPALISFFVVVVFIAYSYFINNIQQKSNLQLNQAEDEEKANISDVFTNIDSIK 229
Cdd:TIGR01193 270 ASTILSLFLDMWI-LVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIK 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 230 YFGKEN-RIKSIYRKFAvktrNALLKNWNYFRwLDSGQLLILGIGLVLLV----WFSVTRFIAEDITIGTMVflftVFNN 304
Cdd:TIGR01193 349 SLTSEAeRYSKIDSEFG----DYLNKSFKYQK-ADQGQQAIKAVTKLILNvvilWTGAYLVMRGKLTLGQLI----TFNA 419

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 305 LFGPlfgFVHGMRNfyrsMADFQDLFKYAKIKN-----------EIEDLPNAGKLKIVHGDIEFKNVSFKYK-KRKIFSD 372
Cdd:TIGR01193 420 LLSY---FLTPLEN----IINLQPKLQAARVANnrlnevylvdsEFINKKKRTELNNLNGDIVINDVSYSYGyGSNILSD 492

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 373 FNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFDDTIYNNIAF-S 451
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgA 572

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 452 NPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQA 531
Cdd:TIGR01193 573 KENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVN 652

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183 532 DLQKLMEgRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLWN 587
Cdd:TIGR01193 653 NLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 76-585 1.62e-70

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 240.78  E-value: 1.62e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  76 TIILLVFLAITIFNSAGywLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRIirgGSAVERLTDVFVF 155
Cdd:TIGR00958 203 AIFFMCLLSIASSVSAG--LRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRL---SSDTQTMSRSLSL 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 156 NFAPLLFQFTIVAASLLF-IGVIP--ALISFFVV-VVFIA---YSYFINNIQ---QKSNLQLNQAEDEEKANISDV--FT 223
Cdd:TIGR00958 278 NVNVLLRNLVMLLGLLGFmLWLSPrlTMVTLINLpLVFLAekvFGKRYQLLSeelQEAVAKANQVAEEALSGMRTVrsFA 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 224 --NIDSIKYFGKENRIKSIYRKFAVkTRNALLknWNYfRWLDSGqllilgiGLVLLVWFSVTRFIAEDITIGTMV-FLft 300
Cdd:TIGR00958 358 aeEGEASRFKEALEETLQLNKRKAL-AYAGYL--WTT-SVLGML-------IQVLVLYYGGQLVLTGKVSSGNLVsFL-- 424

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 301 vfnnLFGPLFG-FVHGMRNFYRSMAD----FQDLFKYAKIKNEIedlPNAGKLK--IVHGDIEFKNVSFKYKKR---KIF 370
Cdd:TIGR00958 425 ----LYQEQLGeAVRVLSYVYSGMMQavgaSEKVFEYLDRKPNI---PLTGTLAplNLEGLIEFQDVSFSYPNRpdvPVL 497

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 371 SDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFDDTIYNNIAF 450
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAY 577

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 451 SNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQ 530
Cdd:TIGR00958 578 GLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQ 657

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 531 ADlqKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKL 585
Cdd:TIGR00958 658 ES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 353-571 2.12e-69

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: 223.52  E-value: 2.12e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 353 GDIEFKNVSFKYKK--RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSEL 430
Cdd:cd03244     1 GDIEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQECVLFDDTIYNNIAFSNpKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKK 510
Cdd:cd03244    81 SIIPQDPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 511 VLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGT 571
Cdd:cd03244   160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 353-570 3.56e-67

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: 217.84  E-value: 3.56e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 353 GDIEFKNVSFKYK--KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSEL 430
Cdd:cd03245     1 GRIEFRNVSFSYPnqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKK 510
Cdd:cd03245    81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 511 VLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQG 570
Cdd:cd03245   161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 343-586 1.93e-64

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 221.24  E-value: 1.93e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 343 PNAGKLKIVHGDIEFKNVSFKYKKR--KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKE 420
Cdd:PRK11160  327 PTTSTAAADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 421 FKQESLRSELSIVPQECVLFDDTIYNNIAFSNPKA---KRKDVFRAMKFAQLLkivnNFPKKEKTVVGERGVKLSGGEKQ 497
Cdd:PRK11160  407 YSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNAsdeALIEVLQQVGLEKLL----EDDKGLNAWLGEGGRQLSGGEQR 482

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 498 RVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIK 577
Cdd:PRK11160  483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLA 562


                  ....*....
gi 1490918183 578 EKGLYKKLW 586
Cdd:PRK11160  563 QQGRYYQLK 571
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
106-590 4.36e-62

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 214.96  E-value: 4.36e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 106 RLILDLKRKFFNHIIHLSYNFHSTHKTGSLISR--------IIRGGSAVERLTDVFVFNFAPLLFQFTIVAASLLFIGVI 177
Cdd:PRK10789   66 QLAVELREDFYRQLSRQHPEFYLRHRTGDLMARatndvdrvVFAAGEGVLTLVDSLVMGCAVLIVMSTQISWQLTLLALL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 178 PalisffVVVVFIAYSYFINNIQQK--------SNLQlNQAEDEekanisdvFTNIDSIKYFGKENRIKSiyrKFAVKTR 249
Cdd:PRK10789  146 P------MPVMAIMIKRYGDQLHERfklaqaafSSLN-DRTQES--------LTSIRMIKAFGLEDRQSA---LFAADAE 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 250 NALLKNWNYFRwLDSGqllilgiglvllvwFSVTRFIAeditIGTMVFL------FTVFNN--LFGPLFGFVHGMRNFYR 321
Cdd:PRK10789  208 DTGKKNMRVAR-IDAR--------------FDPTIYIA----IGMANLLaigggsWMVVNGslTLGQLTSFVMYLGLMIW 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 322 SMADFQDLFK--------YAKIKNEIEDLP--NAGKLKIVHG----DIEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVG 387
Cdd:PRK10789  269 PMLALAWMFNivergsaaYSRIRAMLAEAPvvKDGSEPVPEGrgelDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICG 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 388 PSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFA 467
Cdd:PRK10789  349 PTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLA 428

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 468 QLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAH 547
Cdd:PRK10789  429 SVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAH 508

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 1490918183 548 RLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLWNLQK 590
Cdd:PRK10789  509 RLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQ 551
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 351-566 7.12e-60

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: 198.85  E-value: 7.12e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 351 VHGDIEFKNVSFKYKKR---KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLR 427
Cdd:cd03248     8 LKGIVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 428 SELSIVPQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILA 507
Cdd:cd03248    88 SKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 508 DKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKI 566
Cdd:cd03248   168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
353-592 2.20e-59

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 208.03  E-value: 2.20e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 353 GDIEFKNVSFKYKK-RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELS 431
Cdd:PRK10790  339 GRIDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVA 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 432 IVPQECVLFDDTIYNNIAFSNPKAKRKdVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKV 511
Cdd:PRK10790  419 MVQQDPVVLADTFLANVTLGRDISEEQ-VWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 512 LVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKLWNLQKG 591
Cdd:PRK10790  498 LILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLA 577


                  .
gi 1490918183 592 G 592
Cdd:PRK10790  578 G 578
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 338-561 4.02e-58

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: 203.29  E-value: 4.02e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 338 EIEDLPNAGKLKIVHGD---IEFKNVSFKYK-KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILI 413
Cdd:TIGR02857 302 DAAPRPLAGKAPVTAAPassLEFSGVSVAYPgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 414 DGKNIKEFKQESLRSELSIVPQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSG 493
Cdd:TIGR02857 382 NGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSG 461

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 494 GEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVL 561
Cdd:TIGR02857 462 GQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
355-566 2.25e-55

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 186.18  E-value: 2.25e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVP 434
Cdd:COG4619     1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDDTIYNNIAFsnPKAKRKDVFRAMKFAQLLKIVnNFPKK--EKTVvgergVKLSGGEKQRVSIARAILADKKVL 512
Cdd:COG4619    81 QEPALWGGTVRDNLPF--PFQLRERKFDRERALELLERL-GLPPDilDKPV-----ERLSGGERQRLALIRALLLQPDVL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 513 VLDEATSSLDSETEHEIQADLQKLM--EGRTSIIIAHRLSTIMN-ADKIIVLDKGKI 566
Cdd:COG4619   153 LLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 352-571 1.14e-54

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: 184.54  E-value: 1.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 352 HGDIEFKNVSFKYKKR--KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSE 429
Cdd:cd03369     4 HGEIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 430 LSIVPQECVLFDDTIYNNIAFSNpKAKRKDVFRAMKfaqllkivnnfpkkektvVGERGVKLSGGEKQRVSIARAILADK 509
Cdd:cd03369    84 LTIIPQDPTLFSGTIRSNLDPFD-EYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRP 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490918183 510 KVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGT 571
Cdd:cd03369   145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 355-570 6.35e-49

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: 167.88  E-value: 6.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKY--KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFkQESLRSELSI 432
Cdd:cd03247     1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQECVLFDDTIYNNIafsnpkakrkdvframkfaqllkivnnfpkkektvvgerGVKLSGGEKQRVSIARAILADKKVL 512
Cdd:cd03247    80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 513 VLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQG 570
Cdd:cd03247   121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 50-590 7.44e-49

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 183.69  E-value: 7.44e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183   50 LFKEVIDASTRFSTKALLLSNYTSIL-------------TIILLVfLAITIFNSAGywLRMHMINLLDARLILDLKRKFF 116
Cdd:PTZ00265   830 IALSILVAGGLYPVFALLYAKYVSTLfdfanleansnkySLYILV-IAIAMFISET--LKNYYNNVIGEKVEKTMKRRLF 906

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  117 NHIIHLSYNF--HSTHKTGSLISRIIRGGSAVER--LTDVFVFNFAPLLFQFTIVAaSLLFIGVIPALIS---FFVVVVF 189
Cdd:PTZ00265   907 ENILYQEISFfdQDKHAPGLLSAHINRDVHLLKTglVNNIVIFTHFIVLFLVSMVM-SFYFCPIVAAVLTgtyFIFMRVF 985

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  190 IAYSYFINN-------IQQKSNLQLNQAEDEEKAN----ISDVFTNIDSIKYFGKENRIKSIYRKfAVKTRNA-----LL 253
Cdd:PTZ00265   986 AIRARLTANkdvekkeINQPGTVFAYNSDDEIFKDpsflIQEAFYNMNTVIIYGLEDYFCNLIEK-AIDYSNKgqkrkTL 1064

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  254 KNWNYFRWLDSGQLLILGIGLvllvWFSvtRFIAEDITIGTMVFLFTVFNNLF-----GPLFGFVHGMRNFYRSMADFQD 328
Cdd:PTZ00265  1065 VNSMLWGFSQSAQLFINSFAY----WFG--SFLIRRGTILVDDFMKSLFTFLFtgsyaGKLMSLKGDSENAKLSFEKYYP 1138

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  329 LFkyakIKNEIEDLPNAGKLKI-----VHGDIEFKNVSFKYKKRK---IFSDFNLKIPRNKKIALVGPSGSGKTTLIRLL 400
Cdd:PTZ00265  1139 LI----IRKSNIDVRDNGGIRIknkndIKGKIEIMDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLL 1214

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  401 FRLYDV------------------------------------------------------NSGAILIDGKNIKEFKQESL 426
Cdd:PTZ00265  1215 MRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDL 1294

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  427 RSELSIVPQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAIL 506
Cdd:PTZ00265  1295 RNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALL 1374

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  507 ADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMNADKIIVLDK----GKIVQ-QGTHNQLIK-E 578
Cdd:PTZ00265  1375 REPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQ 1454

                          650
                   ....*....|..
gi 1490918183  579 KGLYKKLWNLQK 590
Cdd:PTZ00265  1455 DGVYKKYVKLAK 1466
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 374-585 1.41e-47

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 175.42  E-value: 1.41e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 374 NLKIPRNKKIALVGPSGSGKTTLIRLL--FRLYdvnSGAILIDGKNIKEFKQESLRSELSIVPQECVLFDDTIYNNIAFS 451
Cdd:PRK11174  370 NFTLPAGQRIALVGPSGAGKTSLLNALlgFLPY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG 446

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 452 NPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQA 531
Cdd:PRK11174  447 NPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ 526

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1490918183 532 DLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKL 585
Cdd:PRK11174  527 ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 355-579 4.70e-47

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: 164.81  E-value: 4.70e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKY-KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIV 433
Cdd:COG1122     1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 PQ--ECVLFDDTIYNNIAFS--N---PKAKRKD-VFRAMKFAQLLKIVNNFPKKektvvgergvkLSGGEKQRVSIArAI 505
Cdd:COG1122    81 FQnpDDQLFAPTVEEDVAFGpeNlglPREEIRErVEEALELVGLEHLADRPPHE-----------LSGGQKQRVAIA-GV 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 506 LA-DKKVLVLDEATSSLDSETEHEIQADLQKL-MEGRTSIIIAHRLSTIM-NADKIIVLDKGKIVQQGTHNQLIKEK 579
Cdd:COG1122   149 LAmEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPREVFSDY 225
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 355-565 8.51e-47

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: 163.02  E-value: 8.51e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRK-----IFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKnikefkqeslrse 429
Cdd:cd03250     1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 430 LSIVPQECVLFDDTIYNNIAFSNP--KAKRKDVFRAmkfAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILA 507
Cdd:cd03250    68 IAYVSQEPWIQNGTIRENILFGKPfdEERYEKVIKA---CALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 508 DKKVLVLDEATSSLDSETEHEI--QADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGK 565
Cdd:cd03250   145 DADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
355-578 5.67e-46

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 162.16  E-value: 5.67e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQEsLRSELSIVP 434
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDD-TIYNNIAF-----SNPKAKRKDvframKFAQLLKIVnNFPKKEKTVVGergvKLSGGEKQRVSIARAILAD 508
Cdd:COG1131    80 QEPALYPDlTVRENLRFfarlyGLPRKEARE-----RIDELLELF-GLTDAADRKVG----TLSGGMKQRLGLALALLHD 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490918183 509 KKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIA-HRLSTI-MNADKIIVLDKGKIVQQGTHNQLIKE 578
Cdd:COG1131   150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 341-549 1.39e-45

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: 169.08  E-value: 1.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 341 DLPNAGKLKIVHGDIEFKNVSFKYK-KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIK 419
Cdd:TIGR02868 321 SAPAAGAVGLGKPTLELRDLSAGYPgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 420 EFKQESLRSELSIVPQECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRV 499
Cdd:TIGR02868 401 SLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRL 480

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1490918183 500 SIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRL 549
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 355-566 6.90e-45

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: 156.99  E-value: 6.90e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKY--KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSI 432
Cdd:cd03246     1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQECVLFDDTIYNNIafsnpkakrkdvframkfaqllkivnnfpkkektvvgergvkLSGGEKQRVSIARAILADKKVL 512
Cdd:cd03246    81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 513 VLDEATSSLDSETEHEIQADLQKL-MEGRTSIIIAHRLSTIMNADKIIVLDKGKI 566
Cdd:cd03246   119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 355-576 1.93e-44

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: 158.23  E-value: 1.93e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKK-RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIV 433
Cdd:cd03295     1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 PQECVLFDD-TIYNNIAF-----SNPKAKRKDvfRAmkfAQLLKIVNNFPKKektvVGER-GVKLSGGEKQRVSIARAIL 506
Cdd:cd03295    81 IQQIGLFPHmTVEENIALvpkllKWPKEKIRE--RA---DELLALVGLDPAE----FADRyPHELSGGQQQRVGVARALA 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 507 ADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRL-STIMNADKIIVLDKGKIVQQGTHNQLI 576
Cdd:cd03295   152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 356-565 2.59e-44

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: 154.71  E-value: 2.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 356 EFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQ 435
Cdd:cd00267     1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 436 ecvlfddtiynniafsnpkakrkdvframkfaqllkivnnfpkkektvvgergvkLSGGEKQRVSIARAILADKKVLVLD 515
Cdd:cd00267    81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1490918183 516 EATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMNA-DKIIVLDKGK 565
Cdd:cd00267   106 EPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 355-575 2.63e-44

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: 157.34  E-value: 2.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVN-----SGAILIDGKNIKEFKQ--ESLR 427
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVdvLELR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 428 SELSIVPQECVLFDDTIYNNIAFSnPKA---KRKDVFRAmKFAQLLKIVNNFPKkektvVGER--GVKLSGGEKQRVSIA 502
Cdd:cd03260    81 RRVGMVFQKPNPFPGSIYDNVAYG-LRLhgiKLKEELDE-RVEEALRKAALWDE-----VKDRlhALGLSGGQQQRLCLA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 503 RAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAH------RLstimnADKIIVLDKGKIVQQGTHNQL 575
Cdd:cd03260   154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFGPTEQI 227
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 355-577 4.29e-44

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: 156.89  E-value: 4.29e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNI---KEFKQESLRSELS 431
Cdd:cd03261     1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRRMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 432 IVPQECVLFDD-TIYNNIAFsnpkakRKDVFRAMKFAQLLKIVnnfpkKEK-TVVGERGVK------LSGGEKQRVSIAR 503
Cdd:cd03261    81 MLFQSGALFDSlTVFENVAF------PLREHTRLSEEEIREIV-----LEKlEAVGLRGAEdlypaeLSGGMKKRVALAR 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 504 AILADKKVLVLDEATSSLDSETEHEIQA---DLQKLMeGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLIK 577
Cdd:cd03261   150 ALALDPELLLYDEPTAGLDPIASGVIDDlirSLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 353-582 6.67e-44

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: 168.59  E-value: 6.67e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  353 GDIEFKNVSFKYKK--RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSEL 430
Cdd:TIGR00957 1283 GRVEFRNYCLRYREdlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKI 1362

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  431 SIVPQECVLFDDTIYNNI-AFSnpKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADK 509
Cdd:TIGR00957 1363 TIIPQDPVLFSGSLRMNLdPFS--QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKT 1440

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183  510 KVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLY 582
Cdd:TIGR00957 1441 KILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 355-571 7.17e-44

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: 156.68  E-value: 7.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQE---SLRSELS 431
Cdd:COG1127     6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRIG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 432 IVPQECVLFDD-TIYNNIAFS-------NPKAKRKDVFRAMKFAQLLKIVNNFPkkektvvGErgvkLSGGEKQRVSIAR 503
Cdd:COG1127    86 MLFQGGALFDSlTVFENVAFPlrehtdlSEAEIRELVLEKLELVGLPGAADKMP-------SE----LSGGMRKRVALAR 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490918183 504 AILADKKVLVLDEATSSLDSETEHEIQA---DLQKLMeGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGT 571
Cdd:COG1127   155 ALALDPEILLYDEPTAGLDPITSAVIDElirELRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGT 225
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
355-567 2.67e-43

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 154.44  E-value: 2.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKK-RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQES---LRSEL 430
Cdd:COG2884     2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQECVLFDD-TIYNNIAFS------NPKAKRKDVFRAMKFAQLLKIVNNFPkkektvvgergVKLSGGEKQRVSIAR 503
Cdd:COG2884    82 GVVFQDFRLLPDrTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGEQQRVAIAR 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 504 AILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIA-HRLSTI--MNAdKIIVLDKGKIV 567
Cdd:COG2884   151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVdrMPK-RVLELEDGRLV 216
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 353-578 1.13e-42

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: 161.45  E-value: 1.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 353 GDIEFKNVSFKY--KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSEL 430
Cdd:COG4618   329 GRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHI 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQECVLFDDTIYNNIA-FsnPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADK 509
Cdd:COG4618   409 GYLPQDVELFDGTIAENIArF--GDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDP 486

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 510 KVLVLDEATSSLDSETEHEIQADLQKL-MEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKE 578
Cdd:COG4618   487 RLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 356-565 7.24e-42

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: 149.92  E-value: 7.24e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 356 EFKNVSFKY--KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIV 433
Cdd:cd03225     1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 PQ--ECVLFDDTIYNNIAFS--NPKAKRKDVfrAMKFAQLLKIVnNFPKKEKTVVGErgvkLSGGEKQRVSIARAILADK 509
Cdd:cd03225    81 FQnpDDQFFGPTVEEEVAFGleNLGLPEEEI--EERVEEALELV-GLEGLRDRSPFT----LSGGQKQRVAIAGVLAMDP 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 510 KVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMN-ADKIIVLDKGK 565
Cdd:cd03225   154 DILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
PLN03232 PLN03232
ABC transporter C family member; Provisional
 49-580 7.67e-42

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 162.45  E-value: 7.67e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183   49 YLFKEVIDASTR----FSTKALLLSNYTS---ILTIILLVF--LAITIFNSagYWL---RMHMINLL-DARLildlkrkf 115
Cdd:PLN03232   921 YLTTEVLRVSSStwlsIWTDQSTPKSYSPgfyIVVYALLGFgqVAVTFTNS--FWLissSLHAAKRLhDAML-------- 990

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  116 fNHIIHLSYNFHSTHKTGSLISRIIRGGSAVER----LTDVFVFNFAPLLFQFTIVA--ASLLFIGVIPALISFFVvvvf 189
Cdd:PLN03232   991 -NSILRAPMLFFHTNPTGRVINRFSKDIGDIDRnvanLMNMFMNQLWQLLSTFALIGtvSTISLWAIMPLLILFYA---- 1065

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  190 iAYSYFINNIQQKSNLQlNQAEDEEKANISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLI 269
Cdd:PLN03232  1066 -AYLYYQSTSREVRRLD-SVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETL 1143

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  270 LGIGLVLLVWFSVTRFIAEDITIG---TMVFLFTVFNNLFGPLFGFVHGMRNFYRSMADFQDLFKYAKIKNEIEDL---- 342
Cdd:PLN03232  1144 GGVMIWLTATFAVLRNGNAENQAGfasTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIienn 1223

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  343 -PNAGKlkIVHGDIEFKNVSFKYKKR--KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIK 419
Cdd:PLN03232  1224 rPVSGW--PSRGSIKFEDVHLRYRPGlpPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA 1301

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  420 EFKQESLRSELSIVPQECVLFDDTIYNNI-AFSnpKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQR 498
Cdd:PLN03232  1302 KFGLTDLRRVLSIIPQSPVLFSGTVRFNIdPFS--EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQL 1379

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  499 VSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKE 578
Cdd:PLN03232  1380 LSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSR 1459


                   ..
gi 1490918183  579 KG 580
Cdd:PLN03232  1460 DT 1461
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 355-570 8.70e-42

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


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 149.98  E-value: 8.70e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIkeFKQESLRSELSIVP 434
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIGMVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDD-TIYNNIAF-----SNPKAKRKDvfRAMKFAQLLKIVNnfpkkektvVGERGV-KLSGGEKQRVSIARAILA 507
Cdd:cd03259    79 QDYALFPHlTVAENIAFglklrGVPKAEIRA--RVRELLELVGLEG---------LLNRYPhELSGGQQQRVALARALAR 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183 508 DKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:cd03259   148 EPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 355-571 9.62e-42

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: 150.42  E-value: 9.62e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKY----KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESL---R 427
Cdd:cd03258     2 IELKNVSKVFgdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 428 SELSIVPQECVLFDD-TIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVN------NFPKKektvvgergvkLSGGEKQRVS 500
Cdd:cd03258    82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELVGledkadAYPAQ-----------LSGGQKQRVG 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490918183 501 IARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGT 571
Cdd:cd03258   151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 355-571 2.35e-41

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: 150.19  E-value: 2.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVP 434
Cdd:COG1120     2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVL-FDDTIYNNIA---------FSNPKAK-RKDVFRAMKFAQLLKIVnnfpkkektvvgERGV-KLSGGEKQRVSIA 502
Cdd:COG1120    82 QEPPApFGLTVRELVAlgryphlglFGRPSAEdREAVEEALERTGLEHLA------------DRPVdELSGGERQRVLIA 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 503 RAILADKKVLVLDEATSSLDseteheI--QADLQKLM------EGRTSIIIAHRLS-TIMNADKIIVLDKGKIVQQGT 571
Cdd:COG1120   150 RALAQEPPLLLLDEPTSHLD------LahQLEVLELLrrlareRGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 355-570 6.45e-41

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: 148.04  E-value: 6.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKR----KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNI---KEFKQESLR 427
Cdd:cd03257     2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklSRRLRKIRR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 428 SELSIVPQecvlfdD---------TIYNNIA--FSNPKAKRKDVFRAMKFAQLLKIVNNfpkkEKTVVGERGVKLSGGEK 496
Cdd:cd03257    82 KEIQMVFQ------DpmsslnprmTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGL----PEEVLNRYPHELSGGQR 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 497 QRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:cd03257   152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 355-565 1.04e-40

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: 145.79  E-value: 1.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNI--KEFKQESLRSELSI 432
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRRIGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQECVLFDD-TIYNNIAFSnpkakrkdvframkfaqllkivnnfpkkektvvgergvkLSGGEKQRVSIARAILADKKV 511
Cdd:cd03229    81 VFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDV 121

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 512 LVLDEATSSLDSETEHEIQADLQKL--MEGRTSIIIAHRLSTIMN-ADKIIVLDKGK 565
Cdd:cd03229   122 LLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 355-569 4.43e-40

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: 145.31  E-value: 4.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKY----KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEfkqesLRSEL 430
Cdd:cd03293     1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQECVLFD-DTIYNNIAFS-----NPKAKRKDVFRAM-KFAQLLKIVNNFPKkektvvgergvKLSGGEKQRVSIAR 503
Cdd:cd03293    76 GYVFQQDALLPwLTVLDNVALGlelqgVPKAEARERAEELlELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 504 AILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLS-TIMNADKIIVLDK--GKIVQQ 569
Cdd:cd03293   145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 356-570 4.65e-40

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: 144.12  E-value: 4.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 356 EFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQ 435
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 436 ecvlfddtiynniafsnpkakrkdvfrAMKFAQLLKIVnnfpkkektvvgERGVK-LSGGEKQRVSIARAILADKKVLVL 514
Cdd:cd03214    81 ---------------------------ALELLGLAHLA------------DRPFNeLSGGERQRVLLARALAQEPPILLL 121

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 515 DEATSSLDSETEHEIQADLQKL--MEGRTSIIIAHRLS-TIMNADKIIVLDKGKIVQQG 570
Cdd:cd03214   122 DEPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 319-590 7.93e-40

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 156.34  E-value: 7.93e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  319 FYRSMADFQDLFKYAKIKNEIEDLPNAGKLKIVHgDIEFKNVSFKYKKRK---IFSDFNLKIPRNKKIALVGPSGSGKTT 395
Cdd:PTZ00265   348 YMKSLEATNSLYEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKST 426

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  396 LIRLLFRLYDVNSGAILI-DGKNIKEFKQESLRSELSIVPQECVLFDDTIYNNIAFS----------------------N 452
Cdd:PTZ00265   427 ILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqE 506

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  453 PKAKRK-----------DVFRAMKFAQLLKIVNNF------------------------PKKEKTVVGERGVKLSGGEKQ 497
Cdd:PTZ00265   507 NKNKRNscrakcagdlnDMSNTTDSNELIEMRKNYqtikdsevvdvskkvlihdfvsalPDKYETLVGSNASKLSGGQKQ 586

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  498 RVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLM--EGRTSIIIAHRLSTIMNADKIIVL-------------- 561
Cdd:PTZ00265   587 RISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdii 666

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183  562 ------------------DKGK---------------IVQQGTHNQLIKEK-GLYKKLWNLQK 590
Cdd:PTZ00265   667 gedptkdnkennnknnkdDNNNnnnnnnnkinnagsyIIEQGTHDALMKNKnGIYYTMINNQK 729
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 354-571 7.64e-39

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 146.01  E-value: 7.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 354 DIEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIkefkqESLRSE---L 430
Cdd:COG3842     5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLPPEkrnV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQECVLFDD-TIYNNIAFS-----NPKAKRKDvfRAMKFAQLLKIVNnfpkkektvVGERGVK-LSGGEKQRVSIAR 503
Cdd:COG3842    80 GMVFQDYALFPHlTVAENVAFGlrmrgVPKAEIRA--RVAELLELVGLEG---------LADRYPHqLSGGQQQRVALAR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 504 AILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLS---TImnADKIIVLDKGKIVQQGT 571
Cdd:COG3842   149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 355-576 8.53e-39

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: 149.67  E-value: 8.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKR-----KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQES---L 426
Cdd:COG1123   261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreL 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 427 RSELSIVPQecvlfD--------DTIYNNIAFS------NPKAKRKDvfRAmkfAQLLKIV-------NNFPkkektvvG 485
Cdd:COG1123   341 RRRVQMVFQ-----DpysslnprMTVGDIIAEPlrlhglLSRAERRE--RV---AELLERVglppdlaDRYP-------H 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 486 ErgvkLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQ---ADLQKLMeGRTSIIIAHRLSTIMN-ADKIIVL 561
Cdd:COG1123   404 E----LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILnllRDLQREL-GLTYLFISHDLAVVRYiADRVAVM 478

                         250
                  ....*....|....*
gi 1490918183 562 DKGKIVQQGTHNQLI 576
Cdd:COG1123   479 YDGRIVEDGPTEEVF 493
PLN03130 PLN03130
ABC transporter C family member; Provisional
 353-585 1.75e-38

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 152.20  E-value: 1.75e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  353 GDIEFKNVSFKYKKR--KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSEL 430
Cdd:PLN03130  1236 GSIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  431 SIVPQECVLFDDTIYNNIAFSNpKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKK 510
Cdd:PLN03130  1316 GIIPQAPVLFSGTVRFNLDPFN-EHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183  511 VLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLI-KEKGLYKKL 585
Cdd:PLN03130  1395 ILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLsNEGSAFSKM 1470
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 355-566 1.84e-38

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: 140.74  E-value: 1.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQE--SLRSELSI 432
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQECVLFDD-TIYNNIAFSNPKAKRKDVFRAMKFA-QLLKIVNNFPKKEKtvvgeRGVKLSGGEKQRVSIARAILADKK 510
Cdd:cd03262    81 VFQQFNLFPHlTVLENITLAPIKVKGMSKAEAEERAlELLEKVGLADKADA-----YPAQLSGGQQQRVAIARALAMNPK 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 511 VLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMN-ADKIIVLDKGKI 566
Cdd:cd03262   156 VMLFDEPTSALDPELVGEVLDVMKDLAeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 355-567 2.09e-38

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 142.15  E-value: 2.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRK----IFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEfkqesLRSEL 430
Cdd:COG1116     8 LELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQECVLFD-DTIYNNIAF-----SNPKAKRKDvfRAMkfaQLLKIV------NNFPKKektvvgergvkLSGGEKQR 498
Cdd:COG1116    83 GVVFQEPALLPwLTVLDNVALglelrGVPKAERRE--RAR---ELLELVglagfeDAYPHQ-----------LSGGMRQR 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 499 VSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAH------RLstimnADKIIVLDK--GKIV 567
Cdd:COG1116   147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIV 220
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 355-566 3.35e-38

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 140.99  E-value: 3.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEfkqesLRSELSIVP 434
Cdd:COG1121     7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 Q-------------ECVLFddTIYNNI-AFSNPKAKRKD-VFRAMKFAQLLKIvnnfpkkEKTVVGErgvkLSGGEKQRV 499
Cdd:COG1121    82 QraevdwdfpitvrDVVLM--GRYGRRgLFRRPSRADREaVDEALERVGLEDL-------ADRPIGE----LSGGQQQRV 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 500 SIARAILADKKVLVLDEATSSLDSETEHEIQADLQKL-MEGRTSIIIAHRLSTIM-NADKIIVLDKGKI 566
Cdd:COG1121   149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVReYFDRVLLLNRGLV 217
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 337-585 6.36e-38

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: 140.81  E-value: 6.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 337 NEIEDLPNAGkLKIVHGDIEFKNVSFKYKK--RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILID 414
Cdd:cd03288     3 ASISGSSNSG-LVGLGGEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVID 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 415 GKNIKEFKQESLRSELSIVPQECVLFDDTIYNNIafsNPKAKRKD--VFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLS 492
Cdd:cd03288    82 GIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECKCTDdrLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 493 GGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGT- 571
Cdd:cd03288   159 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTp 238

                         250
                  ....*....|....
gi 1490918183 572 HNQLIKEKGLYKKL 585
Cdd:cd03288   239 ENLLAQEDGVFASL 252
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 355-592 8.23e-38

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


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 140.64  E-value: 8.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYK--KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDG------KNIKEfkqesL 426
Cdd:TIGR04520   1 IEVENVSFSYPesEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtldeENLWE-----I 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 427 RSELSIVPQ-----------EcvlfDDtiynnIAFS--NPKAKRKDVFRAMKFAqlLKIVN--NFPKKEKTvvgergvKL 491
Cdd:TIGR04520  76 RKKVGMVFQnpdnqfvgatvE----DD-----VAFGleNLGVPREEMRKRVDEA--LKLVGmeDFRDREPH-------LL 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 492 SGGEKQRVSIArAILA-DKKVLVLDEATSSLDSETEHEIQADLQKLM--EGRTSIIIAHRLSTIMNADKIIVLDKGKIVQ 568
Cdd:TIGR04520 138 SGGQKQRVAIA-GVLAmRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVA 216

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1490918183 569 QGT------HNQLIKEKGL-----YKKLWNLQKGG 592
Cdd:TIGR04520 217 EGTpreifsQVELLKEIGLdvpfiTELAKALKKRG 251
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 355-566 8.73e-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: 137.53  E-value: 8.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEfKQESLRSELSIVP 434
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDD-TIYNNIafsnpkakrkdvframkfaqllkivnnfpkkektvvgergvKLSGGEKQRVSIARAILADKKVLV 513
Cdd:cd03230    80 EEPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPELLI 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 514 LDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMN-ADKIIVLDKGKI 566
Cdd:cd03230   119 LDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 355-566 1.82e-37

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: 138.39  E-value: 1.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYK----KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNI---KEFKQESLR 427
Cdd:cd03255     1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklSEKELAAFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 428 SE-LSIVPQECVLFDD-TIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNnFPKKEKTVVGErgvkLSGGEKQRVSIARAI 505
Cdd:cd03255    81 RRhIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERAEELLERVG-LGDRLNHYPSE----LSGGQQQRVAIARAL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 506 LADKKVLVLDEATSSLDSETEHEIQADLQKL--MEGRTSIIIAHRLSTIMNADKIIVLDKGKI 566
Cdd:cd03255   156 ANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 353-571 2.31e-37

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 141.75  E-value: 2.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 353 GDIEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEfkqesLRSE--- 429
Cdd:COG3839     2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD-----LPPKdrn 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 430 LSIVPQECVLFDD-TIYNNIAFS-----NPKAKRKDvfRAMKFAQLLKI---VNNFPKkektvvgergvKLSGGEKQRVS 500
Cdd:COG3839    77 IAMVFQSYALYPHmTVYENIAFPlklrkVPKAEIDR--RVREAAELLGLedlLDRKPK-----------QLSGGQRQRVA 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183 501 IARAILADKKVLVLDEATSSLD----SETEHEIQADLQKLmeGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGT 571
Cdd:COG3839   144 LGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL--GTTTIYVTHDQVEAMTlADRIAVMNDGRIQQVGT 217
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
355-571 3.02e-37

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 141.37  E-value: 3.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVS--FKYKKRKI--FSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESL---R 427
Cdd:COG1135     2 IELENLSktFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 428 SELSIVPQECVLFDD-TIYNNIAFS-----NPKAKRKDvframKFAQLLKIV------NNFPKKektvvgergvkLSGGE 495
Cdd:COG1135    82 RKIGMIFQHFNLLSSrTVAENVALPleiagVPKAEIRK-----RVAELLELVglsdkaDAYPSQ-----------LSGGQ 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 496 KQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGT 571
Cdd:COG1135   146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
355-569 5.40e-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: 5.40e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYK----KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESL---- 426
Cdd:COG1136     5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 427 RSELSIVPQECVLFDD-TIYNNIAF-----SNPKAKRKDvfRAMkfaQLLKIV------NNFPKKektvvgergvkLSGG 494
Cdd:COG1136    85 RRHIGFVFQFFNLLPElTALENVALplllaGVSRKERRE--RAR---ELLERVglgdrlDHRPSQ-----------LSGG 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 495 EKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMNADKIIVLDKGKIVQQ 569
Cdd:COG1136   149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 370-519 6.82e-37

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 134.31  E-value: 6.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 370 FSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFDD-TIYNNI 448
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 449 AFSnpkAKRKDVFRAMKFAQLLKIVNNF--PKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATS 519
Cdd:pfam00005  81 RLG---LLLKGLSKREKDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 355-571 7.20e-37

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 137.43  E-value: 7.20e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQE--SLRSELSI 432
Cdd:COG1126     2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRRKVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQECVLFDD-TIYNNIAFSNPKAKRKDVFRAMKFA-QLLKIV------NNFPKkektvvgergvKLSGGEKQRVSIARA 504
Cdd:COG1126    82 VFQQFNLFPHlTVLENVTLAPIKVKKMSKAEAEERAmELLERVgladkaDAYPA-----------QLSGGQQQRVAIARA 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 505 ILADKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRlstiMN-----ADKIIVLDKGKIVQQGT 571
Cdd:COG1126   151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAkEGMTMVVVTHE----MGfarevADRVVFMDGGRIVEEGP 219
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 355-576 1.78e-36

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 142.73  E-value: 1.78e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFS--DFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVN---SGAILIDGKNIKEFKQESLRSE 429
Cdd:COG1123     5 LEVRDLSVRYPGGDVPAvdGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 430 LSIVPQE--CVLFDDTIYNNIAFS------NPKAKRKDVFRAMKFAQLLKIVNNFPKKektvvgergvkLSGGEKQRVSI 501
Cdd:COG1123    85 IGMVFQDpmTQLNPVTVGDQIAEAlenlglSRAEARARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAI 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 502 ARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLI 576
Cdd:COG1123   154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEIL 231
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 356-566 4.02e-36

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: 134.20  E-value: 4.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 356 EFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFkqeslRSELSIVPQ 435
Cdd:cd03235     1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 436 -------------ECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVN-NFpkkektvvGErgvkLSGGEKQRVSI 501
Cdd:cd03235    76 rrsidrdfpisvrDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADrQI--------GE----LSGGQQQRVLL 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 502 ARAILADKKVLVLDEATSSLDSETEHEIQADLQKL-MEGRTSIIIAHRLSTIMN-ADKIIVLDKGKI 566
Cdd:cd03235   144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 355-570 4.11e-36

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: 134.24  E-value: 4.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPrNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQEsLRSELSIVP 434
Cdd:cd03264     1 LQLENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDD-TIYNNIAFS------NPKAKRKDVframkfAQLLKIVNNFPKKEKTVVgergvKLSGGEKQRVSIARAILA 507
Cdd:cd03264    79 QEFGVYPNfTVREFLDYIawlkgiPSKEVKARV------DEVLELVNLGDRAKKKIG-----SLSGGMRRRVGIAQALVG 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490918183 508 DKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTI-MNADKIIVLDKGKIVQQG 570
Cdd:cd03264   148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFEG 211
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 355-570 1.76e-35

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: 132.76  E-value: 1.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQEslRSELSIVP 434
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAMVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDD-TIYNNIAFSNPKAK-RKDVF--RAMKFAQLLKIVNNFPKKEKTvvgergvkLSGGEKQRVSIARAILADKK 510
Cdd:cd03301    79 QNYALYPHmTVYDNIAFGLKLRKvPKDEIdeRVREVAELLQIEHLLDRKPKQ--------LSGGQRQRVALGRAIVREPK 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 511 VLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:cd03301   151 VFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 355-571 1.92e-35

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: 133.13  E-value: 1.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQEslRSELSIVP 434
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDD-TIYNNIAF------SNPKAKRKDVFRAMKFAQLLKIVNNFPKkektvvgergvKLSGGEKQRVSIARAILA 507
Cdd:cd03300    79 QNYALFPHlTVFENIAFglrlkkLPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALVN 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 508 DKKVLVLDEATSSLDSETEHEIQADLQKL--MEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGT 571
Cdd:cd03300   148 EPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGT 214
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 355-571 4.07e-34

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 129.92  E-value: 4.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKK----RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSEL 430
Cdd:COG1124     2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQEcvlfddtiynniAFS--NPkakRKDVFRAMkfAQLLKIvNNFPKKEKTV------VG-ERGVK------LSGGE 495
Cdd:COG1124    82 QMVFQD------------PYAslHP---RHTVDRIL--AEPLRI-HGLPDREERIaelleqVGlPPSFLdryphqLSGGQ 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 496 KQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTI--MnADKIIVLDKGKIVQQGT 571
Cdd:COG1124   144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVahL-CDRVAVMQNGRIVEELT 222
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
355-576 4.54e-34

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 129.44  E-value: 4.54e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIK--EFKQESLRSELSI 432
Cdd:PRK09493    2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQECVLFDD-TIYNNIAFSnP----KAKRKDVfRAMKFAQLLKI-----VNNFPKkektvvgergvKLSGGEKQRVSIA 502
Cdd:PRK09493   82 VFQQFYLFPHlTALENVMFG-PlrvrGASKEEA-EKQARELLAKVglaerAHHYPS-----------ELSGGQQQRVAIA 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183 503 RAILADKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLI 576
Cdd:PRK09493  149 RALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 355-575 1.47e-33

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 128.25  E-value: 1.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYK-KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESL---RSEL 430
Cdd:COG3638     3 LELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlRRRI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQEcvlfddtiYNNIafsnpkaKRKDVFRA--------MKFAQLLkiVNNFPKKEKTV-------VG------ERGV 489
Cdd:COG3638    83 GMIFQQ--------FNLV-------PRLSVLTNvlagrlgrTSTWRSL--LGLFPPEDRERalealerVGladkayQRAD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 490 KLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKI 566
Cdd:COG3638   146 QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDGRV 225


                  ....*....
gi 1490918183 567 VQQGTHNQL 575
Cdd:COG3638   226 VFDGPPAEL 234
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 355-577 4.99e-33

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: 126.68  E-value: 4.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIfSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQEslRSELSIVP 434
Cdd:cd03299     1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDD-TIYNNIAF-----SNPKAKRKDvfRAMKFAQLLKIVNNFPKKEKTvvgergvkLSGGEKQRVSIARAILAD 508
Cdd:cd03299    78 QNYALFPHmTVYKNIAYglkkrKVDKKEIER--KVLEIAEMLGIDHLLNRKPET--------LSGGEQQRVAIARALVVN 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490918183 509 KKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTI-MNADKIIVLDKGKIVQQGTHNQLIK 577
Cdd:cd03299   148 PKILLLDEPFSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFK 219
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 355-566 6.67e-33

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


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 125.60  E-value: 6.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKR-KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQES---LRSEL 430
Cdd:cd03292     1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQEC-VLFDDTIYNNIAFS------NPKAKRKDVFRAMKFAQLLKIVNNFPKKektvvgergvkLSGGEKQRVSIAR 503
Cdd:cd03292    81 GVVFQDFrLLPDRNVYENVAFAlevtgvPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 504 AILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADK--IIVLDKGKI 566
Cdd:cd03292   150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 355-571 7.06e-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: 126.30  E-value: 7.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKefKQESLRSELSIVP 434
Cdd:cd03296     3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVGFVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDD-TIYNNIAF---------SNPKAK-RKDVFRAMKFAQLLKIVNNFPKkektvvgergvKLSGGEKQRVSIAR 503
Cdd:cd03296    81 QHYALFRHmTVFDNVAFglrvkprseRPPEAEiRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVALAR 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 504 AILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGT 571
Cdd:cd03296   150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGT 220
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 355-579 1.03e-32

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 125.76  E-value: 1.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYK-KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRS----- 428
Cdd:cd03256     1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrqi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 429 -----ELSIVPQ----ECVLF----DDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNfpkkektvvgeRGVKLSGGE 495
Cdd:cd03256    81 gmifqQFNLIERlsvlENVLSgrlgRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQ-----------RADQLSGGQ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 496 KQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKL--MEGRTSIIIAHRLSTIM-NADKIIVLDKGKIVQQGTH 572
Cdd:cd03256   150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPP 229


                  ....*..
gi 1490918183 573 NQLIKEK 579
Cdd:cd03256   230 AELTDEV 236
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 355-575 1.21e-32

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 125.92  E-value: 1.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGA-----ILIDGKNI--KEFKQESLR 427
Cdd:COG1117    12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIydPDVDVVELR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 428 SELSIVPQECVLFDDTIYNNIAFS------NPKAKRKD-VFRAMKFAQLLKIVnnfpkkeKTVVGERGVKLSGGEKQRVS 500
Cdd:COG1117    92 RRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEiVEESLRKAALWDEV-------KDRLKKSALGLSGGQQQRLC 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 501 IARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAH------RLStimnaDKIIVLDKGKIVQQGTHNQ 574
Cdd:COG1117   165 IARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYLGELVEFGPTEQ 239


                  .
gi 1490918183 575 L 575
Cdd:COG1117   240 I 240
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
355-578 3.07e-32

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 127.51  E-value: 3.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRseLSIVP 434
Cdd:PRK10851    3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDD-TIYNNIAFS----------NPKAKRKDVFRAMKFAQLLKIVNNFPKkektvvgergvKLSGGEKQRVSIAR 503
Cdd:PRK10851   81 QHYALFRHmTVFDNIAFGltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYPA-----------QLSGGQKQRVALAR 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 504 AILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLIKE 578
Cdd:PRK10851  150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQVWRE 227
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 355-571 6.63e-32

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 126.41  E-value: 6.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNikefkqesLRSELSI-- 432
Cdd:COG1118     3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD--------LFTNLPPre 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 -----VPQECVLFDD-TIYNNIAF------SNPKAKRKDVFRAMKFAQLLKIVNNFPKkektvvgergvKLSGGEKQRVS 500
Cdd:COG1118    75 rrvgfVFQHYALFPHmTVAENIAFglrvrpPSKAEIRARVEELLELVQLEGLADRYPS-----------QLSGGQRQRVA 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 501 IARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAH------RLstimnADKIIVLDKGKIVQQGT 571
Cdd:COG1118   144 LARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGT 217
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
355-571 2.06e-31

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 125.83  E-value: 2.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQEslRSELSIVP 434
Cdd:PRK09452   15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDD-TIYNNIAFS-----NPKAK-RKDVFRAMKFAQLLKIVNNFPKkektvvgergvKLSGGEKQRVSIARAILA 507
Cdd:PRK09452   93 QSYALFPHmTVFENVAFGlrmqkTPAAEiTPRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVN 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 508 DKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAH----RLStiMnADKIIVLDKGKIVQQGT 571
Cdd:PRK09452  162 KPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdqeeALT--M-SDRIVVMRDGRIEQDGT 228
cbiO PRK13637
energy-coupling factor transporter ATPase;
355-578 8.36e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 121.69  E-value: 8.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKK-----RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNI--KEFKQESLR 427
Cdd:PRK13637    3 IKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 428 SELSIVPQ--ECVLFDDTIYNNIAF-------SNPKAKRKdVFRAMKFAQLlkivnnfpkKEKTVVGERGVKLSGGEKQR 498
Cdd:PRK13637   83 KKVGLVFQypEYQLFEETIEKDIAFgpinlglSEEEIENR-VKRAMNIVGL---------DYEDYKDKSPFELSGGQKRR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 499 VSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQL 575
Cdd:PRK13637  153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREV 232


                  ...
gi 1490918183 576 IKE 578
Cdd:PRK13637  233 FKE 235
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 355-579 2.29e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 120.10  E-value: 2.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYK--KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSI 432
Cdd:PRK13632    8 IKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQ--ECVLFDDTIYNNIAFS--NPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTvvgergvKLSGGEKQRVSIARAILAD 508
Cdd:PRK13632   88 IFQnpDNQFIGATVEDDIAFGleNKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQ-------NLSGGQKQRVAIASVLALN 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490918183 509 KKVLVLDEATSSLDSETEHEIQA---DLQKLMEgRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEK 579
Cdd:PRK13632  161 PEIIIFDESTSMLDPKGKREIKKimvDLRKTRK-KTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 358-567 3.69e-30

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: 117.36  E-value: 3.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 358 KNVSFKYKK-RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKqesLRSELSIVPQE 436
Cdd:cd03226     3 ENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 437 C--VLFDDTIYNNIAFSNPKAKRKdvfrAMKFAQLLKIVNNFPKKEKtvvgeRGVKLSGGEKQRVSIARAILADKKVLVL 514
Cdd:cd03226    80 VdyQLFTDSVREELLLGLKELDAG----NEQAETVLKDLDLYALKER-----HPLSLSGGQKQRLAIAAALLSGKDLLIF 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 515 DEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIV 567
Cdd:cd03226   151 DEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 355-575 3.75e-30

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: 117.92  E-value: 3.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQES-LRSELSIV 433
Cdd:cd03224     1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 PQECVLFDD-TIYNNI---AFSNPKAKRKdvframkfAQLLKIVNNFPK-KEKtvVGERGVKLSGGEKQRVSIARAILAD 508
Cdd:cd03224    81 PEGRRIFPElTVEENLllgAYARRRAKRK--------ARLERVYELFPRlKER--RKQLAGTLSGGEQQMLAIARALMSR 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 509 KKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIII----AHRLSTImnADKIIVLDKGKIVQQGTHNQL 575
Cdd:cd03224   151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAEL 219
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
 49-324 4.92e-30

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: 119.58  E-value: 4.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  49 YLFKEVIDAstrfstkaLLLSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHS 128
Cdd:cd07346    20 LLTKLLIDD--------VIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 129 THKTGSLISRIIRGGSAVERLTDVFVFNFAPLLFQFTIVAASLLFIGVIPALISFFVVVVFIAYSYFINNIQQKSNLQLN 208
Cdd:cd07346    92 RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 209 QAEDEEKANISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWFSVTRFIAE 288
Cdd:cd07346   172 ESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQG 251

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1490918183 289 DITIGTMVFLFTVFNNLFGPLFGFVHGMRNFYRSMA 324
Cdd:cd07346   252 SLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALA 287
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
354-589 7.94e-30

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 118.19  E-value: 7.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 354 DIEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIV 433
Cdd:PRK11231    2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 PQ-----------ECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNnfpkkektvvgERGVKLSGGEKQRVSIA 502
Cdd:PRK11231   82 PQhhltpegitvrELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLAD-----------RRLTDLSGGQRQRAFLA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 503 RAILADKKVLVLDEATSSLDseTEHeiQADLQKLM-----EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLI 576
Cdd:PRK11231  151 MVLAQDTPVVLLDEPTTYLD--INH--QVELMRLMrelntQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226

                         250
                  ....*....|...
gi 1490918183 577 KEkGLYKKLWNLQ 589
Cdd:PRK11231  227 TP-GLLRTVFDVE 238
PLN03232 PLN03232
ABC transporter C family member; Provisional
 355-585 1.80e-29

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 124.70  E-value: 1.80e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  355 IEFKNVSFKYK---KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIR-LLFRLYDVNSGAILIdgknikefkqeslRSEL 430
Cdd:PLN03232   615 ISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI-------------RGSV 681

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  431 SIVPQECVLFDDTIYNNIAFSNpKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKK 510
Cdd:PLN03232   682 AYVPQVSWIFNATVRENILFGS-DFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183  511 VLVLDEATSSLDSETEHEI-QADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKL 585
Cdd:PLN03232   761 IYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL 836
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 355-571 2.98e-29

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 118.75  E-value: 2.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVS--FKYKKRKI--FSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSE- 429
Cdd:PRK11153    2 IELKNISkvFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 430 ------------LSivpqecvlfDDTIYNNIAF-----SNPKAKRKDvframKFAQLLKIV------NNFPKKektvvge 486
Cdd:PRK11153   82 rqigmifqhfnlLS---------SRTVFDNVALplelaGTPKAEIKA-----RVTELLELVglsdkaDRYPAQ------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 487 rgvkLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDK 563
Cdd:PRK11153  141 ----LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDA 216


                  ....*...
gi 1490918183 564 GKIVQQGT 571
Cdd:PRK11153  217 GRLVEQGT 224
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 372-576 3.39e-29

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: 116.59  E-value: 3.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 372 DFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESL----RSELSIVPQECVLFDD-TIYN 446
Cdd:cd03294    42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTVLE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 447 NIAFS-----NPKAKRKDvfRAMkfaQLLKIVnNFPKKEKTVVGErgvkLSGGEKQRVSIARAILADKKVLVLDEATSSL 521
Cdd:cd03294   122 NVAFGlevqgVPRAEREE--RAA---EALELV-GLEGWEHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSAL 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 522 DSETEHEIQADLQKL--MEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLI 576
Cdd:cd03294   192 DPLIRREMQDELLRLqaELQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEIL 249
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 355-578 3.39e-29

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 117.85  E-value: 3.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKN--VSFKYKKRKIF--SDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVN---SGAILIDGKNIKEFKQESLR 427
Cdd:COG0444     2 LEVRNlkVYFPTRRGVVKavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 428 S----ELSIVPQEcvlfddtiynniAFS--NP----------------KAKRKDVFRamKFAQLLKIV---------NNF 476
Cdd:COG0444    82 KirgrEIQMIFQD------------PMTslNPvmtvgdqiaeplrihgGLSKAEARE--RAIELLERVglpdperrlDRY 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 477 PkkektvvGErgvkLSGGEKQRVSIARAILADKKVLVLDEATSSLD-SeteheIQA-------DLQKlmEGRTSII-IAH 547
Cdd:COG0444   148 P-------HE----LSGGMRQRVMIARALALEPKLLIADEPTTALDvT-----IQAqilnllkDLQR--ELGLAILfITH 209

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1490918183 548 RLSTIMN-ADKIIVLDKGKIVQQGTHNQLIKE 578
Cdd:COG0444   210 DLGVVAEiADRVAVMYAGRIVEEGPVEELFEN 241
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 352-570 5.08e-29

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: 113.80  E-value: 5.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 352 HGDIEFKNVSFKYK------KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLL--FRLYDVNSGAILIDGKNIKEFkq 423
Cdd:cd03213     1 GVTLSFRNLTVTVKsspsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKR-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 424 eSLRSELSIVPQECVLFDD-TIYNNIAFSnpkakrkdvframkfAQLlkivnnfpkkektvvgeRGvkLSGGEKQRVSIA 502
Cdd:cd03213    79 -SFRKIIGYVPQDDILHPTlTVRETLMFA---------------AKL-----------------RG--LSGGERKRVSIA 123

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 503 RAILADKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIM--NADKIIVLDKGKIVQQG 570
Cdd:cd03213   124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 57-584 5.62e-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: 123.10  E-value: 5.62e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183   57 ASTRFSTKALLLSNYTSILTIILLVFLAITIFnSAGYWLRMHMINLLdARLILDLKRKFFNHIIHLSYNFHSTHKTGSLI 136
Cdd:TIGR01271  908 ASSPDVQKPVIITPTSAYYIFYIYVGTADSVL-ALGFFRGLPLVHTL-LTVSKRLHEQMLHSVLQAPMAVLNTMKAGRIL 985

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  137 SRIIRGGSAVERLTDVFVFNFAPLLFQF--TIVAASLL----FIGVIPalisffVVVVFIAY-SYFINNIQQksnlqLNQ 209
Cdd:TIGR01271  986 NRFTKDMAIIDDMLPLTLFDFIQLTLIVlgAIFVVSVLqpyiFIAAIP------VAVIFIMLrAYFLRTSQQ-----LKQ 1054

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  210 AEDEEKANI-SDVFTNID---SIKYFGKENRIKSIYRKfAVKTRNAllknwNYFRWLDSGQLLILGIGLVLLVWFSVTRF 285
Cdd:TIGR01271 1055 LESEARSPIfSHLITSLKglwTIRAFGRQSYFETLFHK-ALNLHTA-----NWFLYLSTLRWFQMRIDIIFVFFFIAVTF 1128

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  286 IA---EDITIGTMVFLFTVFNNLFGPLFGFVHGMRNFYRSMADFQDLFKYAKIKNE-----------------IEDLPNA 345
Cdd:TIGR01271 1129 IAigtNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEeprpsggggkyqlstvlVIENPHA 1208

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  346 GKLKIVHGDIEFKNVSFKYKK--RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNsGAILIDGKNIKEFKQ 423
Cdd:TIGR01271 1209 QKCWPSGGQMDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTL 1287

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  424 ESLRSELSIVPQECVLFDDTIYNNIafsNPKAKRKD--VFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSI 501
Cdd:TIGR01271 1288 QTWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDeeIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCL 1364

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  502 ARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGL 581
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSL 1444


                   ...
gi 1490918183  582 YKK 584
Cdd:TIGR01271 1445 FKQ 1447
PTZ00243 PTZ00243
ABC transporter; Provisional
 343-576 7.23e-29

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 122.58  E-value: 7.23e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  343 PNAGKLKIVHGDIEFKNVSFKYKK------RKIfsdfNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGK 416
Cdd:PTZ00243  1297 TSAAPHPVQAGSLVFEGVQMRYREglplvlRGV----SFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGR 1372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  417 NIKEFKQESLRSELSIVPQECVLFDDTIYNNI-AFSnpKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGE 495
Cdd:PTZ00243  1373 EIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVdPFL--EASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQ 1450

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  496 KQRVSIARAILA-DKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQ 574
Cdd:PTZ00243  1451 RQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRE 1530


                   ..
gi 1490918183  575 LI 576
Cdd:PTZ00243  1531 LV 1532
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 355-575 7.60e-29

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: 114.14  E-value: 7.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKK--RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEfKQESLRSELSI 432
Cdd:cd03263     1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQECVLFDD-TIYNNIAFSnpkAKRKDVFRAMKFA---QLLKIVNNFPKKEKTVVgergvKLSGGEKQRVSIARAILAD 508
Cdd:cd03263    80 CPQFDALFDElTVREHLRFY---ARLKGLPKSEIKEeveLLLRVLGLTDKANKRAR-----TLSGGMKRKLSLAIALIGG 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 509 KKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQL 575
Cdd:cd03263   152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
355-577 9.48e-29

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 120.12  E-value: 9.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSfkykkrKIF------SDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIkEFK--QESL 426
Cdd:COG1129     5 LEMRGIS------KSFggvkalDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRspRDAQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 427 RSELSIVPQECVLFDD-TIYNNIAFSNPKAKRKDV-FRAM--KFAQLLKIVNnFPKKEKTVVGErgvkLSGGEKQRVSIA 502
Cdd:COG1129    78 AAGIAIIHQELNLVPNlSVAENIFLGREPRRGGLIdWRAMrrRARELLARLG-LDIDPDTPVGD----LSVAQQQLVEIA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 503 RAILADKKVLVLDEATSSL-DSETEH--EIQADLQKlmEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG-----THN 573
Cdd:COG1129   153 RALSRDARVLILDEPTASLtEREVERlfRIIRRLKA--QGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTED 230


                  ....
gi 1490918183 574 QLIK 577
Cdd:COG1129   231 ELVR 234
ABC_6TM_ATM1_ABCB7 cd18582
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...
 49-329 2.16e-28

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


Pssm-ID: 350026 [Multi-domain]  Cd Length: 292  Bit Score: 114.90  E-value: 2.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  49 YLFKEVIDAstrFSTKAlllsnyTSILTIILLVFLA-------ITIFNSagywLRMHMINLLDARLILDLKRKFFNHIIH 121
Cdd:cd18582    17 FLLKYAVDA---LSAPA------SALLAVPLLLLLAyglarilSSLFNE----LRDALFARVSQRAVRRLALRVFRHLHS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 122 LSYNFHSTHKTGSLISRIIRGGSAVERLTDVFVFNFAPLLFQFTIVAASLLFI-GVIPALISFFVVVVFIAYSYFINNIQ 200
Cdd:cd18582    84 LSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLyGWSYALITLVTVALYVAFTIKVTEWR 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 201 QKSNLQLNQAEDEEKANISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWF 280
Cdd:cd18582   164 TKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISLGLTAIMLL 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 281 SVTRFIAEDITIGTMVFLFTVFNNLFGPL--FGFVHgmRNFYRSMADFQDL 329
Cdd:cd18582   244 AAQGVVAGTLTVGDFVLVNTYLLQLYQPLnfLGFVY--REIRQSLIDMEKL 292
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 354-581 3.51e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 114.35  E-value: 3.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 354 DIEFKNVSFKYKKRKIFS-----DFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILI------DGKNIKEFK 422
Cdd:PRK13634    2 DITFQKVEHRYQYKTPFErralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 423 qeSLRSELSIVPQ--ECVLFDDTIYNNIAF--SNPKAKRKDVFRamKFAQLLKIVNnfpkKEKTVVGERGVKLSGGEKQR 498
Cdd:PRK13634   82 --PLRKKVGIVFQfpEHQLFEETVEKDICFgpMNFGVSEEDAKQ--KAREMIELVG----LPEELLARSPFELSGGQMRR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 499 VSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGT---- 571
Cdd:PRK13634  154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTprei 233

                         250
                  ....*....|..
gi 1490918183 572 --HNQLIKEKGL 581
Cdd:PRK13634  234 faDPDELEAIGL 245
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 355-571 5.93e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 113.31  E-value: 5.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFS--DFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSI 432
Cdd:PRK13648    8 IVFKNVSFQYQSDASFTlkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQ--ECVLFDDTIYNNIAF--SNPKAKRKDVFRamKFAQLLKIVNNFPKKEktvvgERGVKLSGGEKQRVSIARAILAD 508
Cdd:PRK13648   88 VFQnpDNQFVGSIVKYDVAFglENHAVPYDEMHR--RVSEALKQVDMLERAD-----YEPNALSGGQKQRVAIAGVLALN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 509 KKVLVLDEATSSLDSETEHEIQADLQKLMEGR--TSIIIAHRLSTIMNADKIIVLDKGKIVQQGT 571
Cdd:PRK13648  161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
355-581 7.07e-28

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 113.19  E-value: 7.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYK--KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSI 432
Cdd:PRK13635    6 IRVEHISFRYPdaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQECvlfDD-----TIYNNIAFS--NPKAKRKDVFRAMKFAqlLKIVN--NFPKKEKTvvgergvKLSGGEKQRVSIAR 503
Cdd:PRK13635   86 VFQNP---DNqfvgaTVQDDVAFGleNIGVPREEMVERVDQA--LRQVGmeDFLNREPH-------RLSGGQKQRVAIAG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 504 AILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGT------HNQL 575
Cdd:PRK13635  154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTpeeifkSGHM 233


                  ....*.
gi 1490918183 576 IKEKGL 581
Cdd:PRK13635  234 LQEIGL 239
cbiO PRK13645
energy-coupling factor transporter ATPase;
353-592 7.84e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 113.56  E-value: 7.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 353 GDIEFKNVSFKYKKRKIF-----SDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDG-------KNIKE 420
Cdd:PRK13645    5 KDIILDNVSYTYAKKTPFefkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 421 FKQesLRSELSIVPQ--ECVLFDDTIYNNIAFS--NPKAKRKDVFRamKFAQLLKIVNnFPKKektVVGERGVKLSGGEK 496
Cdd:PRK13645   85 VKR--LRKEIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAYK--KVPELLKLVQ-LPED---YVKRSPFELSGGQK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 497 QRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHN 573
Cdd:PRK13645  157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPF 236

                         250       260       270
                  ....*....|....*....|....*....|
gi 1490918183 574 QL-----------IKEKGLYKKLWNLQKGG 592
Cdd:PRK13645  237 EIfsnqelltkieIDPPKLYQLMYKLKNKG 266
PLN03130 PLN03130
ABC transporter C family member; Provisional
 166-585 8.11e-28

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 119.46  E-value: 8.11e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  166 IVAASLLF--IGVIPALISFFVVVVFIAYSYFINNIQQKSNLQLnQAEDEEKANISDVFTNIDSIKYFGKENRIKSiyrk 243
Cdd:PLN03130   429 IIAMVLLYqqLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGL-QRTDKRIGLMNEVLAAMDTVKCYAWENSFQS---- 503

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  244 fAVKT-RNALLKnwnyfrWLDSGQLLIlgiglvllvwfSVTRFIAEDITIGTMVFLFTVFNNLFG--------------- 307
Cdd:PLN03130   504 -KVQTvRDDELS------WFRKAQLLS-----------AFNSFILNSIPVLVTVVSFGVFTLLGGdltparaftslslfa 565

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  308 ----PLFGF---VHGMRNFYRSMADFQDLFkyakIKNEIEDLPNAgKLKIVHGDIEFKNVSFKYK---KRKIFSDFNLKI 377
Cdd:PLN03130   566 vlrfPLFMLpnlITQAVNANVSLKRLEELL----LAEERVLLPNP-PLEPGLPAISIKNGYFSWDskaERPTLSNINLDV 640

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  378 PRNKKIALVGPSGSGKTTLIR-LLFRLYDVNSGAILIDGKnikefkqeslrseLSIVPQECVLFDDTIYNNIAFSNP-KA 455
Cdd:PLN03130   641 PVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------VAYVPQVSWIFNATVRDNILFGSPfDP 707

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  456 KRKDvfRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEI-QADLQ 534
Cdd:PLN03130   708 ERYE--RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIK 785

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1490918183  535 KLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKKL 585
Cdd:PLN03130   786 DELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
cbiO PRK13640
energy-coupling factor transporter ATPase;
355-581 9.67e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 112.97  E-value: 9.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYK--KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLY---DVNSGAILIDGKNIKEFKQESLRSE 429
Cdd:PRK13640    6 VEFKHVSFTYPdsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 430 LSIVPQ--ECVLFDDTIYNNIAFSNPKakrkdvfRAMKFAQLLKIVNNfpkkektVVGERGV---------KLSGGEKQR 498
Cdd:PRK13640   86 VGIVFQnpDNQFVGATVGDDVAFGLEN-------RAVPRPEMIKIVRD-------VLADVGMldyidsepaNLSGGQKQR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 499 VSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGT----- 571
Cdd:PRK13640  152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSpveif 231

                         250
                  ....*....|.
gi 1490918183 572 -HNQLIKEKGL 581
Cdd:PRK13640  232 sKVEMLKEIGL 242
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
355-577 1.16e-27

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 114.43  E-value: 1.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEfkqeslRS----EL 430
Cdd:PRK11432    7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSiqqrDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQECVLFDD-TIYNNIAF-----SNPKAKRKDvframKFAQLLKIVN--NFpkkektvvGERGV-KLSGGEKQRVSI 501
Cdd:PRK11432   81 CMVFQSYALFPHmSLGENVGYglkmlGVPKEERKQ-----RVKEALELVDlaGF--------EDRYVdQISGGQQQRVAL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 502 ARAILADKKVLVLDEATSSLDS-------ETEHEIQadlQKLmeGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHN 573
Cdd:PRK11432  148 ARALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQ---QQF--NITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQ 222


                  ....
gi 1490918183 574 QLIK 577
Cdd:PRK11432  223 ELYR 226
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 359-570 1.54e-27

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: 110.46  E-value: 1.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 359 NVSFKYKKRkiFSDFNLKIPRNKK---IALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQE----SLRSELS 431
Cdd:cd03297     1 MLCVDIEKR--LPDFTLKIDFDLNeevTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinlpPQQRKIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 432 IVPQECVLFDD-TIYNNIAFSNP-KAKRKDVFRAMKFAQLLKIvnnfpkkekTVVGERGV-KLSGGEKQRVSIARAILAD 508
Cdd:cd03297    79 LVFQQYALFPHlNVRENLAFGLKrKRNREDRISVDELLDLLGL---------DHLLNRYPaQLSGGEKQRVALARALAAQ 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 509 KKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTI-MNADKIIVLDKGKIVQQG 570
Cdd:cd03297   150 PELLLLDEPFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 355-565 2.98e-27

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: 109.11  E-value: 2.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKqESLRSELSIVP 434
Cdd:COG4133     3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDD-TIYNNIAF----SNPKAKRKDVFRAMKFAQLLKIVNNFPKkektvvgergvKLSGGEKQRVSIARAILADK 509
Cdd:COG4133    82 HADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPA 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 510 KVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIA-HRLSTImNADKIIVLDKGK 565
Cdd:COG4133   151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLEL-AAARVLDLGDFK 206
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
355-576 3.70e-27

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 109.84  E-value: 3.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIfsDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKefKQESLRSELSIVP 434
Cdd:COG3840     2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT--ALPPAERPVSMLF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDD-TIYNNIAFS-NPKAK-----RKDVFRAMKFAQLLKIVNNFPkkektvvGErgvkLSGGEKQRVSIARAILA 507
Cdd:COG3840    78 QENNLFPHlTVAQNIGLGlRPGLKltaeqRAQVEQALERVGLAGLLDRLP-------GQ----LSGGQRQRVALARCLVR 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490918183 508 DKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLI 576
Cdd:COG3840   147 KRPILLLDEPFSALDPALRQEMLDLVDELCRerGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 355-570 3.78e-27

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: 109.23  E-value: 3.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKqESLRSELSIV- 433
Cdd:cd03268     1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGALIe 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 -PqecvlfddTIYNNI-AFSNPKAKRKDV-FRAMKFAQLLKIVNnfpkkEKTVVGERGVKLSGGEKQRVSIARAILADKK 510
Cdd:cd03268    80 aP--------GFYPNLtARENLRLLARLLgIRKKRIDEVLDVVG-----LKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490918183 511 VLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:cd03268   147 LLILDEPTNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 363-570 4.29e-27

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: 109.28  E-value: 4.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 363 KYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYD---VNSGAILIDGKnikEFKQESLRSELSIVPQECVL 439
Cdd:cd03234    16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQ---PRKPDQFQKCVAYVRQDDIL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 440 FD-----DTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNfpkkekTVVGERGVK-LSGGEKQRVSIARAILADKKVLV 513
Cdd:cd03234    93 LPgltvrETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLAL------TRIGGNLVKgISGGERRRVSIAVQLLWDPKVLI 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 514 LDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHR-LSTIMNA-DKIIVLDKGKIVQQG 570
Cdd:cd03234   167 LDEPTSGLDSFTALNLVSTLSQLArRNRIVILTIHQpRSDLFRLfDRILLLSSGEIVYSG 226
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
355-573 7.73e-27

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 109.33  E-value: 7.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDG------KNIKEFKQESLRS 428
Cdd:COG4161     3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 429 ELSIVPQECVLFDD-TIYNNIAFSNPK----AKRKDVFRAMKFAQLLKIVN---NFPkkektvvgergVKLSGGEKQRVS 500
Cdd:COG4161    83 KVGMVFQQYNLWPHlTVMENLIEAPCKvlglSKEQAREKAMKLLARLRLTDkadRFP-----------LHLSGGQQQRVA 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 501 IARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME-GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHN 573
Cdd:COG4161   152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 355-570 8.50e-27

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


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 108.35  E-value: 8.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIfsDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEfkQESLRSELSIVP 434
Cdd:cd03298     1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVSMLF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDD-TIYNNIAFS-NPKAKRKDVFRAMKFAQLLKIvnNFPKKEKTVVGErgvkLSGGEKQRVSIARAILADKKVL 512
Cdd:cd03298    77 QENNLFAHlTVEQNVGLGlSPGLKLTAEDRQAIEVALARV--GLAGLEKRLPGE----LSGGERQRVALARVLVRDKPVL 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 513 VLDEATSSLDSETEHEIQADLQKL--MEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:cd03298   151 LLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 375-575 1.26e-26

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 110.98  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 375 LKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESL---RSELSIVpqecvlFDD--------- 442
Cdd:COG4608    39 FDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMV------FQDpyaslnprm 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 443 TIYNNIAF------SNPKAKRKDvframKFAQLLKIV-------NNFPKKektvvgergvkLSGGEKQRVSIARAILADK 509
Cdd:COG4608   113 TVGDIIAEplrihgLASKAERRE-----RVAELLELVglrpehaDRYPHE-----------FSGGQRQRIGIARALALNP 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 510 KVLVLDEATSSLD-SeteheIQA-------DLQKLMeGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQL 575
Cdd:COG4608   177 KLIVCDEPVSALDvS-----IQAqvlnlleDLQDEL-GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 355-567 3.49e-26

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: 104.82  E-value: 3.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIkefkqeslrselsivp 434
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV---------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 qecvlfddtiynniAFSNPKAkrkdvframkfAQLLKIVnnfpkkekTVVgergvKLSGGEKQRVSIARAILADKKVLVL 514
Cdd:cd03216    65 --------------SFASPRD-----------ARRAGIA--------MVY-----QLSVGERQMVEIARALARNARLLIL 106

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 515 DEATSSL-DSETEH--EIQADLQKlmEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIV 567
Cdd:cd03216   107 DEPTAALtPAEVERlfKVIRRLRA--QGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 355-575 7.73e-26

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 106.76  E-value: 7.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSG-----AILIDG-KNIKEFKQ--ESL 426
Cdd:PRK11264    4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTaRSLSQQKGliRQL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 427 RSELSIVPQECVLFDD-TIYNNIAFSNPKAKRKDVFRAMKFA-QLLKIV------NNFPKKektvvgergvkLSGGEKQR 498
Cdd:PRK11264   84 RQHVGFVFQNFNLFPHrTVLENIIEGPVIVKGEPKEEATARArELLAKVglagkeTSYPRR-----------LSGGQQQR 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 499 VSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQL 575
Cdd:PRK11264  153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 326-575 1.20e-25

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: 106.86  E-value: 1.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 326 FQDLFKYAKIKNeiedlpNAGKLKIVHGDIEFKNvsFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYD 405
Cdd:cd03291    17 FGELLEKAKQEN------NDRKHSSDDNNLFFSN--LCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 406 VNSGAILIDGKnikefkqeslrseLSIVPQECVLFDDTIYNNIAF--SNPKAKRKDVFRAmkfAQLLKIVNNFPKKEKTV 483
Cdd:cd03291    89 PSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENIIFgvSYDEYRYKSVVKA---CQLEEDITKFPEKDNTV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 484 VGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEI-QADLQKLMEGRTSIIIAHRLSTIMNADKIIVLD 562
Cdd:cd03291   153 LGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILH 232

                         250
                  ....*....|...
gi 1490918183 563 KGKIVQQGTHNQL 575
Cdd:cd03291   233 EGSSYFYGTFSEL 245
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 355-561 1.30e-25

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 105.18  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVP 434
Cdd:PRK10247    8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDDTIYNNIAFsnPKAKRKDVFRAMKFAQLLKivnNFPKKEkTVVGERGVKLSGGEKQRVSIARAILADKKVLVL 514
Cdd:PRK10247   88 QTPTLFGDTVYDNLIF--PWQIRNQQPDPAIFLDDLE---RFALPD-TILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1490918183 515 DEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMNADKIIVL 561
Cdd:PRK10247  162 DEITSALDESNKHNVNEIIHRYVReqNIAVLWVTHDKDEINHADKVITL 210
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 355-572 1.52e-25

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 105.48  E-value: 1.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDG------KNIKEFKQESLRS 428
Cdd:PRK11124    3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 429 ELSIVPQECVLFDD-TIYNNI--------AFSNPKAKRkdvfRAMKFAQLLKI---VNNFPkkektvvgergVKLSGGEK 496
Cdd:PRK11124   83 NVGMVFQQYNLWPHlTVQQNLieapcrvlGLSKDQALA----RAEKLLERLRLkpyADRFP-----------LHLSGGQQ 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 497 QRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME-GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTH 572
Cdd:PRK11124  148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDA 225
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 355-581 1.98e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 105.97  E-value: 1.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKK-RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIV 433
Cdd:PRK13647    5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 PQEC--VLFDDTIYNNIAFS--NPKAKRKDVFRAMKFAqlLKIVNNFPKKEKTvvgerGVKLSGGEKQRVSIARAILADK 509
Cdd:PRK13647   85 FQDPddQVFSSTVWDDVAFGpvNMGLDKDEVERRVEEA--LKAVRMWDFRDKP-----PYHLSYGQKKRVAIAGVLAMDP 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 510 KVLVLDEATSSLDSETEHEIQADLQKL-MEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG-----THNQLIKEKGL 581
Cdd:PRK13647  158 DVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGdksllTDEDIVEQAGL 236
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
354-570 2.94e-25

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 107.81  E-value: 2.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 354 DIEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFkqESLRSELSIV 433
Cdd:PRK11000    3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV--PPAERGVGMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 PQECVLFDD-TIYNNIAFSNPKAK------RKDVFRAMKFAQLLKIVNNFPKkektvvgergvKLSGGEKQRVSIARAIL 506
Cdd:PRK11000   81 FQSYALYPHlSVAENMSFGLKLAGakkeeiNQRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGRTLV 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 507 ADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:PRK11000  150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVG 216
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 355-581 3.55e-25

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 104.78  E-value: 3.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVP 434
Cdd:COG4604     2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QEcvlfddtiyNNI----------AF-----SNPKAKRKD---VFRAMKFAQLLKIVNNFpkkektvVGErgvkLSGGEK 496
Cdd:COG4604    82 QE---------NHInsrltvrelvAFgrfpySKGRLTAEDreiIDEAIAYLDLEDLADRY-------LDE----LSGGQR 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 497 QRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLstimN-----ADKIIVLDKGKIVQQ 569
Cdd:COG4604   142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADelGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQ 217

                         250
                  ....*....|..
gi 1490918183 570 GTHNQLIKEKGL 581
Cdd:COG4604   218 GTPEEIITPEVL 229
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 355-582 5.41e-25

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 110.81  E-value: 5.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  355 IEFKNVSFKYKKRK--IFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGknikefkqeslrsELSI 432
Cdd:TIGR00957  637 ITVHNATFTWARDLppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAY 703

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  433 VPQECVLFDDTIYNNIAFSnpKAKRKDVFRA-MKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKV 511
Cdd:TIGR00957  704 VPQQAWIQNDSLRENILFG--KALNEKYYQQvLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADI 781

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490918183  512 LVLDEATSSLDSETEHEIQADL---QKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLY 582
Cdd:TIGR00957  782 YLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 355-581 5.99e-25

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: 104.01  E-value: 5.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGA-ILIDGK-----NIKEFK------ 422
Cdd:COG1119     4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGErrggeDVWELRkriglv 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 423 ----QESLRSELSIvpQECVL--FDDTI--YNNIafsnpkaKRKDVFRAMkfaQLLKIVNNFPKKEKTVVgergvKLSGG 494
Cdd:COG1119    84 spalQLRFPRDETV--LDVVLsgFFDSIglYREP-------TDEQRERAR---ELLELLGLAHLADRPFG-----TLSQG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 495 EKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSII-IAHRLSTIMNA-DKIIVLDKGKIVQQGT 571
Cdd:COG1119   147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAaEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAAGP 226

                         250
                  ....*....|
gi 1490918183 572 HNQLIKEKGL 581
Cdd:COG1119   227 KEEVLTSENL 236
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 355-549 7.14e-25

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 103.70  E-value: 7.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVN-----SGAILIDGKNIKEFKQES--LR 427
Cdd:PRK14239    6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDTvdLR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 428 SELSIVPQECVLFDDTIYNNIAFSNPKAKRKD-------VFRAMKFAQLLKIVnnfpkkeKTVVGERGVKLSGGEKQRVS 500
Cdd:PRK14239   86 KEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDkqvldeaVEKSLKGASIWDEV-------KDRLHDSALGLSGGQQQRVC 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1490918183 501 IARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRL 549
Cdd:PRK14239  159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 353-584 8.53e-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: 104.17  E-value: 8.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 353 GDIEFKNVSFKYKK--RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNsGAILIDGKNIKEFKQESLRSEL 430
Cdd:cd03289     1 GQMTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQECVLFDDTIYNNIafsNPKAKRKD--VFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILAD 508
Cdd:cd03289    80 GVIPQKVFIFSGTFRKNL---DPYGKWSDeeIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183 509 KKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGLYKK 584
Cdd:cd03289   157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
355-571 8.86e-25

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 103.66  E-value: 8.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVP 434
Cdd:COG4559     2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVL-FDDTIYNNIA------FSNPKAKRKDVFRAMKFAQLLKIVN-NFPKkektvvgergvkLSGGEKQRVSIARAiL 506
Cdd:COG4559    82 QHSSLaFPFTVEEVVAlgraphGSSAAQDRQIVREALALVGLAHLAGrSYQT------------LSGGEQQRVQLARV-L 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 507 A--------DKKVLVLDEATSSLDseteheI--QadlQKLM--------EGRTSIIIAHRLS-TIMNADKIIVLDKGKIV 567
Cdd:COG4559   149 AqlwepvdgGPRWLFLDEPTSALD------LahQ---HAVLrlarqlarRGGGVVAVLHDLNlAAQYADRILLLHQGRLV 219


                  ....
gi 1490918183 568 QQGT 571
Cdd:COG4559   220 AQGT 223
cbiO PRK13650
energy-coupling factor transporter ATPase;
355-575 1.10e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 104.04  E-value: 1.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKK---RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELS 431
Cdd:PRK13650    5 IEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 432 IVPQ--ECVLFDDTIYNNIAF--SNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTvvgergvKLSGGEKQRVSIARAILA 507
Cdd:PRK13650   85 MVFQnpDNQFVGATVEDDVAFglENKGIPHEEMKERVNEALELVGMQDFKEREPA-------RLSGGQKQRVAIAGAVAM 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 508 DKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQL 575
Cdd:PRK13650  158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
355-575 1.53e-24

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 103.31  E-value: 1.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESL---RSELS 431
Cdd:PRK11831    8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 432 IVPQECVLFDD-TIYNNIAFSNPKAKR--KDVFRAMKFAQLlkivnnfpkkekTVVGERGV------KLSGGEKQRVSIA 502
Cdd:PRK11831   88 MLFQSGALFTDmNVFDNVAYPLREHTQlpAPLLHSTVMMKL------------EAVGLRGAaklmpsELSGGMARRAALA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 503 RAILADKKVLVLDEATSSLDSETeheiQADLQKLME------GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQL 575
Cdd:PRK11831  156 RAIALEPDLIMFDEPFVGQDPIT----MGVLVKLISelnsalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 355-570 1.72e-24

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 102.68  E-value: 1.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVN-----SGAILIDGKNIKEFKQESLRSE 429
Cdd:PRK14247    4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 430 LSIVPQ-ECVLFDDTIYNNIAF--------SNPKAKRKDVFRAMKFAQLLKIVnnfpkkeKTVVGERGVKLSGGEKQRVS 500
Cdd:PRK14247   84 VQMVFQiPNPIPNLSIFENVALglklnrlvKSKKELQERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLC 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183 501 IARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAH------RLStimnaDKIIVLDKGKIVQQG 570
Cdd:PRK14247  157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 372-575 1.77e-24

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: 105.19  E-value: 1.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 372 DFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESL----RSELSIVPQECVLFDD-TIYN 446
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppeKRRIGYVFQEARLFPHlSVRG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 447 NIAFSNPKAKRKDvfRAMKFAQLLKIVNNFPkkektVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETE 526
Cdd:TIGR02142  95 NLRYGMKRARPSE--RRISFERVIELLGIGH-----LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1490918183 527 HEIQADLQKLM-EGRTSII-IAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQL 575
Cdd:TIGR02142 168 YEILPYLERLHaEFGIPILyVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEV 219
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 355-587 2.04e-24

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 102.81  E-value: 2.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNS-----GAILIDGKNIKEFKQ--ESLR 427
Cdd:PRK14258    8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVnlNRLR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 428 SELSIVPQECVLFDDTIYNNIAFS------NPKAKRKDVFR-AMKFAQLLKIVNNfpKKEKTvvgerGVKLSGGEKQRVS 500
Cdd:PRK14258   88 RQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVEsALKDADLWDEIKH--KIHKS-----ALDLSGGQQQRLC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 501 IARAILADKKVLVLDEATSSLDSETEHEIQADLQ--KLMEGRTSIIIAHRLSTIMNADKIIVLDKGkivQQGTHNQLIkE 578
Cdd:PRK14258  161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKG---NENRIGQLV-E 236


                  ....*....
gi 1490918183 579 KGLYKKLWN 587
Cdd:PRK14258  237 FGLTKKIFN 245
PTZ00243 PTZ00243
ABC transporter; Provisional
 362-570 2.57e-24

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 108.33  E-value: 2.57e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  362 FKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILidgknikefkqeslrSELSI--VPQECVL 439
Cdd:PTZ00243   668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW---------------AERSIayVPQQAWI 732

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  440 FDDTIYNNIAFSNPK--AKRKDVFRAmkfAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEA 517
Cdd:PTZ00243   733 MNATVRGNILFFDEEdaARLADAVRV---SQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1490918183  518 TSSLDSET-EHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQG 570
Cdd:PTZ00243   810 LSALDAHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 370-564 4.02e-24

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: 100.87  E-value: 4.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 370 FSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSE----LSIVPQECVLFDDTIY 445
Cdd:cd03290    17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 446 NNIAFSNP--KAKRKDVFRAmkfAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDS 523
Cdd:cd03290    97 ENITFGSPfnKQRYKAVTDA---CSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1490918183 524 E-TEHEIQADLQKLM--EGRTSIIIAHRLSTIMNADKIIVLDKG 564
Cdd:cd03290   174 HlSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 371-571 5.00e-24

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: 100.97  E-value: 5.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 371 SDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKeFKQESLRSELSIV-----PQecvLFDD-TI 444
Cdd:cd03219    17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT-GLPPHEIARLGIGrtfqiPR---LFPElTV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 445 YNNI-------------AFSNPKAKRKDVFRAMkfaQLLKIVNnFPKKEKTVVGErgvkLSGGEKQRVSIARAILADKKV 511
Cdd:cd03219    93 LENVmvaaqartgsgllLARARREEREARERAE---ELLERVG-LADLADRPAGE----LSYGQQRRLEIARALATDPKL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490918183 512 LVLDEATSSLDSETEHEIQADLQKL-MEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGT 571
Cdd:cd03219   165 LLLDEPAAGLNPEETEELAELIRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 326-579 5.81e-24

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: 107.30  E-value: 5.81e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  326 FQDLFKYAKIKNEIEDLPNagklkivhGDIEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYD 405
Cdd:TIGR01271  406 IGELFEKIKQNNKARKQPN--------GDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELE 477

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  406 VNSGAILIDGKnikefkqeslrseLSIVPQECVLFDDTIYNNIAFsnpkAKRKDVFR---AMKFAQLLKIVNNFPKKEKT 482
Cdd:TIGR01271  478 PSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIF----GLSYDEYRytsVIKACQLEEDIALFPEKDKT 540

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  483 VVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEI-QADLQKLMEGRTSIIIAHRLSTIMNADKIIVL 561
Cdd:TIGR01271  541 VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLL 620

                          250
                   ....*....|....*...
gi 1490918183  562 DKGKIVQQGTHNQLIKEK 579
Cdd:TIGR01271  621 HEGVCYFYGTFSELQAKR 638
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 355-567 1.20e-23

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 104.76  E-value: 1.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIdGKNIKE--FKQEslRSELSI 432
Cdd:COG0488   316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIgyFDQH--QEELDP 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 vpqecvlfDDTIYNNIAFSNPKAKRKDVfRAM--KFaqllkivnNFPKKE-KTVVGergvKLSGGEKQRVSIARAILADK 509
Cdd:COG0488   393 --------DKTVLDELRDGAPGGTEQEV-RGYlgRF--------LFSGDDaFKPVG----VLSGGEKARLALAKLLLSPP 451

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 510 KVLVLDEATSSLDSETeheIQADLQKLM--EGrTSIIIAH-R--LSTImnADKIIVLDKGKIV 567
Cdd:COG0488   452 NVLLLDEPTNHLDIET---LEALEEALDdfPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVR 508
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 355-549 1.50e-23

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 100.24  E-value: 1.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGA-----ILIDGKNI--KEFKQESLR 427
Cdd:PRK14243   11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFrvegkVTFHGKNLyaPDVDPVEVR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 428 SELSIVPQECVLFDDTIYNNIAFS---NPKAKRKD--VFRAMKFAQLLKIVnnfpkKEKtvVGERGVKLSGGEKQRVSIA 502
Cdd:PRK14243   91 RRIGMVFQKPNPFPKSIYDNIAYGariNGYKGDMDelVERSLRQAALWDEV-----KDK--LKQSGLSLSGGQQQRLCIA 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1490918183 503 RAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRL 549
Cdd:PRK14243  164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
cbiO PRK13649
energy-coupling factor transporter ATPase;
355-578 1.77e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 100.59  E-value: 1.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYK-----KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNI------KEFKQ 423
Cdd:PRK13649    3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsknKDIKQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 424 esLRSELSIVPQ--ECVLFDDTIYNNIAFSnPK----AKRKDVFRAMKFAQLLKIVNNFPKKEKtvvgergVKLSGGEKQ 497
Cdd:PRK13649   83 --IRKKVGLVFQfpESQLFEETVLKDVAFG-PQnfgvSQEEAEALAREKLALVGISESLFEKNP-------FELSGGQMR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 498 RVSIArAILA-DKKVLVLDEATSSLDSETEHEIQADLQKLME-GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQ 574
Cdd:PRK13649  153 RVAIA-GILAmEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKD 231


                  ....
gi 1490918183 575 LIKE 578
Cdd:PRK13649  232 IFQD 235
cbiO PRK13644
energy-coupling factor transporter ATPase;
355-581 1.80e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 100.45  E-value: 1.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKK-RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEF-KQESLRSELSI 432
Cdd:PRK13644    2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQ--ECVLFDDTIYNNIAFSN------PKAKRKDVFRAMKFAQLLKIVNNFPKKektvvgergvkLSGGEKQRVSIARA 504
Cdd:PRK13644   82 VFQnpETQFVGRTVEEDLAFGPenlclpPIEIRKRVDRALAEIGLEKYRHRSPKT-----------LSGGQGQCVALAGI 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 505 ILADKKVLVLDEATSSLDSETEHEIQADLQKLME-GRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQLIKEKGL 581
Cdd:PRK13644  151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSL 228
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 355-571 2.68e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 99.88  E-value: 2.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYK-KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIV 433
Cdd:PRK13652    4 IETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 PQ--ECVLFDDTIYNNIAFS------NPKAKRKDVFRAMKFAQLLKIVNNFPKKektvvgergvkLSGGEKQRVSIARAI 505
Cdd:PRK13652   84 FQnpDDQIFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIAGVI 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 506 LADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGT 571
Cdd:PRK13652  153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGT 221
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
 49-309 6.09e-23

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: 98.87  E-value: 6.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  49 YLFKEVIDASTRFStkalllSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHS 128
Cdd:pfam00664  20 LVLGRILDVLLPDG------DPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 129 THKTGSLISRIIRGGSAVERLTDVFVFNFAPLLFQFTIVAASLLFIGVIPALISFFVVVVFIAYSYFINNIQQKSNLQLN 208
Cdd:pfam00664  94 TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQ 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 209 QAEDEEKANISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWFSVTRFIAE 288
Cdd:pfam00664 174 KAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISG 253

                         250       260
                  ....*....|....*....|.
gi 1490918183 289 DITIGTMVFLFTVFNNLFGPL 309
Cdd:pfam00664 254 ELSVGDLVAFLSLFAQLFGPL 274
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 355-575 6.43e-23

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: 97.44  E-value: 6.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNI-KEFKQesLRSELSIV 433
Cdd:cd03265     1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREPRE--VRRRIGIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 PQECVLFDD-TIYNNIA-----FSNPKAKRKDvframKFAQLLKIVNNFPKKEKTVvgergVKLSGGEKQRVSIARAILA 507
Cdd:cd03265    79 FQDLSVDDElTGWENLYiharlYGVPGAERRE-----RIDELLDFVGLLEAADRLV-----KTYSGGMRRRLEIARSLVH 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 508 DKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTI-MNADKIIVLDKGKIVQQGTHNQL 575
Cdd:cd03265   149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
cbiO PRK13641
energy-coupling factor transporter ATPase;
355-584 1.16e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 98.36  E-value: 1.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYK-----KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNI------KEFKQ 423
Cdd:PRK13641    3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgnKNLKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 424 esLRSELSIVPQ--ECVLFDDTIYN-------NIAFSNPKAKRKdvfrAMKFAQLLKIvnnfpkkEKTVVGERGVKLSGG 494
Cdd:PRK13641   83 --LRKKVSLVFQfpEAQLFENTVLKdvefgpkNFGFSEDEAKEK----ALKWLKKVGL-------SEDLISKSPFELSGG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 495 EKQRVSIARAILADKKVLVLDEATSSLDSETEHE---IQADLQKlmEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:PRK13641  150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEmmqLFKDYQK--AGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHA 227

                         250
                  ....*....|....
gi 1490918183 571 THNQLIKEKGLYKK 584
Cdd:PRK13641  228 SPKEIFSDKEWLKK 241
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 355-584 1.57e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 98.77  E-value: 1.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKR-----KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILI---------------- 413
Cdd:PRK13631   22 LRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhelit 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 414 --DGKNIKEFKQesLRSELSIVPQ--ECVLFDDTIYNNIAFSnPKAKRKDVFRAMKFAQ--LLKIVNNFPKKEKTVVGer 487
Cdd:PRK13631  102 npYSKKIKNFKE--LRRRVSMVFQfpEYQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKfyLNKMGLDDSYLERSPFG-- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 488 gvkLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHE-IQADLQKLMEGRTSIIIAHRLSTIMN-ADKIIVLDKGK 565
Cdd:PRK13631  177 ---LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGK 253

                         250
                  ....*....|....*....
gi 1490918183 566 IVQQGTHNQLIKEKGLYKK 584
Cdd:PRK13631  254 ILKTGTPYEIFTDQHIINS 272
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 355-571 2.47e-22

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 96.76  E-value: 2.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLL---FRLYdvnSGAILIDGKNIKEFKQESLRSELS 431
Cdd:PRK13548    3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsgeLSPD---SGEVRLNGRPLADWSPAELARRRA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 432 IVPQecvlfddtiYNNIAFS----------------NPKAKRKDVFRAMKFAQLLKIVN-NFPKkektvvgergvkLSGG 494
Cdd:PRK13548   80 VLPQ---------HSSLSFPftveevvamgraphglSRAEDDALVAAALAQVDLAHLAGrDYPQ------------LSGG 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 495 EKQRVSIARAiLA-------DKKVLVLDEATSSLDSETEHEIQADLQKLM--EGRTSIIIAHRLS-TIMNADKIIVLDKG 564
Cdd:PRK13548  139 EQQRVQLARV-LAqlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAheRGLAVIVVLHDLNlAARYADRIVLLHQG 217


                  ....*..
gi 1490918183 565 KIVQQGT 571
Cdd:PRK13548  218 RLVADGT 224
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
372-576 4.54e-22

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 98.57  E-value: 4.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 372 DFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRS----ELSIVPQECVLFDD-TIYN 446
Cdd:PRK10070   46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTVLD 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 447 NIAFSNPKA------KRKDVFRAMKFAQLLKIVNNFPKkektvvgergvKLSGGEKQRVSIARAILADKKVLVLDEATSS 520
Cdd:PRK10070  126 NTAFGMELAginaeeRREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSA 194

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 521 LDSETEHEIQADLQKLM--EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLI 576
Cdd:PRK10070  195 LDPLIRTEMQDELVKLQakHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 356-575 4.55e-22

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: 95.43  E-value: 4.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 356 EFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIkefkqESLRSE------ 429
Cdd:COG0410     5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-----TGLPPHriarlg 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 430 LSIVPQECVLFDD-TIYNNI---AFSNPKAKRkdvfRAMKFAQLLKIvnnFPK-KEKTvvGERGVKLSGGEKQRVSIARA 504
Cdd:COG0410    80 IGYVPEGRRIFPSlTVEENLllgAYARRDRAE----VRADLERVYEL---FPRlKERR--RQRAGTLSGGEQQMLAIGRA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 505 ILADKKVLVLDEAtssldseTE-------HEIQADLQKLMEGRTSIII----AHRLSTImnADKIIVLDKGKIVQQGTHN 573
Cdd:COG0410   151 LMSRPKLLLLDEP-------SLglaplivEEIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAA 221


                  ..
gi 1490918183 574 QL 575
Cdd:COG0410   222 EL 223
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 355-570 4.92e-22

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: 94.65  E-value: 4.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIkefkQESLRSELSIVP 434
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFddtiynniafsnPKAKRKDVfrAMKFAQL---------------LKIVNNFPKKEKTVvgergVKLSGGEKQRV 499
Cdd:cd03269    77 EERGLY------------PKMKVIDQ--LVYLAQLkglkkeearrridewLERLELSEYANKRV-----EELSKGNQQKV 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 500 SIARAILADKKVLVLDEATSSLDS-ETEHEIQADLQKLMEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:cd03269   138 QFIAAVIHDPELLILDEPFSGLDPvNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
355-576 5.06e-22

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 96.80  E-value: 5.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESlRSELSIVP 434
Cdd:PRK13537    8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVVP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QecvlFDD-----TIYNNIA-----FSNPKAK-RKDVFRAMKFAQLlkivnnfPKKEKTVVGErgvkLSGGEKQRVSIAR 503
Cdd:PRK13537   87 Q----FDNldpdfTVRENLLvfgryFGLSAAAaRALVPPLLEFAKL-------ENKADAKVGE----LSGGMKRRLTLAR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 504 AILADKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAH------RLstimnADKIIVLDKGKIVQQGTHNQLI 576
Cdd:PRK13537  152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALI 226
cbiO PRK13646
energy-coupling factor transporter ATPase;
355-579 5.42e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 96.39  E-value: 5.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKK-----RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNI------KEFKQ 423
Cdd:PRK13646    3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkdKYIRP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 424 esLRSELSIVPQ--ECVLFDDTIYNNIAFSnPKAKRKDVFRAMKFAQLLKIVNNFPKKektVVGERGVKLSGGEKQRVSI 501
Cdd:PRK13646   83 --VRKRIGMVFQfpESQLFEDTVEREIIFG-PKNFKMNLDEVKNYAHRLLMDLGFSRD---VMSQSPFQMSGGQMRKIAI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 502 ARAILADKKVLVLDEATSSLDSETEHEIQADLQKLM--EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLIKE 578
Cdd:PRK13646  157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236


                  .
gi 1490918183 579 K 579
Cdd:PRK13646  237 K 237
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 372-571 8.85e-22

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: 98.99  E-value: 8.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 372 DFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDvNSGAILIDGKNIKEFKQE---SLRSELSIVpqecvlFDD------ 442
Cdd:COG4172   304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRalrPLRRRMQVV------FQDpfgsls 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 443 ---TIYNNIA----FSNPKAKRKDvfRAMKFAQLLKIV-------NNFPkkektvvGErgvkLSGGEKQRVSIARAILAD 508
Cdd:COG4172   377 prmTVGQIIAeglrVHGPGLSAAE--RRARVAEALEEVgldpaarHRYP-------HE----FSGGQRQRIAIARALILE 443

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 509 KKVLVLDEATSSLD-SeteheIQA-------DLQKLMeGRTSIIIAHRLSTI--MnADKIIVLDKGKIVQQGT 571
Cdd:COG4172   444 PKLLVLDEPTSALDvS-----VQAqildllrDLQREH-GLAYLFISHDLAVVraL-AHRVMVMKDGKVVEQGP 509
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 284-564 1.27e-21

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 98.73  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 284 RFIAEDITIGTMVFLFTVFNNLFGPLFGFVhgmrNFYRSMADFQ------DLFKYAkIKNEIEDLPNAGKLKIVHGD-IE 356
Cdd:COG4178   290 RYFAGEITLGGLMQAASAFGQVQGALSWFV----DNYQSLAEWRatvdrlAGFEEA-LEAADALPEAASRIETSEDGaLA 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 357 FKNVSFK-YKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAI----------------LIDGknik 419
Cdd:COG4178   365 LEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIarpagarvlflpqrpyLPLG---- 440

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 420 efkqeSLRSELSivpqecvlfddtiYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNnfpkkektVVGERGVKLSGGEKQRV 499
Cdd:COG4178   441 -----TLREALL-------------YPATAEAFSDAELREALEAVGLGHLAERLD--------EEADWDQVLSLGEQQRL 494

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 500 SIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKG 564
Cdd:COG4178   495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 371-571 1.37e-21

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: 94.34  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 371 SDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQE--------------SLRSELSIVpqE 436
Cdd:COG0411    21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHriarlgiartfqnpRLFPELTVL--E 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 437 CVL-----FDDTIYNNIAFSNPKAKRKD---VFRAMkfaQLLKIVNnFPKKEKTVVGErgvkLSGGEKQRVSIARAILAD 508
Cdd:COG0411    99 NVLvaahaRLGRGLLAALLRLPRARREEreaRERAE---ELLERVG-LADRADEPAGN----LSYGQQRRLEIARALATE 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 509 KKVLVLDEATSSL-DSETEhEIQADLQKL--MEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGT 571
Cdd:COG0411   171 PKLLLLDEPAAGLnPEETE-ELAELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
363-575 1.61e-21

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 94.27  E-value: 1.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 363 KYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIK------------EFKQ-ESLRSE 429
Cdd:PRK10619   14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvaDKNQlRLLRTR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 430 LSIVPQECVLFDD-TIYNNI--------AFSNPKAKRkdvfRAMKFAQLLKIvnnfpkkEKTVVGERGVKLSGGEKQRVS 500
Cdd:PRK10619   94 LTMVFQHFNLWSHmTVLENVmeapiqvlGLSKQEARE----RAVKYLAKVGI-------DERAQGKYPVHLSGGQQQRVS 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 501 IARAILADKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQL 575
Cdd:PRK10619  163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQL 239
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 367-575 2.34e-21

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 93.96  E-value: 2.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 367 RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILID------GKNIKEFKQESLRSELSIVPQECVLF 440
Cdd:PRK14246   23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQPNPF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 441 DD-TIYNNIAF---SNPKAKRKDVFRAMKfaQLLKIVNNFpKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDE 516
Cdd:PRK14246  103 PHlSIYDNIAYplkSHGIKEKREIKKIVE--ECLRKVGLW-KEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 517 ATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQL 575
Cdd:PRK14246  180 PTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 359-576 5.62e-21

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: 92.22  E-value: 5.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 359 NVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESlRSELSI--VPQE 436
Cdd:cd03218     5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIgyLPQE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 437 CVLFDD-TIYNNIA-----FSNPKAKRKDvfRAMKFAQLLKIvnnfpkkeKTVVGERGVKLSGGEKQRVSIARAILADKK 510
Cdd:cd03218    84 ASIFRKlTVEENILavleiRGLSKKEREE--KLEELLEEFHI--------THLRKSKASSLSGGERRRVEIARALATNPK 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 511 VLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIA-HRLS-TIMNADKIIVLDKGKIVQQGTHNQLI 576
Cdd:cd03218   154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 355-573 6.30e-21

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 96.25  E-value: 6.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSfkykkrKIFSDF------NLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKeFK--QESL 426
Cdd:COG3845     6 LELRGIT------KRFGGVvanddvSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-IRspRDAI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 427 RSELSIVPQECVLFDD-TIYNNIAFSNPKAKRkdVFRAMKFA--QLLKIVNNF-----PKKektVVGErgvkLSGGEKQR 498
Cdd:COG3845    79 ALGIGMVHQHFMLVPNlTVAENIVLGLEPTKG--GRLDRKAAraRIRELSERYgldvdPDA---KVED----LSVGEQQR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 499 VSIARAILADKKVLVLDEATSSLdseTEHEIQaDLQKLM-----EGRTSIIIAHRLSTIM-NADKIIVLDKGKIVqqGTH 572
Cdd:COG3845   150 VEILKALYRGARILILDEPTAVL---TPQEAD-ELFEILrrlaaEGKSIIFITHKLREVMaIADRVTVLRRGKVV--GTV 223


                  .
gi 1490918183 573 N 573
Cdd:COG3845   224 D 224
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
337-570 6.43e-21

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 94.90  E-value: 6.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 337 NEIEDLPNAGKLKIVHGDIEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGK 416
Cdd:PRK11607    2 NDAIPRPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 417 NIKEFKqeSLRSELSIVPQECVLFDD-TIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVN--NFPKKEKTvvgergvKLSG 493
Cdd:PRK11607   82 DLSHVP--PYQRPINMMFQSYALFPHmTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHmqEFAKRKPH-------QLSG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 494 GEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:PRK11607  153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIG 232
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 355-571 7.22e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 92.83  E-value: 7.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKK-RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKeFKQESL---RSEL 430
Cdd:PRK13639    2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRKTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQ--ECVLFDDTIYNNIAFS--NPKAKRKDVFRAMKFAqlLKIVN--NFPKKEKTvvgergvKLSGGEKQRVSIArA 504
Cdd:PRK13639   81 GIVFQnpDDQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEA--LKAVGmeGFENKPPH-------HLSGGQKKRVAIA-G 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 505 ILADK-KVLVLDEATSSLDSETEHEIQADLQKL-MEGRTSIIIAHRLSTI-MNADKIIVLDKGKIVQQGT 571
Cdd:PRK13639  151 ILAMKpEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGT 220
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 372-571 8.11e-21

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: 94.40  E-value: 8.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 372 DFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDG-------KNIkefkqeSLRSE---LSIVPQECVLFD 441
Cdd:COG4148    17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsaRGI------FLPPHrrrIGYVFQEARLFP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 442 D-TIYNNIAFSNPKAKRKDvfRAMKFAQ---LLKIvnnfpkkektvvG---ERGV-KLSGGEKQRVSIARAILADKKVLV 513
Cdd:COG4148    91 HlSVRGNLLYGRKRAPRAE--RRISFDEvveLLGI------------GhllDRRPaTLSGGERQRVAIGRALLSSPRLLL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 514 LDEATSSLDSETEHEIQADLQKLM-EGRTSII-IAHRLSTIMN-ADKIIVLDKGKIVQQGT 571
Cdd:COG4148   157 MDEPLAALDLARKAEILPYLERLRdELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGP 217
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
355-585 8.62e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 92.84  E-value: 8.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYK-----KRKI-FSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQE-SLR 427
Cdd:PRK13633    5 IKCKNVSYKYEsneesTEKLaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 428 SELSIVPQECvlfDDTIYNNI-----AFS------NPKAKRKDVFRAMKFAQLLKIVNNFPKKektvvgergvkLSGGEK 496
Cdd:PRK13633   85 NKAGMVFQNP---DNQIVATIveedvAFGpenlgiPPEEIRERVDESLKKVGMYEYRRHAPHL-----------LSGGQK 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 497 QRVSIArAILADK-KVLVLDEATSSLDSETEHEIQADLQKL--MEGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHN 573
Cdd:PRK13633  151 QRVAIA-GILAMRpECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229

                         250
                  ....*....|..
gi 1490918183 574 QLIKEKGLYKKL 585
Cdd:PRK13633  230 EIFKEVEMMKKI 241
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 363-569 8.84e-21

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: 92.18  E-value: 8.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 363 KYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQES---LRSELSIVPQECvl 439
Cdd:TIGR02769  20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDS-- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 440 fddtiynnIAFSNPKAKRKDVF--------------RAMKFAQLLKIVNNFPKkektVVGERGVKLSGGEKQRVSIARAI 505
Cdd:TIGR02769  98 --------PSAVNPRMTVRQIIgeplrhltsldeseQKARIAELLDMVGLRSE----DADKLPRQLSGGQLQRINIARAL 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 506 LADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQ 569
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 cd18560
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ...
 76-329 1.36e-20

Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.


Pssm-ID: 350004 [Multi-domain]  Cd Length: 292  Bit Score: 92.29  E-value: 1.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  76 TIILLVFLAITIFNSAGYWlrmHMINLLDARL----ILDLKRKFFNHIIHLSYNFHSTHKTGSLISRIIRGGSAVERLTD 151
Cdd:cd18560    37 AVTLILLYALLRFSSKLLK---ELRSLLYRRVqqnaYRELSLKTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLS 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 152 VFVFNFAPLLFQFTIVAASLLFIGVIP-ALISFFVVVVFIAYSYFINNIQQKSNLQLNQAEDEEKANISDVFTNIDSIKY 230
Cdd:cd18560   114 YLVFYLVPTLLELIVVSVVFAFHFGAWlALIVFLSVLLYGVFTIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKY 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 231 FGKENRIK-------SIYRKFAVKTRNALlknwnyfRWLDSGQLLILGIGLVLLVWFSVTRFIAEDITIGTMVFLFTVFN 303
Cdd:cd18560   194 FTNEKYEVdrygeavKEYQKSSVKVQASL-------SLLNVGQQLIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIF 266

                         250       260
                  ....*....|....*....|....*...
gi 1490918183 304 NLFGPLF--GFVHGMrnFYRSMADFQDL 329
Cdd:cd18560   267 QLFQPLNflGTIYRM--IIQSLTDMENL 292
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 355-570 1.42e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 91.44  E-value: 1.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVN-----SGAILIDGKNIKEFKQESL--R 427
Cdd:PRK14267    5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIevR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 428 SELSIVPQECVLFDD-TIYNNIAFS---NPKAKRKD-----VFRAMKFAQLLKIVnnfpkkeKTVVGERGVKLSGGEKQR 498
Cdd:PRK14267   85 REVGMVFQYPNPFPHlTIYDNVAIGvklNGLVKSKKelderVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 499 VSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:PRK14267  158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 356-580 3.02e-20

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 90.13  E-value: 3.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 356 EFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLL--FRLYDVNSGAILIDGKNIKEFKQESlRSELSIv 433
Cdd:COG0396     2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDE-RARAGI- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 pqecvlFddtiynnIAFSNP----------------KAKRKDVFRAMKFAQLLKivnnfpkKEKTVVG------ERGV-- 489
Cdd:COG0396    80 ------F-------LAFQYPveipgvsvsnflrtalNARRGEELSAREFLKLLK-------EKMKELGldedflDRYVne 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 490 KLSGGEKQRVSIARAILADKKVLVLDEATSSLD-------SETeheiqadLQKLM-EGRTSIIIAH--RLSTIMNADKII 559
Cdd:COG0396   140 GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDidalrivAEG-------VNKLRsPDRGILIITHyqRILDYIKPDFVH 212

                         250       260
                  ....*....|....*....|...
gi 1490918183 560 VLDKGKIVQQGTHN--QLIKEKG 580
Cdd:COG0396   213 VLVDGRIVKSGGKElaLELEEEG 235
cbiO PRK13642
energy-coupling factor transporter ATPase;
355-575 3.62e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 90.92  E-value: 3.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFN---LKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELS 431
Cdd:PRK13642    5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 432 IVPQ--ECVLFDDTIYNNIAF--SNPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTvvgergvKLSGGEKQRVSIARAILA 507
Cdd:PRK13642   85 MVFQnpDNQFVGATVEDDVAFgmENQGIPREEMIKRVDEALLAVNMLDFKTREPA-------RLSGGQKQRVAVAGIIAL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 508 DKKVLVLDEATSSLDSETEHEIQADLQKLMEGR--TSIIIAHRLSTIMNADKIIVLDKGKIVQQGTHNQL 575
Cdd:PRK13642  158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 356-579 4.55e-20

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: 89.51  E-value: 4.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 356 EFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFK-QESLRSELSIVP 434
Cdd:TIGR03410   2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIAYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDD-TIYNNI---AFSNPKAKRK---DVFramkfaQLlkivnnFPKKeKTVVGERGVKLSGGEKQRVSIARAILA 507
Cdd:TIGR03410  82 QGREIFPRlTVEENLltgLAALPRRSRKipdEIY------EL------FPVL-KEMLGRRGGDLSGGQQQQLAIARALVT 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 508 DKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSII-IAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLIKEK 579
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQPSIIKDIGRVIRRLRaEGGMAILlVEQYLDFARElADRYYVMERGRVVASGAGDELDEDK 223
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 358-570 6.22e-20

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 88.58  E-value: 6.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 358 KNVSFKYKKRKIFsdfnlkiprnkkiALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESlRSELSIVPQEC 437
Cdd:cd03266    22 DGVSFTVKPGEVT-------------GLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA-RRRLGFVSDST 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 438 VLFDD-TIYNNIAF---------SNPKAKRKDVFRAMKFAQLLKivnnfpkkektvvgERGVKLSGGEKQRVSIARAILA 507
Cdd:cd03266    88 GLYDRlTARENLEYfaglyglkgDELTARLEELADRLGMEELLD--------------RRVGGFSTGMRQKVAIARALVH 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 508 DKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIA-HRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:cd03266   154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 355-565 6.40e-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: 86.35  E-value: 6.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGaILIDGKNIKefkqeslrseLSIVP 434
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-IVTWGSTVK----------IGYFE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QecvlfddtiynniafsnpkakrkdvframkfaqllkivnnfpkkektvvgergvkLSGGEKQRVSIARAILADKKVLVL 514
Cdd:cd03221    70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1490918183 515 DEATSSLDSETEHEIQADLQKLmeGRTSIIIAH-R--LSTImnADKIIVLDKGK 565
Cdd:cd03221    95 DEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDGK 144
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 356-522 8.67e-20

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 87.92  E-value: 8.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 356 EFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLL-------FRLydvnSGAILIDGKNIKEFKQEslRS 428
Cdd:COG4136     3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlspaFSA----SGEVLLNGRRLTALPAE--QR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 429 ELSIVPQECVLFDD-TIYNNIAF----SNPKAKRKD-VFRAMKFAQLLKIVNNFPKKektvvgergvkLSGGEKQRVSIA 502
Cdd:COG4136    77 RIGILFQDDLLFPHlSVGENLAFalppTIGRAQRRArVEQALEEAGLAGFADRDPAT-----------LSGGQRARVALL 145

                         170       180
                  ....*....|....*....|
gi 1490918183 503 RAILADKKVLVLDEATSSLD 522
Cdd:COG4136   146 RALLAEPRALLLDEPFSKLD 165
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 355-570 9.19e-20

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 91.83  E-value: 9.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVP 434
Cdd:PRK09536    4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVL-FDDTIYNNIA---------FSNP-KAKRKDVFRAMKFAQllkiVNNFPKKEKTvvgergvKLSGGEKQRVSIAR 503
Cdd:PRK09536   84 QDTSLsFEFDVRQVVEmgrtphrsrFDTWtETDRAAVERAMERTG----VAQFADRPVT-------SLSGGERQRVLLAR 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 504 AILADKKVLVLDEATSSLDseTEHEIQ--ADLQKLME-GRTSIIIAHRLStiMNA---DKIIVLDKGKIVQQG 570
Cdd:PRK09536  153 ALAQATPVLLLDEPTASLD--INHQVRtlELVRRLVDdGKTAVAAIHDLD--LAArycDELVLLADGRVRAAG 221
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 355-584 1.49e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 89.14  E-value: 1.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKK-RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQE--SLRSELS 431
Cdd:PRK13636    6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESVG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 432 IVPQ--ECVLFDDTIYNNIAFS--NPKAKRKDVFRAMKFAqlLKIVNNFPKKEKTVVGergvkLSGGEKQRVSIARAILA 507
Cdd:PRK13636   86 MVFQdpDNQLFSASVYQDVSFGavNLKLPEDEVRKRVDNA--LKRTGIEHLKDKPTHC-----LSFGQKKRVAIAGVLVM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 508 DKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTI-MNADKIIVLDKGKIVQQGTHNQLIKEKGLYKK 584
Cdd:PRK13636  159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRK 238
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
 45-309 1.95e-19

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: 89.04  E-value: 1.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  45 VINKYLFKEVIDAstrfstkaLLLSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSY 124
Cdd:cd18570    19 IAGSFFFQILIDD--------IIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 125 NFHSTHKTGSLISRIirggSAVERLTDVFVFNFAPLLFQFTIVAAS---LLFIGVIPALISFFVVVVFIAYSYFINNIQQ 201
Cdd:cd18570    91 SFFETRKTGEIISRF----NDANKIREAISSTTISLFLDLLMVIISgiiLFFYNWKLFLITLLIIPLYILIILLFNKPFK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 202 KSNLQLNQAEDEEKANISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWFS 281
Cdd:cd18570   167 KKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIG 246

                         250       260
                  ....*....|....*....|....*...
gi 1490918183 282 VTRFIAEDITIGTMVFLFTVFNNLFGPL 309
Cdd:cd18570   247 SYLVIKGQLSLGQLIAFNALLGYFLGPI 274
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 369-568 2.10e-19

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


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 87.49  E-value: 2.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 369 IFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQES---LRSE-LSIVPQECVLFDD-T 443
Cdd:COG4181    27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDArarLRARhVGFVFQSFQLLPTlT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 444 IYNNIAFSNPKAKRKDVF-RAmkfAQLLKIVNnfpkkektvVGERG----VKLSGGEKQRVSIARAILADKKVLVLDEAT 518
Cdd:COG4181   107 ALENVMLPLELAGRRDARaRA---RALLERVG---------LGHRLdhypAQLSGGEQQRVALARAFATEPAILFADEPT 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 519 SSLDSETEHEIqADLqkLME-----GRTSIIIAHRLSTIMNADKIIVLDKGKIVQ 568
Cdd:COG4181   175 GNLDAATGEQI-IDL--LFElnrerGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
373-576 2.88e-19

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 86.94  E-value: 2.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 373 FNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNikEFKQESLRSELSIVPQECVLFDD-TIYNNIAFS 451
Cdd:PRK10771   18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRPVSMLFQENNLFSHlTVAQNIGLG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 452 -NP--------KAKRKDVFRAMKFAQLLkivNNFPKKektvvgergvkLSGGEKQRVSIARAILADKKVLVLDEATSSLD 522
Cdd:PRK10771   96 lNPglklnaaqREKLHAIARQMGIEDLL---ARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALD 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 523 SETEHEIQADLQKLMEGR--TSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLI 576
Cdd:PRK10771  162 PALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
355-579 3.31e-19

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 89.12  E-value: 3.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEfKQESLRSELSIVP 434
Cdd:PRK13536   42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVP 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QecvlFDD-----TIYNNIA-----FSNPKAKRKDVFRAM-KFAQLlkivnnfPKKEKTVVGErgvkLSGGEKQRVSIAR 503
Cdd:PRK13536  121 Q----FDNldlefTVRENLLvfgryFGMSTREIEAVIPSLlEFARL-------ESKADARVSD----LSGGMKRRLTLAR 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 504 AILADKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHrlstIMN-----ADKIIVLDKGKIVQQGTHNQLIK 577
Cdd:PRK13536  186 ALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTH----FMEeaerlCDRLCVLEAGRKIAEGRPHALID 261


                  ..
gi 1490918183 578 EK 579
Cdd:PRK13536  262 EH 263
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 383-577 3.45e-19

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 91.26  E-value: 3.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 383 IALVGPSGSGKTTLIRLL-FRLYD--VNSGAILIDGKNIkEFKQESLRSelSIVPQECVLFDD-TIYNNIAFSN----PK 454
Cdd:TIGR00955  54 LAVMGSSGAGKTTLMNALaFRSPKgvKGSGSVLLNGMPI-DAKEMRAIS--AYVQQDDLFIPTlTVREHLMFQAhlrmPR 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 455 AKRKDVFRAMkFAQLLKIVNnFPKKEKTVVGERGVK--LSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQAD 532
Cdd:TIGR00955 131 RVTKKEKRER-VDEVLQALG-LRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQV 208

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1490918183 533 LQKL-MEGRTSIIIAHR-LSTIM-NADKIIVLDKGKIVQQGTHNQLIK 577
Cdd:TIGR00955 209 LKGLaQKGKTIICTIHQpSSELFeLFDKIILMAEGRVAYLGSPDQAVP 256
cbiO PRK13643
energy-coupling factor transporter ATPase;
355-583 3.53e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 88.25  E-value: 3.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFS-----DFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAI----LIDGKNIKEFKQES 425
Cdd:PRK13643    2 IKFEKVNYTYQPNSPFAsralfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 426 LRSELSIVPQ--ECVLFDDTIYNNIAFSnPK----AKRKDVFRAMKFAQLLKIVNNFPKKEKtvvgergVKLSGGEKQRV 499
Cdd:PRK13643   82 VRKKVGVVFQfpESQLFEETVLKDVAFG-PQnfgiPKEKAEKIAAEKLEMVGLADEFWEKSP-------FELSGGQMRRV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 500 SIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME-GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLIK 577
Cdd:PRK13643  154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233


                  ....*.
gi 1490918183 578 EKGLYK 583
Cdd:PRK13643  234 EVDFLK 239
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 359-575 3.55e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 87.84  E-value: 3.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 359 NVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDV-----NSGAILIDGKNIKEFKQE-SLRSELSI 432
Cdd:PRK14271   26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVlEFRRRVGM 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQECVLFDDTIYNNI---AFSNPKAKRKDvFRAMKFAQLLKIvnNFPKKEKTVVGERGVKLSGGEKQRVSIARAILADK 509
Cdd:PRK14271  106 LFQRPNPFPMSIMDNVlagVRAHKLVPRKE-FRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNP 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 510 KVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQL 575
Cdd:PRK14271  183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 372-564 6.41e-19

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


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 85.98  E-value: 6.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 372 DFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLrselsIVPQECVLFD-DTIYNNIAF 450
Cdd:TIGR01184   3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 451 S-------NPKAKRKDVFRamkfaQLLKIVNNFPKKEKtvvgeRGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDS 523
Cdd:TIGR01184  78 AvdrvlpdLSKSERRAIVE-----EHIALVGLTEAADK-----RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1490918183 524 ETEHEIQADLQKLME--GRTSIIIAHRL-STIMNADKIIVLDKG 564
Cdd:TIGR01184 148 LTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 358-566 7.44e-19

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 86.66  E-value: 7.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 358 KNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEfkqesLRSELSIVPQEC 437
Cdd:PRK11247   16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTRLMFQDA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 438 VLFD-DTIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPkkektvvgergVKLSGGEKQRVSIARAILADKKVLVLDE 516
Cdd:PRK11247   91 RLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLLLLDE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 517 ATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLS-TIMNADKIIVLDKGKI 566
Cdd:PRK11247  160 PLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 355-580 7.80e-19

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 84.89  E-value: 7.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLL--FRLYDVNSGAILIDGKNIKEFKQESlRSELSI 432
Cdd:cd03217     1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARLGI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VpqecvlfddtiynnIAFSNPKAkrkdvFRAMKFAQLLKIVNnfpkkektvvgergVKLSGGEKQRVSIARAILADKKVL 512
Cdd:cd03217    80 F--------------LAFQYPPE-----IPGVKNADFLRYVN--------------EGFSGGEKKRNEILQLLLLEPDLA 126

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 513 VLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAH--RLSTIMNADKIIVLDKGKIVQQGTHN--QLIKEKG 580
Cdd:cd03217   127 ILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEKKG 199
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
349-577 1.88e-18

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 85.61  E-value: 1.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 349 KIVHGDIEF--KNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESL 426
Cdd:PRK10575    4 YTNHSDTTFalRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 427 RSELSIVPQECvlfddtiynniafsnPKAKrkdvfrAMKFAQLLKI-------------VNNFPKKEK--TVVG-----E 486
Cdd:PRK10575   84 ARKVAYLPQQL---------------PAAE------GMTVRELVAIgrypwhgalgrfgAADREKVEEaiSLVGlkplaH 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 487 RGV-KLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGR--TSIIIAHRLStiMNA---DKIIV 560
Cdd:PRK10575  143 RLVdSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDIN--MAArycDYLVA 220

                         250
                  ....*....|....*..
gi 1490918183 561 LDKGKIVQQGTHNQLIK 577
Cdd:PRK10575  221 LRGGEMIAQGTPAELMR 237
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 355-581 2.36e-18

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 85.91  E-value: 2.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKR-----KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQ------ 423
Cdd:PRK13651    3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkekek 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 424 ------------------ESLRSELSIVPQ--ECVLFDDTIYNNIAFSN-----PKAKRKDvfRAMKFAQLLKIVNNFPK 478
Cdd:PRK13651   83 vleklviqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPvsmgvSKEEAKK--RAAKYIELVGLDESYLQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 479 KEKtvvgergVKLSGGEKQRVSIArAILA-DKKVLVLDEATSSLDSETEHEIQADLQKL-MEGRTSIIIAHRLSTIMN-A 555
Cdd:PRK13651  161 RSP-------FELSGGQKRRVALA-GILAmEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEwT 232

                         250       260
                  ....*....|....*....|....*..
gi 1490918183 556 DKIIVLDKGKIVQQG-THNQLIKEKGL 581
Cdd:PRK13651  233 KRTIFFKDGKIIKDGdTYDILSDNKFL 259
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 373-575 2.90e-18

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 86.17  E-value: 2.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 373 FNLKipRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEF---KQESLRSELSIVPQecvlfddtiyNNIA 449
Cdd:PRK11308   36 FTLE--RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdpeAQKLLRQKIQIVFQ----------NPYG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 450 FSNPKAKRKDVFramkfAQLLKIVNNFPKKEKTvvgER--------GVK----------LSGGEKQRVSIARAILADKKV 511
Cdd:PRK11308  104 SLNPRKKVGQIL-----EEPLLINTSLSAAERR---EKalammakvGLRpehydryphmFSGGQRQRIAIARALMLDPDV 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490918183 512 LVLDEATSSLDSetehEIQA-------DLQKLMeGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQL 575
Cdd:PRK11308  176 VVADEPVSALDV----SVQAqvlnlmmDLQQEL-GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
355-576 6.83e-18

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 83.39  E-value: 6.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQES-LRSELSIV 433
Cdd:PRK11614    6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 PQECVLFDD-TIYNNIAFSNPKAKRKdvframKFAQLLKIVNN-FPK-KEKTVvgERGVKLSGGEKQRVSIARAILADKK 510
Cdd:PRK11614   86 PEGRRVFSRmTVEENLAMGGFFAERD------QFQERIKWVYElFPRlHERRI--QRAGTMSGGEQQMLAIGRALMSQPR 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 511 VLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLI 576
Cdd:PRK11614  158 LLLLDEPSLGLAPIIIQQIFDTIEQLReQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALL 225
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
 43-323 6.85e-18

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: 84.44  E-value: 6.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  43 TRVINKYLFKEVIDastrfstKALLLSNYTSiLTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHL 122
Cdd:cd18545    15 ASLAGPYLIKIAID-------EYIPNGDLSG-LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 123 SYNFHSTHKTGSLISRIIrggSAVERLTDVF---VFNFAPLLFQFTIVAASLLFIGVIPALISFFVVVVFIAYSYFINNI 199
Cdd:cd18545    87 SFSFFDSRPVGKILSRVI---NDVNSLSDLLsngLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRR 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 200 QQKSNLQLNQAEDEEKANISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVW 279
Cdd:cd18545   164 ARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYW 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1490918183 280 FSVTRFIAEDITIGTMV-FLFTVfNNLFGPLFGFVhgmrNFYRSM 323
Cdd:cd18545   244 YGGKLVLGGAITVGVLVaFIGYV-GRFWQPIRNLS----NFYNQL 283
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
355-547 7.38e-18

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 83.60  E-value: 7.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKE--------FKQESL 426
Cdd:PRK11248    2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGpgaergvvFQNEGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 427 rselsiVPQECVLfddtiyNNIAFS-----NPKAKRKDVFRAMkfaqlLKIVN--NFPKKektvvgeRGVKLSGGEKQRV 499
Cdd:PRK11248   82 ------LPWRNVQ------DNVAFGlqlagVEKMQRLEIAHQM-----LKKVGleGAEKR-------YIWQLSGGQRQRV 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1490918183 500 SIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAH 547
Cdd:PRK11248  138 GIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH 187
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 355-522 1.04e-17

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 82.85  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILidgknikefKQESLRseLSIVP 434
Cdd:PRK09544    5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR--IGYVP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLfDDTI---YNNIAFSNPKAKRKDVFRAMKFAQLLKIVnNFPKKektvvgergvKLSGGEKQRVSIARAILADKKV 511
Cdd:PRK09544   74 QKLYL-DTTLpltVNRFLRLRPGTKKEDILPALKRVQAGHLI-DAPMQ----------KLSGGETQRVLLARALLNRPQL 141

                         170
                  ....*....|.
gi 1490918183 512 LVLDEATSSLD 522
Cdd:PRK09544  142 LVLDEPTQGVD 152
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 351-575 1.11e-17

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 84.37  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 351 VHGDIEFKNVSF--KYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESL-- 426
Cdd:PRK15079   16 VHFDIKDGKQWFwqPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWra 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 427 -RSELSIVpqecvlFDD---------TIYNNIA----FSNPKAKRKDV---FRAM--KFAQLLKIVNNFPKKektvvger 487
Cdd:PRK15079   96 vRSDIQMI------FQDplaslnprmTIGEIIAeplrTYHPKLSRQEVkdrVKAMmlKVGLLPNLINRYPHE-------- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 488 gvkLSGGEKQRVSIARAILADKKVLVLDEATSSLDSetehEIQA-------DLQKLMeGRTSIIIAHRLSTIMN-ADKII 559
Cdd:PRK15079  162 ---FSGGQCQRIGIARALILEPKLIICDEPVSALDV----SIQAqvvnllqQLQREM-GLSLIFIAHDLAVVKHiSDRVL 233

                         250
                  ....*....|....*.
gi 1490918183 560 VLDKGKIVQQGTHNQL 575
Cdd:PRK15079  234 VMYLGHAVELGTYDEV 249
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 359-568 1.13e-17

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 82.31  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 359 NVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDgknikeFKQESLRSELSIVpqECV 438
Cdd:COG2401    35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------VPDNQFGREASLI--DAI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 439 LFDDTIYNNIAFSNpKAKRKDV--FRAmKFAQllkivnnfpkkektvvgergvkLSGGEKQRVSIARAILADKKVLVLDE 516
Cdd:COG2401   107 GRKGDFKDAVELLN-AVGLSDAvlWLR-RFKE----------------------LSTGQKFRFRLALLLAERPKLLVIDE 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183 517 ATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTI--MNADKIIVLDKGKIVQ 568
Cdd:COG2401   163 FCSHLDRQTAKRVARNLQKLARraGITLVVATHHYDVIddLQPDLLIFVGYGGVPE 218
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
355-567 1.17e-17

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 82.23  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKY-KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQES---LRSEL 430
Cdd:PRK10908    2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQEC-VLFDDTIYNNIAF------SNPKAKRKDVFRAMKFAQLLKIVNNFPkkektvvgergVKLSGGEKQRVSIAR 503
Cdd:PRK10908   82 GMIFQDHhLLMDRTVYDNVAIpliiagASGDDIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 504 AILADKKVLVLDEATSSLDSetehEIQADLQKLME-----GRTSIIIAHRLSTIMNAD-KIIVLDKGKIV 567
Cdd:PRK10908  151 AVVNKPAVLLADEPTGNLDD----ALSEGILRLFEefnrvGVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 355-563 1.39e-17

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: 80.28  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIF-SDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGknikefkqeslRSELSIV 433
Cdd:cd03223     1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 PQEcvlfddtiynniafsnPKakrkdvfraMKFAQLLKIVNnFPKKEKtvvgergvkLSGGEKQRVSIARAILADKKVLV 513
Cdd:cd03223    70 PQR----------------PY---------LPLGTLREQLI-YPWDDV---------LSGGEQQRLAFARLLLHKPKFVF 114

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 514 LDEATSSLDSETEHEIqadLQKLMEGRTSII-IAHRLSTIMNADKIIVLDK 563
Cdd:cd03223   115 LDEATSALDEESEDRL---YQLLKELGITVIsVGHRPSLWKFHDRVLDLDG 162
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
359-571 1.42e-17

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 82.81  E-value: 1.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 359 NVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQE---SLRSELSIVpq 435
Cdd:PRK10419   17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMV-- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 436 ecvlFDDTIYnniAFsNPkakRKDVF-----------------RAMKFAQLLKIVNNFPkkekTVVGERGVKLSGGEKQR 498
Cdd:PRK10419   95 ----FQDSIS---AV-NP---RKTVReiireplrhllsldkaeRLARASEMLRAVDLDD----SVLDKRPPQLSGGQLQR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183 499 VSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGT 571
Cdd:PRK10419  160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVETQP 235
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 356-566 1.62e-17

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: 80.55  E-value: 1.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 356 EFKNVSFKYKkrkiFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFK-QESLRSELSIVP 434
Cdd:cd03215     6 EVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QE-----CVLfDDTIYNNIAFSNPkakrkdvframkfaqllkivnnfpkkektvvgergvkLSGGEKQRVSIARAILADK 509
Cdd:cd03215    82 EDrkregLVL-DLSVAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDP 123

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 510 KVLVLDEATSSLDSETEHEIQADLQKL-MEGRTSIIIAHRLSTIMN-ADKIIVLDKGKI 566
Cdd:cd03215   124 RVLILDEPTRGVDVGAKAEIYRLIRELaDAGKAVLLISSELDELLGlCDRILVMYEGRI 182
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 355-580 1.80e-17

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 82.38  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLL--FRLYDVNSGAILIDGKNIKEFKQEsLRSELSI 432
Cdd:CHL00131    8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPE-ERAHLGI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 V-----PQEC-----VLFDDTIYNniafSNPKAKRKDVFRAMKFAQL----LKIVNNFPKKEKTVVGErgvKLSGGEKQR 498
Cdd:CHL00131   87 FlafqyPIEIpgvsnADFLRLAYN----SKRKFQGLPELDPLEFLEIinekLKLVGMDPSFLSRNVNE---GFSGGEKKR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 499 VSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSII-IAH--RLSTIMNADKIIVLDKGKIVQQGTHN-- 573
Cdd:CHL00131  160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGDAEla 239


                  ....*..
gi 1490918183 574 QLIKEKG 580
Cdd:CHL00131  240 KELEKKG 246
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 362-571 2.10e-17

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: 86.61  E-value: 2.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  362 FKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIkEFKQESLRSELSIVPQECVLFD 441
Cdd:TIGR01257  938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFH 1016

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  442 D-TIYNNIAFSNPKAKRKDVFRAMKFAQLLKIVNNFPKKEktvvgERGVKLSGGEKQRVSIARAILADKKVLVLDEATSS 520
Cdd:TIGR01257 1017 HlTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRN-----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1490918183  521 LDSETEHEIQADLQKLMEGRTSIIIAHRLSTI-MNADKIIVLDKGKIVQQGT 571
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGT 1143
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
355-567 2.41e-17

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 85.55  E-value: 2.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKY----KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESL---- 426
Cdd:PRK10535    5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 427 RSELSIVPQECVLFDD-TIYNNIAF-----SNPKAKRKDvfRAMKFAQLLKIVNNfpkkektvVGERGVKLSGGEKQRVS 500
Cdd:PRK10535   85 REHFGFIFQRYHLLSHlTAAQNVEVpavyaGLERKQRLL--RAQELLQRLGLEDR--------VEYQPSQLSGGQQQRVS 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 501 IARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME-GRTSIIIAHRLSTIMNADKIIVLDKGKIV 567
Cdd:PRK10535  155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 358-579 3.23e-17

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 81.48  E-value: 3.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 358 KNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFK-QESLRSELSIVPQE 436
Cdd:PRK10895    7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 437 CVLFDD-TIYNN------IAFSNPKAKRKDvfRAMKFAQLLKIVNnfpkkektVVGERGVKLSGGEKQRVSIARAILADK 509
Cdd:PRK10895   87 ASIFRRlSVYDNlmavlqIRDDLSAEQRED--RANELMEEFHIEH--------LRDSMGQSLSGGERRRVEIARALAANP 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490918183 510 KVLVLDEATSSLDSETEHEIQADLQKLME-GRTSIIIAHRL-STIMNADKIIVLDKGKIVQQGTHNQLIKEK 579
Cdd:PRK10895  157 KFILLDEPFAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 367-567 4.59e-17

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 81.29  E-value: 4.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 367 RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNI---KEFKqeslRSEL-SIVpqecvlFDD 442
Cdd:COG1101    19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklPEYK----RAKYiGRV------FQD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 443 ---------TIYNNIAFSNPKAKRKDVFRAMK------FAQLLKIVNN-FPKKEKTVVGergvKLSGGEKQRVSIARAIL 506
Cdd:COG1101    89 pmmgtapsmTIEENLALAYRRGKRRGLRRGLTkkrrelFRELLATLGLgLENRLDTKVG----LLSGGQRQALSLLMATL 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 507 ADKKVLVLDEATSSLDSETEheiqadlQKLMEGRTSIIIAHRLSTIM---N-------ADKIIVLDKGKIV 567
Cdd:COG1101   165 TKPKLLLLDEHTAALDPKTA-------ALVLELTEKIVEENNLTTLMvthNmeqaldyGNRLIMMHEGRII 228
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 355-566 4.81e-17

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 84.25  E-value: 4.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKiFS--DFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSI 432
Cdd:PRK10522  323 LELRNVTFAYQDNG-FSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQECVLFDDTIynniafsNPKAKRKDVFRAMKFAQLLKIvnnfpkKEK-TVVGER--GVKLSGGEKQRVSIARAILADK 509
Cdd:PRK10522  402 VFTDFHLFDQLL-------GPEGKPANPALVEKWLERLKM------AHKlELEDGRisNLKLSKGQKKRLALLLALAEER 468

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 510 KVLVLDEATSSLDSETEHEIQADLQKLM--EGRTSIIIAHRLSTIMNADKIIVLDKGKI 566
Cdd:PRK10522  469 DILLLDEWAADQDPHFRREFYQVLLPLLqeMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
355-569 5.51e-17

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 81.06  E-value: 5.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRK----IFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIkefkqESLRSEL 430
Cdd:COG4525     4 LTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-----TGPGADR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQECVLFD-DTIYNNIAFS-----NPKAKRKDvfRAMKFAQLLKIVNnfpkkektvVGERGV-KLSGGEKQRVSIAR 503
Cdd:COG4525    79 GVVFQKDALLPwLNVLDNVAFGlrlrgVPKAERRA--RAEELLALVGLAD---------FARRRIwQLSGGMRQRVGIAR 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183 504 AILADKKVLVLDEATSSLDSETEHEIQADLQKL--MEGRTSIIIAHR------LSTimnadKIIVLDK--GKIVQQ 569
Cdd:COG4525   148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITHSveealfLAT-----RLVVMSPgpGRIVER 218
ABC_6TM_HMT1 cd18583
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ...
 111-325 5.70e-17

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


Pssm-ID: 350027 [Multi-domain]  Cd Length: 290  Bit Score: 81.81  E-value: 5.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 111 LKRKFFNHIIHLSYNFHSTHKTGSLIsRIIRGGSAVERLTDVFVFNFAPLLFQFTIVAA--SLLFIGVIpALISFFVVVV 188
Cdd:cd18583    72 LSTAAFNHVMNLSMDFHDSKKSGEVL-KAIEQGSSINDLLEQILFQIVPMIIDLVIAIVylYYLFDPYM-GLIVAVVMVL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 189 FIAYSYFINNIQQKSNLQLNQAEDEEKANISDVFTNIDSIKYFGKENRIKSIYRKfAVKTRN-ALLKNWNYFRWLDSGQL 267
Cdd:cd18583   150 YVWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYRE-AVKNYQkAERKYLFSLNLLNAVQS 228

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 268 LILGIGLVLLVWFSVTRFIAEDITIGTMVFLFTVFNNLFGPLFGFVHGMRNFYRSMAD 325
Cdd:cd18583   229 LILTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLID 286
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
358-589 5.71e-17

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 81.19  E-value: 5.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 358 KNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQEC 437
Cdd:PRK10253   11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 438 VLFDD-TIYNNIA---------FSNPKAKRKD-VFRAMKFAQLLKIVNnfpkkektvvgERGVKLSGGEKQRVSIARAIL 506
Cdd:PRK10253   91 TTPGDiTVQELVArgryphqplFTRWRKEDEEaVTKAMQATGITHLAD-----------QSVDTLSGGQRQRAWIAMVLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 507 ADKKVLVLDEATSSLDseTEHEIqaDLQKLM------EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLIKEK 579
Cdd:PRK10253  160 QETAIMLLDEPTTWLD--ISHQI--DLLELLselnreKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTAE 235

                         250
                  ....*....|
gi 1490918183 580 gLYKKLWNLQ 589
Cdd:PRK10253  236 -LIERIYGLR 244
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
362-581 1.88e-16

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 79.67  E-value: 1.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 362 FKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQE--SLRSELSIV---PQE 436
Cdd:PRK13638    9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVATVfqdPEQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 437 CVLFDDtIYNNIAFS--NPKAKRKDVFRAMKFAQLLKIVNNFPKKEKTVvgergvkLSGGEKQRVSIARAILADKKVLVL 514
Cdd:PRK13638   89 QIFYTD-IDSDIAFSlrNLGVPEAEITRRVDEALTLVDAQHFRHQPIQC-------LSHGQKKRVAIAGALVLQARYLLL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 515 DEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG------THNQLIKEKGL 581
Cdd:PRK13638  161 DEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGapgevfACTEAMEQAGL 235
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
383-571 2.01e-16

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 81.04  E-value: 2.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 383 IALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQeslrSELSI--VPQECVLFDD-TIYNNIAFS-----NPK 454
Cdd:PRK11650   33 IVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP----ADRDIamVFQNYALYPHmSVRENMAYGlkirgMPK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 455 AKRKDvfRAMKFAQLLKIVNNFPKKEKtvvgergvKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQ 534
Cdd:PRK11650  109 AEIEE--RVAEAARILELEPLLDRKPR--------ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQ 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1490918183 535 KLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGT 571
Cdd:PRK11650  179 RLHRrlKTTSLYVTHDQVEAMTlADRVVVMNGGVAEQIGT 218
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
372-570 2.16e-16

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 79.54  E-value: 2.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 372 DFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLrseLSIVPQE-------CVLFDDTI 444
Cdd:PRK15056   25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLVEDVV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 445 ----YNNIAFSNpKAKRKDvfRAMKFAQLLKI-VNNFPKKEktvVGErgvkLSGGEKQRVSIARAILADKKVLVLDEATS 519
Cdd:PRK15056  102 mmgrYGHMGWLR-RAKKRD--RQIVTAALARVdMVEFRHRQ---IGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1490918183 520 SLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMNADKIIVLDKGKIVQQG 570
Cdd:PRK15056  172 GVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 368-576 2.78e-16

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 81.97  E-value: 2.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 368 KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKeFK--QESLRSELSIVPQECVLFDD-TI 444
Cdd:PRK10762   18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-FNgpKSSQEAGIGIIHQELNLIPQlTI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 445 YNNI----AFSNP--KAKRKDVFRAMkfAQLLKIVNnFPKKEKTVVGErgvkLSGGEKQRVSIARAILADKKVLVLDEAT 518
Cdd:PRK10762   97 AENIflgrEFVNRfgRIDWKKMYAEA--DKLLARLN-LRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPT 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 519 SSL-DSETE------HEIQAdlqklmEGRTSIIIAHRLSTIMN-ADKIIVLDKGKI-----VQQGTHNQLI 576
Cdd:PRK10762  170 DALtDTETEslfrviRELKS------QGRGIVYISHRLKEIFEiCDDVTVFRDGQFiaereVADLTEDSLI 234
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
372-570 2.96e-16

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 80.30  E-value: 2.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 372 DFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKnikefkqeslrselsivpqecVLFDdtIYNNIAFs 451
Cdd:PRK11144   16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR---------------------VLFD--AEKGICL- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 452 nPKAKRK--DVF--------------------RAMKfAQLLKIV---------NNFPkkektvvgergVKLSGGEKQRVS 500
Cdd:PRK11144   72 -PPEKRRigYVFqdarlfphykvrgnlrygmaKSMV-AQFDKIVallgiepllDRYP-----------GSLSGGEKQRVA 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 501 IARAILADKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSII-IAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:PRK11144  139 IGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLArEINIPILyVSHSLDEILRlADRVVVLEQGKVKAFG 211
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 357-566 3.25e-16

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 81.65  E-value: 3.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 357 FKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDgKNIKefkqeslrseLSIVPQE 436
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR----------IGYLPQE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 437 CVLFDDT----------------------IYNNIAFSNPKAKR----KDVFRAM-------KFAQLLKIVnNFPKKEktv 483
Cdd:COG0488    70 PPLDDDLtvldtvldgdaelraleaeleeLEAKLAEPDEDLERlaelQEEFEALggweaeaRAEEILSGL-GFPEED--- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 484 vGERGVK-LSGGEKQRVSIARAILADKKVLVLDEATSSLDSETeheIQAdLQKLMEGRTS--IIIAH-R--LSTImnADK 557
Cdd:COG0488   146 -LDRPVSeLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEW-LEEFLKNYPGtvLVVSHdRyfLDRV--ATR 218


                  ....*....
gi 1490918183 558 IIVLDKGKI 566
Cdd:COG0488   219 ILELDRGKL 227
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
 355-570 3.43e-16

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: 78.46  E-value: 3.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLF--RLYDVNSGAILIDGKNIKEFK-QESLRSELS 431
Cdd:TIGR01978   1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDLLELEpDERARAGLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 432 IVPQECV--------LFDDTIYNNIAfsnpKAKRKDVFRAMKFAQLLKivnnfpKKEKTV-----VGERGVK--LSGGEK 496
Cdd:TIGR01978  81 LAFQYPEeipgvsnlEFLRSALNARR----SARGEEPLDLLDFEKLLK------EKLALLdmdeeFLNRSVNegFSGGEK 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 497 QRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTS-IIIAH--RLSTIMNADKIIVLDKGKIVQQG 570
Cdd:TIGR01978 151 KRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSfLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 355-585 3.70e-16

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 79.38  E-value: 3.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIkefkqeslrselsivp 434
Cdd:COG4152     2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 qecvlfDDTIYNNIAFS------NPKAKRKDVfrAMKFAQLlkivNNFPKK----------EKTVVGERGVK----LSGG 494
Cdd:COG4152    66 ------DPEDRRRIGYLpeerglYPKMKVGEQ--LVYLARL----KGLSKAeakrradewlERLGLGDRANKkveeLSKG 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 495 EKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME-GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTH 572
Cdd:COG4152   134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSV 213

                         250
                  ....*....|...
gi 1490918183 573 NQlIKEKGLYKKL 585
Cdd:COG4152   214 DE-IRRQFGRNTL 225
GguA NF040905
sugar ABC transporter ATP-binding protein;
368-568 4.12e-16

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 81.37  E-value: 4.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 368 KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNS--GAILIDGKnIKEFK--QESLRSELSIVPQECVLFDD- 442
Cdd:NF040905   15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGE-VCRFKdiRDSEALGIVIIHQELALIPYl 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 443 TIYNNIAFSNPKAKR-----KDVFRamKFAQLLKIVNnfpKKE--KTVVGERGVklsgGEKQRVSIARAILADKKVLVLD 515
Cdd:NF040905   94 SIAENIFLGNERAKRgvidwNETNR--RARELLAKVG---LDEspDTLVTDIGV----GKQQLVEIAKALSKDVKLLILD 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 516 EATSSL-DSETEHeiqadLQKLM-----EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQ 568
Cdd:NF040905  165 EPTAALnEEDSAA-----LLDLLlelkaQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 355-565 4.60e-16

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 81.13  E-value: 4.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNS--GAILIDG-----KNIKEfkqeSLR 427
Cdd:PRK13549    6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGeelqaSNIRD----TER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 428 SELSIVPQECVLFDD-TIYNNIAFSNP--KAKRKD----VFRAMKFAQLLKIVNNfpkkektvVGERGVKLSGGEKQRVS 500
Cdd:PRK13549   82 AGIAIIHQELALVKElSVLENIFLGNEitPGGIMDydamYLRAQKLLAQLKLDIN--------PATPVGNLGLGQQQLVE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 501 IARAILADKKVLVLDEATSSL-DSETEH--EIQADLQKlmEGRTSIIIAHRLSTIMN-ADKIIVLDKGK 565
Cdd:PRK13549  154 IAKALNKQARLLILDEPTASLtESETAVllDIIRDLKA--HGIACIYISHKLNEVKAiSDTICVIRDGR 220
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
355-571 5.17e-16

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 78.34  E-value: 5.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRK-IFS----------DFNLKipRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIkEFKQ 423
Cdd:COG4167     5 LEVRNLSKTFKYRTgLFRrqqfeavkpvSFTLE--AGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL-EYGD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 424 ESLRSELsIVpqecVLFDDTiynNIAFS-------------------NPKAKRKDVFRAMKFAQLLKIVNNFPKKEktvv 484
Cdd:COG4167    82 YKYRCKH-IR----MIFQDP---NTSLNprlnigqileeplrlntdlTAEEREERIFATLRLVGLLPEHANFYPHM---- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 485 gergvkLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEI---QADLQKLMeGRTSIIIAHRLSTIMN-ADKIIV 560
Cdd:COG4167   150 ------LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIinlMLELQEKL-GISYIYVSQHLGIVKHiSDKVLV 222

                         250
                  ....*....|.
gi 1490918183 561 LDKGKIVQQGT 571
Cdd:COG4167   223 MHQGEVVEYGK 233
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 334-525 7.00e-16

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 81.15  E-value: 7.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 334 KIKNEIEDLPNAGKlkIVhgdIEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILI 413
Cdd:PRK11147  304 TAKMQVEEASRSGK--IV---FEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 414 DGK-NIKEFKQEslRSELSivPqecvlfDDTIYNNIAfsnpkAKRKDVFRAMKFAQLLKIVNNF---PKKEKTVVGergv 489
Cdd:PRK11147  379 GTKlEVAYFDQH--RAELD--P------EKTVMDNLA-----EGKQEVMVNGRPRHVLGYLQDFlfhPKRAMTPVK---- 439

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1490918183 490 KLSGGEKQRVSIARAILADKKVLVLDEATSSLDSET 525
Cdd:PRK11147  440 ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 355-576 9.22e-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: 80.23  E-value: 9.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRL--YDVNSGAIL-------------------- 412
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvge 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 413 -------------IDGKNIKEFKQESLRSELSIVPQEC-VLF-DDTIYNNIAFSNPKAK---RKDVFRAMKfaqLLKIVN 474
Cdd:TIGR03269  81 pcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTfALYgDDTVLDNVLEALEEIGyegKEAVGRAVD---LIEMVQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 475 nfpkkektvVGER----GVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLM--EGRTSIIIAHR 548
Cdd:TIGR03269 158 ---------LSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHW 228

                         250       260
                  ....*....|....*....|....*....
gi 1490918183 549 LSTIMN-ADKIIVLDKGKIVQQGTHNQLI 576
Cdd:TIGR03269 229 PEVIEDlSDKAIWLENGEIKEEGTPDEVV 257
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 358-577 1.20e-15

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 76.61  E-value: 1.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 358 KNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIkefkqESL----RSELSI- 432
Cdd:COG1137     7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-----THLpmhkRARLGIg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 -VPQECVLFDD-TIYNNIA-----FSNPKAKRKDvframKFAQLL------KIVNNfpkkektvvgeRGVKLSGGEKQRV 499
Cdd:COG1137    82 yLPQEASIFRKlTVEDNILavlelRKLSKKEREE-----RLEELLeefgitHLRKS-----------KAYSLSGGERRRV 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 500 SIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIA-HR----LSTImnaDKIIVLDKGKIVQQGTHNQ 574
Cdd:COG1137   146 EIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITdHNvretLGIC---DRAYIISEGKVLAEGTPEE 222


                  ...
gi 1490918183 575 LIK 577
Cdd:COG1137   223 ILN 225
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 362-570 1.66e-15

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: 76.22  E-value: 1.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 362 FKYKKRKI--FSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAI----LIDGKNIKEF-KQESL----RSEL 430
Cdd:cd03267    27 FKRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvagLVPWKRRKKFlRRIGVvfgqKTQL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 S--IVPQECVLFDDTIYNnIAFSNPKAKRKDVFRAMKFAQLLKIvnnfPKKektvvgergvKLSGGEKQRVSIARAILAD 508
Cdd:cd03267   107 WwdLPVIDSFYLLAAIYD-LPPARFKKRLDELSELLDLEELLDT----PVR----------QLSLGQRMRAEIAAALLHE 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 509 KKVLVLDEATSSLDSETEHEIQADLQKLMEGR--TSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:cd03267   172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 359-571 2.16e-15

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 78.96  E-value: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 359 NVSFK--YKKRKIFSDFNLKIPRNKKIALVGPSGSGKT----TLIRLLFRLYDVNSGAILIDGKNIKEFKQESLR----S 428
Cdd:COG4172    13 SVAFGqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 429 ELSIVPQECV-----LFddTIYNNIAFS-------NPKAKRKdvfRAmkfAQLLKIV---------NNFPKKektvvger 487
Cdd:COG4172    93 RIAMIFQEPMtslnpLH--TIGKQIAEVlrlhrglSGAAARA---RA---LELLERVgipdperrlDAYPHQ-------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 488 gvkLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEI---QADLQKlmEGRTSII-IAHRLSTIMN-ADKIIVLD 562
Cdd:COG4172   157 ---LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQIldlLKDLQR--ELGMALLlITHDLGVVRRfADRVAVMR 231


                  ....*....
gi 1490918183 563 KGKIVQQGT 571
Cdd:COG4172   232 QGEIVEQGP 240
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 365-525 3.33e-15

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: 75.16  E-value: 3.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 365 KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKN-------IKEfkQESL---RSELSIVP 434
Cdd:COG4778    22 KRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlaqASP--REILalrRRTIGYVS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 Q-----------ECV---LFDDtiynniAFSNPKAKRkdvfRAmkfAQLLKIVNnfpkkektvVGERgvkL--------S 492
Cdd:COG4778   100 QflrviprvsalDVVaepLLER------GVDREEARA----RA---RELLARLN---------LPER---LwdlppatfS 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1490918183 493 GGEKQRVSIARAILADKKVLVLDEATSSLDSET 525
Cdd:COG4778   155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAAN 187
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 357-570 4.06e-15

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: 74.22  E-value: 4.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 357 FKNVSFKYKKR----KIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVN---SGAILIDGKNIKEFKqESLRSE 429
Cdd:cd03233     6 WRNISFTTGKGrskiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFA-EKYPGE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 430 LSIVPQECVLFddtiynniafsnpkaKRKDVFRAMKFAQLLKiVNNFpkkektvvgERGVklSGGEKQRVSIARAILADK 509
Cdd:cd03233    85 IIYVSEEDVHF---------------PTLTVRETLDFALRCK-GNEF---------VRGI--SGGERKRVSIAEALVSRA 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 510 KVLVLDEATSSLDSETEHEIQADLQKL--MEGRTSIIIAHRLSTIMNA--DKIIVLDKGKIVQQG 570
Cdd:cd03233   138 SVLCWDNSTRGLDSSTALEILKCIRTMadVLKTTTFVSLYQASDEIYDlfDKVLVLYEGRQIYYG 202
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 373-570 7.26e-15

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 77.44  E-value: 7.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 373 FNLKipRNKKIALVGPSGSGKTTLIRLLFRLydVNS-GAILIDGKNIKEFKQESLrseLSIVPQECVLFDDTiynNIAFs 451
Cdd:PRK15134  307 FTLR--PGETLGLVGESGSGKSTTGLALLRL--INSqGEIWFDGQPLHNLNRRQL---LPVRHRIQVVFQDP---NSSL- 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 452 NPkakRKDVFRAMkfAQLLKI---VNNFPKKEKTVVG---ERGV----------KLSGGEKQRVSIARAILADKKVLVLD 515
Cdd:PRK15134  376 NP---RLNVLQII--EEGLRVhqpTLSAAQREQQVIAvmeEVGLdpetrhrypaEFSGGQRQRIAIARALILKPSLIILD 450

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 516 EATSSLDSETEHEIQADLQKLMEGR--TSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:PRK15134  451 EPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
356-578 1.02e-14

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 76.87  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 356 EFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKeFK--QESLRSELSIV 433
Cdd:PRK11288    6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR-FAstTAALAAGVAII 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 PQECVLFDD-TIYNNI---------AFSNPKAKRKDVFRAMKfaQL-LKIVNNFPKKEktvvgergvkLSGGEKQRVSIA 502
Cdd:PRK11288   85 YQELHLVPEmTVAENLylgqlphkgGIVNRRLLNYEAREQLE--HLgVDIDPDTPLKY----------LSIGQRQMVEIA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 503 RAILADKKVLVLDEATSSLDS-ETEH--EIQADLQKlmEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIV------QQGTH 572
Cdd:PRK11288  153 KALARNARVIAFDEPTSSLSArEIEQlfRVIRELRA--EGRVILYVSHRMEEIFAlCDAITVFKDGRYVatfddmAQVDR 230


                  ....*.
gi 1490918183 573 NQLIKE 578
Cdd:PRK11288  231 DQLVQA 236
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 68-567 1.08e-14

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: 77.15  E-value: 1.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  68 LSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRIirgGSAVE 147
Cdd:COG4615    40 LNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAAL---TEDVR 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 148 RLTDVFVfNFAPLLFQFTIVAASLLFIGVIpALISFFVVVVFIAYSYFINNI-QQKSNLQLNQAEDEEkaniSDVFTNID 226
Cdd:COG4615   117 TISQAFV-RLPELLQSVALVLGCLAYLAWL-SPPLFLLTLVLLGLGVAGYRLlVRRARRHLRRAREAE----DRLFKHFR 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 227 SIKYFGKE---NRIKS------IYRKFAVKTRNALLKNWNYFRWLDSgqllilgiglvllvWFSVTRFIAeditIGTMVF 297
Cdd:COG4615   191 ALLEGFKElklNRRRRraffdeDLQPTAERYRDLRIRADTIFALANN--------------WGNLLFFAL----IGLILF 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 298 LFTVFNN---------------LFGPLFGFVHGMRNF------YRSMADFQdlfkyAKIKNEIEDLPNAGKLKIVHG--D 354
Cdd:COG4615   253 LLPALGWadpavlsgfvlvllfLRGPLSQLVGALPTLsranvaLRKIEELE-----LALAAAEPAAADAAAPPAPADfqT 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDF-----NLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSE 429
Cdd:COG4615   328 LELRGVTYRYPGEDGDEGFtlgpiDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 430 LSIVPQECVLFDDTIynniafsnPKAKRKDVFRAMKFAQLLKIvnnfpkKEKTVVgERG----VKLSGGEKQRVSIARAI 505
Cdd:COG4615   408 FSAVFSDFHLFDRLL--------GLDGEADPARARELLERLEL------DHKVSV-EDGrfstTDLSQGQRKRLALLVAL 472

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 506 LADKKVLVLDEATSSLDSETE----HEIQADLQKlmEGRTSIIIAH-----RLstimnADKIIVLDKGKIV 567
Cdd:COG4615   473 LEDRPILVFDEWAADQDPEFRrvfyTELLPELKA--RGKTVIAISHddryfDL-----ADRVLKMDYGKLV 536
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 383-581 1.19e-14

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 74.11  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 383 IALVGPSGSGKTTLIRLLFRLYDvNSGAILIDGKNIKEFKQESLRSELSIVPQECV-LFDDTIYNNIAFSNP-KAKRKDV 460
Cdd:COG4138    25 IHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYLSQQQSpPFAMPVFQYLALHQPaGASSEAV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 461 FRAMKF-AQLLKIVnnfPKKEKTVVgergvKLSGGEKQRVSIARAIL-------ADKKVLVLDEATSSLDseteheI--Q 530
Cdd:COG4138   104 EQLLAQlAEALGLE---DKLSRPLT-----QLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLD------VaqQ 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 531 ADLQKLME-----GRTSIIIAHRLS-TIMNADKIIVLDKGKIVQQGTHNQLIKEKGL 581
Cdd:COG4138   170 AALDRLLRelcqqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMTPENL 226
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 352-564 1.45e-14

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: 72.28  E-value: 1.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 352 HGDIEFKNVSF----KYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYD--VNSGAILIDGKNIKEfkqeS 425
Cdd:cd03232     1 GSVLTWKNLNYtvpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDK----N 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 426 LRSELSIVPQECVLFddtiynniafsnPKAKrkdVFRAMKFAQLLkivnnfpkkektvvgeRGvkLSGGEKQRVSIARAI 505
Cdd:cd03232    77 FQRSTGYVEQQDVHS------------PNLT---VREALRFSALL----------------RG--LSVEQRKRLTIGVEL 123

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490918183 506 LADKKVLVLDEATSSLDSETEHEIQADLQKL-MEGRTSIIIAHRLS-TIM-NADKIIVLDKG 564
Cdd:cd03232   124 AAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSaSIFeKFDRLLLLKRG 185
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 358-567 2.46e-14

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 75.54  E-value: 2.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 358 KNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIkEFK--QESLRSELSIVPQ 435
Cdd:PRK10982    2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKssKEALENGISMVHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 436 ECVLF-DDTIYNNIAFSNPKAK-----RKDVFRAMK--FAQLLKIVNnfPKkektvvgERGVKLSGGEKQRVSIARAILA 507
Cdd:PRK10982   81 ELNLVlQRSVMDNMWLGRYPTKgmfvdQDKMYRDTKaiFDELDIDID--PR-------AKVATLSVSQMQMIEIAKAFSY 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 508 DKKVLVLDEATSSL-DSETEHEIQAdLQKLMEGRTSII-IAHRLSTIMN-ADKIIVLDKGKIV 567
Cdd:PRK10982  152 NAKIVIMDEPTSSLtEKEVNHLFTI-IRKLKERGCGIVyISHKMEEIFQlCDEITILRDGQWI 213
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 384-586 2.77e-14

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 75.47  E-value: 2.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 384 ALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKqESLRSELSI--VPQECVLFDD-TIYNNIAFSNPKAKRkdv 460
Cdd:PRK15439   41 ALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIylVPQEPLLFPNlSVKENILFGLPKRQA--- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 461 fRAMKFAQLLKIVN---NFPKKEKTvvgergvkLSGGEKQRVSIARAILADKKVLVLDEATSSLD-SETEH---EIQADL 533
Cdd:PRK15439  117 -SMQKMKQLLAALGcqlDLDSSAGS--------LEVADRQIVEILRGLMRDSRILILDEPTASLTpAETERlfsRIRELL 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 534 QKlmeGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG-----THNQLI-------KEKGLYK--KLW 586
Cdd:PRK15439  188 AQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSGktadlSTDDIIqaitpaaREKSLSAsqKLW 252
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
356-567 3.07e-14

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 75.44  E-value: 3.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 356 EFKNVSfkykKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKeFK--QESLRSELSIV 433
Cdd:COG1129   258 EVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR-IRspRDAIRAGIAYV 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 P----QECVLFDDTIYNNIAFS-----------NPKAKRKDVFRAMKfaqLLKIvnnfpkkeKTVVGERGVK-LSGGEKQ 497
Cdd:COG1129   333 PedrkGEGLVLDLSIRENITLAsldrlsrggllDRRRERALAEEYIK---RLRI--------KTPSPEQPVGnLSGGNQQ 401

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 498 RVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAhrlST-----IMNADKIIVLDKGKIV 567
Cdd:COG1129   402 KVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI---SSelpelLGLSDRILVMREGRIV 473
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 49-324 4.28e-14

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: 73.31  E-value: 4.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  49 YLFKEVIDASTRFSTkallLSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHS 128
Cdd:cd18563    20 YLTKILIDDVLIQLG----PGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 129 THKTGSLISRIirgGSAVERLTDVFVF---NFAPLLFQFTIVAASLLFI-------GVIPALISFFVVVVFIAYSYFINN 198
Cdd:cd18563    96 KRQTGSLMSRV---TSDTDRLQDFLSDglpDFLTNILMIIGIGVVLFSLnwklallVLIPVPLVVWGSYFFWKKIRRLFH 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 199 IQQKSNLQLNqaedeekANISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKN---WN--------------YFRW 261
Cdd:cd18563   173 RQWRRWSRLN-------SVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAeklWAtffplltfltslgtLIVW 245

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 262 ldsgqllilgiglvllvWFSVTRFIAEDITIGTMVFLFTVFNNLFGPLFGFVHGMRNFYRSMA 324
Cdd:cd18563   246 -----------------YFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALT 291
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
 45-327 1.03e-13

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: 72.08  E-value: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  45 VINKYLFKEVIDAstrfstkaLLLSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSY 124
Cdd:cd18542    16 LLIPLLIRRIIDS--------VIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 125 NFHSTHKTGSLISRIIrggSAVERLTDVFVF---NFAPLLFQFTIVAASLLFIGVIPALISFFVVVVFIAYSYFINNIQQ 201
Cdd:cd18542    88 SFHDKARTGDLMSRCT---SDVDTIRRFLAFglvELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVR 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 202 KSNLQLNQAEDE------EkaNISDV-----FTNIDS-IKYFGKENRiksIYRKFAVKTRNALLKNWNYFRWLDSGQlli 269
Cdd:cd18542   165 PAFEEIREQEGElntvlqE--NLTGVrvvkaFAREDYeIEKFDKENE---EYRDLNIKLAKLLAKYWPLMDFLSGLQ--- 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 270 lgigLVLLVWFSVTRFIAEDITIGTMVFLFTVFNNLFGPlfgfvhgMRNFYRSMADFQ 327
Cdd:cd18542   237 ----IVLVLWVGGYLVINGEITLGELVAFISYLWMLIWP-------VRQLGRLINDMS 283
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 362-570 1.60e-13

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: 70.25  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 362 FKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGK--NIKEFkQESLRSELSIVpqECVL 439
Cdd:cd03220    30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsSLLGL-GGGFNPELTGR--ENIY 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 440 FDDTIYNniafsnpkAKRKDVFRAMK----FAQLLKIVNnfpKKEKTvvgergvkLSGGEKQRVSIARAILADKKVLVLD 515
Cdd:cd03220   107 LNGRLLG--------LSRKEIDEKIDeiieFSELGDFID---LPVKT--------YSSGMKARLAFAIATALEPDILLID 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 516 EATSSLDSETEHEIQADLQKLME-GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:cd03220   168 EVLAVGDAAFQEKCQRRLRELLKqGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
355-579 1.74e-13

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 70.81  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLfrlydvnSGaiLIDGKNIKEFKQESLRSelsIVP 434
Cdd:PRK09984    5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SG--LITGDKSAGSHIELLGR---TVQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDDtiynniaFSNPKAKRKDVFRAMKFAQLLKIVNN------------------FPKKEK-------TVVG---- 485
Cdd:PRK09984   73 REGRLARD-------IRKSRANTGYIFQQFNLVNRLSVLENvligalgstpfwrtcfswFTREQKqralqalTRVGmvhf 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 486 --ERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKL--MEGRTSIIIAHRLSTIMN-ADKIIV 560
Cdd:PRK09984  146 ahQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDYALRyCERIVA 225

                         250
                  ....*....|....*....
gi 1490918183 561 LDKGKIVQQGTHNQLIKEK 579
Cdd:PRK09984  226 LRQGHVFYDGSSQQFDNER 244
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
358-571 1.76e-13

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 70.97  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 358 KNVSFKYKKRKifsdfnlkiprnkKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIkEFKQESLRSE-------- 429
Cdd:PRK15112   30 KPLSFTLREGQ-------------TLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSQrirmifqd 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 430 --LSIVPQECV--LFDDTIYNNIAFSnPKAKRKDVFRAMKFAQLLKI-VNNFPKKektvvgergvkLSGGEKQRVSIARA 504
Cdd:PRK15112   96 psTSLNPRQRIsqILDFPLRLNTDLE-PEQREKQIIETLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARA 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 505 ILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGT 571
Cdd:PRK15112  164 LILRPKVIIADEALASLDMSMRSQLINLMLELQEkqGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
355-570 1.96e-13

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 72.89  E-value: 1.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQEsLRSEL--SI 432
Cdd:PRK09700    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQLgiGI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 VPQECVLFDD-TIYNNIAFSN-PKAKRKDV----FRAMKF--AQLLKIVNnfpkkEKTVVGERGVKLSGGEKQRVSIARA 504
Cdd:PRK09700   85 IYQELSVIDElTVLENLYIGRhLTKKVCGVniidWREMRVraAMMLLRVG-----LKVDLDEKVANLSISHKQMLEIAKT 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 505 ILADKKVLVLDEATSSL-DSETEH--EIQADLQKlmEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:PRK09700  160 LMLDAKVIIMDEPTSSLtNKEVDYlfLIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 383-570 2.02e-13

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 72.97  E-value: 2.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 383 IALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEF---KQESLRSELSIVPQECVLFDD---TIYNNI-------A 449
Cdd:PRK10261  353 LSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDPYASLDprqTVGDSImeplrvhG 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 450 FSNPKAKRKDVframkfAQLLKIVNNFPKKEKTVVGErgvkLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEI 529
Cdd:PRK10261  433 LLPGKAAAARV------AWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1490918183 530 ---QADLQKLMeGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:PRK10261  503 inlLLDLQRDF-GIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
359-550 2.44e-13

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 69.84  E-value: 2.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 359 NVSFKYKKRKIFSDF----NLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEF----KQESLRSEL 430
Cdd:PRK11629   10 NLCKRYQEGSVQTDVlhnvSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNQKL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQ-ECVLFDDTIYNNIAF------SNPKAKRKDVFRAMKFAQLLKIVNNFPKKektvvgergvkLSGGEKQRVSIAR 503
Cdd:PRK11629   90 GFIYQfHHLLPDFTALENVAMplligkKKPAEINSRALEMLAAVGLEHRANHRPSE-----------LSGGERQRVAIAR 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1490918183 504 AILADKKVLVLDEATSSLDSETEHEIQADLQKL--MEGRTSIIIAHRLS 550
Cdd:PRK11629  159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQ 207
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 367-546 2.66e-13

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 69.13  E-value: 2.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 367 RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFK----------QESLRSELSIvpQE 436
Cdd:PRK13539   15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaeachylghRNAMKPALTV--AE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 437 CVLFDDTIYNNiafsnpkaKRKDVFRAMKFAQLLKIVnNFPKKEktvvgergvkLSGGEKQRVSIARAILADKKVLVLDE 516
Cdd:PRK13539   93 NLEFWAAFLGG--------EELDIAAALEAVGLAPLA-HLPFGY----------LSAGQKRRVALARLLVSNRPIWILDE 153

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1490918183 517 ATSSLDSETeheiQADLQKLMEGRT---SIIIA 546
Cdd:PRK13539  154 PTAALDAAA----VALFAELIRAHLaqgGIVIA 182
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
 49-312 3.99e-13

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: 70.11  E-value: 3.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  49 YLFKEVIDASTRFSTKALllsnytSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHS 128
Cdd:cd18544    20 LLIKRAIDDYIVPGQGDL------QGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 129 THKTGSLISRIIrggSAVERLTDVFVFNFAPL---LFQFTIVAASLLFIGVIPALISFFVVVVFIAYSYFINNIQQKSNL 205
Cdd:cd18544    94 RTPVGRLVTRVT---NDTEALNELFTSGLVTLigdLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYR 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 206 -------QLNqaedeekANISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLV 278
Cdd:cd18544   171 evreklsRLN-------AFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVL 243

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1490918183 279 WFSVTRFIAEDITIGTMVFLFTVFNNLFGPLFGF 312
Cdd:cd18544   244 WYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDL 277
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 323-525 3.99e-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: 71.89  E-value: 3.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 323 MADFQDLFKYAKIK----NEIEdLPNAGKLkivhGD--IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTL 396
Cdd:TIGR03719 290 LARYEELLSQEFQKrnetAEIY-IPPGPRL----GDkvIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTL 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 397 IRLLFRLYDVNSGAILIdGKNIKefkqeslrseLSIVPQecvlFDDTIYNNiafsnpkakrKDVFRAMKFAQLLKIVNNF 476
Cdd:TIGR03719 365 FRMITGQEQPDSGTIEI-GETVK----------LAYVDQ----SRDALDPN----------KTVWEEISGGLDIIKLGKR 419

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 477 PKKEKTVVGERGVK----------LSGGEKQRVSIARAILADKKVLVLDEATSSLDSET 525
Cdd:TIGR03719 420 EIPSRAYVGRFNFKgsdqqkkvgqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET 478
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 385-581 5.77e-13

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 68.81  E-value: 5.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 385 LVGPSGSGKTTLIRLLFRLYDvNSGAILIDGKNIKEFKQESL---RSELSivPQECVLFDDTIYNNIAFSNPKAKRKDVF 461
Cdd:PRK03695   27 LVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELarhRAYLS--QQQTPPFAMPVFQYLTLHQPDKTRTEAV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 462 RAM--KFAQLLKIVNNFPkkektvvgeRGV-KLSGGEKQRVSIARAIL-------ADKKVLVLDEATSSLDSETeheiQA 531
Cdd:PRK03695  104 ASAlnEVAEALGLDDKLG---------RSVnQLSGGEWQRVRLAAVVLqvwpdinPAGQLLLLDEPMNSLDVAQ----QA 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183 532 DLQKLME-----GRTSIIIAHRLS-TIMNADKIIVLDKGKIVQQGTHNQLIKEKGL 581
Cdd:PRK03695  171 ALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENL 226
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 45-327 7.26e-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: 349994 [Multi-domain]  Cd Length: 294  Bit Score: 69.43  E-value: 7.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  45 VINKYLFKEVIDastrfstKALLLSNyTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSY 124
Cdd:cd18550    16 LLPPLLLREIID-------DALPQGD-LGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 125 NFHSTHKTGSLISRIIrggSAVERLTDVFVFNFAPLLFQFTIVAASLLFIGVIP---ALISFFVVVVFIAYSYFINNI-- 199
Cdd:cd18550    88 AFFTRTRTGEIQSRLN---NDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDwrlALLSLVLLPLFVLPTRRVGRRrr 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 200 -----QQKSNLQLNqAEDEEKANISDVFTnidsIKYFGKEnriKSIYRKFAvkTRNALLKNWN-----YFRWLDSGQLLI 269
Cdd:cd18550   165 kltreQQEKLAELN-SIMQETLSVSGALL----VKLFGRE---DDEAARFA--RRSRELRDLGvrqalAGRWFFAALGLF 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 270 LGIGLVLLVWFSVTRFIAEDITIGTMVFLFTVFNNLFGPLFGFVHGMRNFYRSMADFQ 327
Cdd:cd18550   235 TAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFE 292
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
 68-243 1.05e-12

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: 68.74  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  68 LSNYTSILTIILLVFLAITIFNSAGYWLrmhmINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRIirgGSAVE 147
Cdd:cd18557    32 LDVLNELALILLAIYLLQSVFTFVRYYL----FNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRL---SSDTS 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 148 RLTDVFVFNFAPLLFQFTIVAASLLFIGVI-----PALISfFVVVVFIAYSYFINNIQQKSN-LQLNQAEDEEKAniSDV 221
Cdd:cd18557   105 VLQSAVTDNLSQLLRNILQVIGGLIILFILswkltLVLLL-VIPLLLIASKIYGRYIRKLSKeVQDALAKAGQVA--EES 181

                         170       180
                  ....*....|....*....|..
gi 1490918183 222 FTNIDSIKYFGKENRIKSIYRK 243
Cdd:cd18557   182 LSNIRTVRSFSAEEKEIRRYSE 203
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 359-578 1.08e-12

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: 70.60  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 359 NVSFKYKKRKIFsdfnlkiprnkkiALVGPSGSGKTTLIRLLFRLYDVNSGAILI--------------DGKNIKEFKQE 424
Cdd:TIGR03269 302 NVSLEVKEGEIF-------------GIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpDGRGRAKRYIG 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 425 SLRSELSIVPQECVLfdDTIYNNIAFSNPkakrkDVFRAMKFAQLLKIVNNFPKKEKTVVGERGVKLSGGEKQRVSIARA 504
Cdd:TIGR03269 369 ILHQEYDLYPHRTVL--DNLTEAIGLELP-----DELARMKAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQV 441

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 505 ILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLIKE 578
Cdd:TIGR03269 442 LIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
PLN03211 PLN03211
ABC transporter G-25; Provisional
 338-576 1.28e-12

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 70.68  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 338 EIEDLPNAGKL--KIVHGDIEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLF-RLYDVN-SGAILI 413
Cdd:PLN03211   50 KFENMKNKGSNikRILGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILA 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 414 DGKNIKefKQESLRSelSIVPQecvlfDDTIYNNIAfsnpkakrkdVFRAMKFAQLLKIVNNFPKKEKTVVGE------- 486
Cdd:PLN03211  130 NNRKPT--KQILKRT--GFVTQ-----DDILYPHLT----------VRETLVFCSLLRLPKSLTKQEKILVAEsviselg 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 487 --------------RGVklSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME-GRTSIIIAHRLST 551
Cdd:PLN03211  191 ltkcentiignsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQkGKTIVTSMHQPSS 268

                         250       260
                  ....*....|....*....|....*..
gi 1490918183 552 IMNA--DKIIVLDKGKIVQQGTHNQLI 576
Cdd:PLN03211  269 RVYQmfDSVLVLSEGRCLFFGKGSDAM 295
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
364-561 1.33e-12

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 66.49  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 364 YKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKnikefkqeslrSELSIVPQECVLfDDT 443
Cdd:NF040873    2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQRSEV-PDS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 444 IynniafsnP----------------------KAKRKDVFRAMKFAQLLKIvnnfpkkEKTVVGErgvkLSGGEKQRVSI 501
Cdd:NF040873   70 L--------PltvrdlvamgrwarrglwrrltRDDRAAVDDALERVGLADL-------AGRQLGE----LSGGQRQRALL 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 502 ARAILADKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMNADKIIVL 561
Cdd:NF040873  131 AQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 68-259 2.54e-12

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: 67.95  E-value: 2.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  68 LSNYTSILTIILLVFLAITIFNSagywLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRIIRGGSAVE 147
Cdd:cd18778    36 LGLLLGLALLLLGAYLLRALLNF----LRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 148 RL----TDVFVFNfaplLFQFTIVAASLLFIGVIPALISF----FVVVVFIAYSYFINNI---QQKSNLQLNqaedeekA 216
Cdd:cd18778   112 RLiadgIPQGITN----VLTLVGVAIILFSINPKLALLTLipipFLALGAWLYSKKVRPRyrkVREALGELN-------A 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1490918183 217 NISDVFTNIDSIKYFGKEN----RIKSIYRKFAVKTRNAlLKNWNYF 259
Cdd:cd18778   181 LLQDNLSGIREIQAFGREEeeakRFEALSRRYRKAQLRA-MKLWAIF 226
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 355-567 2.77e-12

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: 69.08  E-value: 2.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNS--GAILIDGKNIKEFK-QESLRSELS 431
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNiRDTERAGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 432 IVPQECVLFDD-TIYNNIAFSNP---KAKRKD----VFRAMKFAQLLKI--VNNfpkkeKTVVGERGvklsGGEKQRVSI 501
Cdd:TIGR02633  82 IIHQELTLVPElSVAENIFLGNEitlPGGRMAynamYLRAKNLLRELQLdaDNV-----TRPVGDYG----GGQQQLVEI 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 502 ARAILADKKVLVLDEATSSLdSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIV 567
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSL-TEKETEILLDIIRDLKahGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 354-575 3.59e-12

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 68.96  E-value: 3.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 354 DIEFKNVSFKYKK--RKIFSDFNLKIPRNKKIALVGPSGSGKT----TLIRLLFR---LYDvnSGAILIDGKNIKEFKQE 424
Cdd:PRK15134    7 AIENLSVAFRQQQtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVYP--SGDIRFHGESLLHASEQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 425 SLR----SELSIVPQECVLFDD---TIYNNIA--FSNPKAKRKDVFRA--------MKFAQLLKIVNNFPKKektvvger 487
Cdd:PRK15134   85 TLRgvrgNKIAMIFQEPMVSLNplhTLEKQLYevLSLHRGMRREAARGeilncldrVGIRQAAKRLTDYPHQ-------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 488 gvkLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKG 564
Cdd:PRK15134  157 ---LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNG 233

                         250
                  ....*....|.
gi 1490918183 565 KIVQQGTHNQL 575
Cdd:PRK15134  234 RCVEQNRAATL 244
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 369-533 4.66e-12

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 65.96  E-value: 4.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 369 IFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQE---SLRSE-LSIVPQECVLFDD-T 443
Cdd:PRK10584   25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAKhVGFVFQSFMLIPTlN 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 444 IYNNI---AFSNPKAKRKDVFRAmkfAQLLKIVNnfpkkektvVGER----GVKLSGGEKQRVSIARAILADKKVLVLDE 516
Cdd:PRK10584  105 ALENVelpALLRGESSRQSRNGA---KALLEQLG---------LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADE 172

                         170
                  ....*....|....*..
gi 1490918183 517 ATSSLDSETEHEIqADL 533
Cdd:PRK10584  173 PTGNLDRQTGDKI-ADL 188
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 359-575 4.88e-12

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 68.73  E-value: 4.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 359 NVSFKYKKRKI--FSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYD-----VNSGAILIDGKN-----IKEFKQESL 426
Cdd:PRK10261   19 NIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEqagglVQCDKMLLRRRSrqvieLSEQSAAQM 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 427 R----SELSIVPQECV-----LFddTIYNNIAFS---NPKAKRKDVFRAMKfaQLLKIVNnFPKKEkTVVGERGVKLSGG 494
Cdd:PRK10261   99 RhvrgADMAMIFQEPMtslnpVF--TVGEQIAESirlHQGASREEAMVEAK--RMLDQVR-IPEAQ-TILSRYPHQLSGG 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 495 EKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQ---ADLQKLMEgRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:PRK10261  173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILqliKVLQKEMS-MGVIFITHDMGVVAEiADRVLVMYQGEAVETG 251


                  ....*
gi 1490918183 571 THNQL 575
Cdd:PRK10261  252 SVEQI 256
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 49-312 5.02e-12

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: 66.74  E-value: 5.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  49 YLFKEVIDAstrfstkaLLLSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHS 128
Cdd:cd18576    17 LLAGQLIDA--------ALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFH 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 129 THKTGSLISRIirgGSAVERLTDVFVFNFAPLLFQFTIVAASLLFIGVIPALISFFVVVVF----IAYSYFINNIQQKS- 203
Cdd:cd18576    89 ERRVGELTSRL---SNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVpvvvLVAVLFGRRIRKLSk 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 204 NLQLNQAEdeekANI--SDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWFS 281
Cdd:cd18576   166 KVQDELAE----ANTivEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYG 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1490918183 282 VTRFIAEDITIGTMV--FLFTVFnnLFGPLFGF 312
Cdd:cd18576   242 GRLVLAGELTAGDLVafLLYTLF--IAGSIGSL 272
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 355-581 5.96e-12

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 68.38  E-value: 5.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAI-LIDGKNIKEFKQESlrseLSIV 433
Cdd:PRK15064  320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYYAQDH----AYDF 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 PQECVLFDdtiynniAFSNPKAKRKD--VFRAMkFAQLLKIVNNFPKKEKTvvgergvkLSGGEKQRVSIARAILADKKV 511
Cdd:PRK15064  396 ENDLTLFD-------WMSQWRQEGDDeqAVRGT-LGRLLFSQDDIKKSVKV--------LSGGEKGRMLFGKLMMQKPNV 459

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490918183 512 LVLDEATSSLDSETEHEIQADLQKLmEGrTSIIIAH-R--LSTImnADKIIVLDKGKIVQ-QGTHNQLIKEKGL 581
Cdd:PRK15064  460 LVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdRefVSSL--ATRIIEITPDGVVDfSGTYEEYLRSQGI 529
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 367-564 1.80e-11

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: 63.67  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 367 RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFDDTIYN 446
Cdd:cd03231    13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 447 NIAFSNPKAKRKDVFRAMKFAQLlkivnnfpkkekTVVGERGV-KLSGGEKQRVSIARAILADKKVLVLDEATSSLDSET 525
Cdd:cd03231    93 NLRFWHADHSDEQVEEALARVGL------------NGFEDRPVaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1490918183 526 EHEIQADLQKLMEGRTSIIIAHRLSTIMNADKIIVLDKG 564
Cdd:cd03231   161 VARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
 68-319 2.77e-11

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: 64.84  E-value: 2.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  68 LSNYTSILTIILLVFLAITIFNSagywLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRI-----IRg 142
Cdd:cd18555    38 LNLLNVLGIGILILFLLYGLFSF----LRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRAnsnvyIR- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 143 gsavERLTDVFVFNFAPLLFQFTIVAAsLLFIGVIPALISFFVVVVFIAYSYFINNIQQKSNLQLNQAEDEEKANISDVF 222
Cdd:cd18555   113 ----QILSNQVISLIIDLLLLVIYLIY-MLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 223 TNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWFSVTRFIAEDITIGTMVFLFTVF 302
Cdd:cd18555   188 YGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLA 267

                         250
                  ....*....|....*..
gi 1490918183 303 NNLFGPLFGFVHGMRNF 319
Cdd:cd18555   268 GSFLTPIVSLINSYNQF 284
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 365-573 2.99e-11

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: 63.97  E-value: 2.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 365 KKRKIFSDFNLK-----IPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKeFKQESLRSELSIVPQEcVL 439
Cdd:cd03237     5 TMKKTLGEFTLEveggsISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADYEGTVRD-LL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 440 FDDTiynNIAFSNPKAKrKDVFRAMKFAQLLkivnnfpkkektvvgERGV-KLSGGEKQRVSIARAILADKKVLVLDEAT 518
Cdd:cd03237    83 SSIT---KDFYTHPYFK-TEIAKPLQIEQIL---------------DREVpELSGGELQRVAIAACLSKDADIYLLDEPS 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 519 SSLDSEteheiqadlQKLMEGR-----------TSIIIAHRLSTI-MNADKIIVLDkGKIVQQGTHN 573
Cdd:cd03237   144 AYLDVE---------QRLMASKvirrfaennekTAFVVEHDIIMIdYLADRLIVFE-GEPSVNGVAN 200
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 366-579 4.64e-11

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: 65.23  E-value: 4.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 366 KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYD-VNSGAILIDGK--NIKEfKQESLRSELSIVPQE----CV 438
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKpvDIRN-PAQAIRAGIAMVPEDrkrhGI 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 439 LFDDTIYNNIAFS-----------NPKAKRKDVFRAMkfaQLLKIVNNFPKKEKTvvgergvKLSGGEKQRVSIARAILA 507
Cdd:TIGR02633 351 VPILGVGKNITLSvlksfcfkmriDAAAELQIIGSAI---QRLKVKTASPFLPIG-------RLSGGNQQKAVLAKMLLT 420

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490918183 508 DKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLIKEK 579
Cdd:TIGR02633 421 NPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKGDFVNHALTQEQ 494
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 367-524 5.36e-11

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: 61.99  E-value: 5.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 367 RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSELSIVPQECVLFDDTIYN 446
Cdd:TIGR01189  13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 447 NIAFSNP--KAKRKDVFRAMKFAQLLKIvnnfpkkEKTVVGErgvkLSGGEKQRVSIARAILADKKVLVLDEATSSLDSE 524
Cdd:TIGR01189  93 NLHFWAAihGGAQRTIEDALAAVGLTGF-------EDLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 367-562 5.84e-11

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: 65.19  E-value: 5.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 367 RKIFSDFNL-----KIPRNKKIALVGPSGSGKTTLIRLLfrlydvnSGAILIDGKNIKEfkqeSLRseLSIVPQECV-LF 440
Cdd:COG1245   348 TKSYGGFSLeveggEIREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVDE----DLK--ISYKPQYISpDY 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 441 DDTIYNNIAFSNPKAK-----RKDVFRAMKFAQLLkivnnfpkkektvvgERGVK-LSGGEKQRVSIARAILADKKVLVL 514
Cdd:COG1245   415 DGTVEEFLRSANTDDFgssyyKTEIIKPLGLEKLL---------------DKNVKdLSGGELQRVAIAACLSRDADLYLL 479

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 515 DEATSSLDSETEHEIQADLQKLMEGR--TSIIIAHRLSTI-MNADKIIVLD 562
Cdd:COG1245   480 DEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLIdYISDRLMVFE 530
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 355-525 9.27e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 64.37  E-value: 9.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIdGKNIKefkqeslrseLSIVP 434
Cdd:PRK11819  325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------LAYVD 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLFDD--TIYNNIAFSNpkakrkDVFRAMKFaqllkIVN--------NF--PKKEKTVvgerGVkLSGGEKQRVSIA 502
Cdd:PRK11819  394 QSRDALDPnkTVWEEISGGL------DIIKVGNR-----EIPsrayvgrfNFkgGDQQKKV----GV-LSGGERNRLHLA 457

                         170       180
                  ....*....|....*....|...
gi 1490918183 503 RAILADKKVLVLDEATSSLDSET 525
Cdd:PRK11819  458 KTLKQGGNVLLLDEPTNDLDVET 480
ABC_6TM_ABCB6 cd18581
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ...
 44-311 1.22e-10

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


Pssm-ID: 350025 [Multi-domain]  Cd Length: 300  Bit Score: 62.65  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  44 RVINKY---LFKEVIDASTRFSTKALLLSNYTSILTIILLVFLAITIFNSAGywlrmhMINLLDARLIL--------DLK 112
Cdd:cd18581     9 RVVNVLvpiLYKKIVDSLTPDSADSPLAFPWALILLYVFLKFLQGGGSGSVG------LLSNLRSFLWIpvqqfttrEIS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 113 RKFFNHIIHLSYNFHSTHKTGSLISRIIRGGSAVERLTDVFVFNFAPLLFQftIVAASLLFIG---VIPALISFFVVVVF 189
Cdd:cd18581    83 VKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIAD--IIIAIIYFAIafnPWFGLIVFVTMALY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 190 IAYSYFINNIQQKSNLQLNQAEDEEKANISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLI 269
Cdd:cd18581   161 LILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNLLNTAQNLI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1490918183 270 LGIGLVLLVWFSVTRFIAEDITIGTMVFLFTVFNNLFGPL--FG 311
Cdd:cd18581   241 ITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPLnfFG 284
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
 49-254 1.32e-10

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: 62.44  E-value: 1.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  49 YLFKEVIDAstrfstkaLLLSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHS 128
Cdd:cd18552    20 WLLKPLLDD--------IFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 129 THKTGSLISRIIrggSAVERLTDVFVFNFAPLLFQ-FTIVA--ASLLFIGVIPALISFFVV-VVFIAYSYFINNIQQKSN 204
Cdd:cd18552    92 RNSSGDLISRIT---NDVNQVQNALTSALTVLVRDpLTVIGllGVLFYLDWKLTLIALVVLpLAALPIRRIGKRLRKISR 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1490918183 205 LQLNQAedeekANISDV----FTNIDSIKYFGKENRIKSIYRKFAVKTRNALLK 254
Cdd:cd18552   169 RSQESM-----GDLTSVlqetLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMK 217
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 359-571 1.33e-10

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 61.93  E-value: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 359 NVSFKYKKRKIFSdfnlkiprnkkiaLVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNI--------------KEFKQE 424
Cdd:PRK11300   23 NVNLEVREQEIVS-------------LIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFQHV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 425 SLRSELSIVPQECVLFDDTIYNNI---AFSNP---KAKRKDVFRAMKFAQ---LLKIVNNfpkkektvvgERGvKLSGGE 495
Cdd:PRK11300   90 RLFREMTVIENLLVAQHQQLKTGLfsgLLKTPafrRAESEALDRAATWLErvgLLEHANR----------QAG-NLAYGQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 496 KQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGT 571
Cdd:PRK11300  159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGT 237
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
356-568 1.67e-10

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 63.65  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 356 EFKNVSfkYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIkefkqeSLRSELSIVPQ 435
Cdd:PRK09700  267 EVRNVT--SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI------SPRSPLDAVKK 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 436 ECVLFDDTIYNNIAFSNPKAKRK-DVFRAMKFAQLLKIVNNFPKKEKTVVGERGVK---------------LSGGEKQRV 499
Cdd:PRK09700  339 GMAYITESRRDNGFFPNFSIAQNmAISRSLKDGGYKGAMGLFHEVDEQRTAENQREllalkchsvnqniteLSGGNQQKV 418

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 500 SIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMNA-DKIIVLDKGKIVQ 568
Cdd:PRK09700  419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
 49-255 1.77e-10

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: 62.04  E-value: 1.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  49 YLFKEVIDAstrFSTKALLLSNYTSILTIILLVFLAITIFnsaGYWLRMHMINLldARLI-LDLKRKFFNHIIHLSYNFH 127
Cdd:cd18541    20 RIIGRAIDA---LTAGTLTASQLLRYALLILLLALLIGIF---RFLWRYLIFGA--SRRIeYDLRNDLFAHLLTLSPSFY 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 128 STHKTGSLISRIIRGGSAVERLTDVFVFNFAPLLFQFTIVAASLLFIGVIPALISF--FVVVVFIAYsYFINNIQQKSnl 205
Cdd:cd18541    92 QKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALlpLPLLALLVY-RLGKKIHKRF-- 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1490918183 206 QLNQaedEEKANISD----VFTNIDSIKYFGKENRIKsiyRKFAVKTRNALLKN 255
Cdd:cd18541   169 RKVQ---EAFSDLSDrvqeSFSGIRVIKAFVQEEAEI---ERFDKLNEEYVEKN 216
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 366-566 1.90e-10

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 63.41  E-value: 1.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 366 KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYD-VNSGAILIDGKNIK-EFKQESLRSELSIVPQE-----CV 438
Cdd:PRK13549  274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKiRNPQQAIAQGIAMVPEDrkrdgIV 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 439 LFDDTIYNnIAFSNPK--AKRKDVFRAMKFAQLLKIVNNFpkKEKTVVGERGV-KLSGGEKQRVSIARAILADKKVLVLD 515
Cdd:PRK13549  354 PVMGVGKN-ITLAALDrfTGGSRIDDAAELKTILESIQRL--KVKTASPELAIaRLSGGNQQKAVLAKCLLLNPKILILD 430

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 516 EATSSLDSETEHEIqadlQKLM-----EGRTSIIIAHRLSTIMN-ADKIIVLDKGKI 566
Cdd:PRK13549  431 EPTRGIDVGAKYEI----YKLInqlvqQGVAIIVISSELPEVLGlSDRVLVMHEGKL 483
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 372-575 2.33e-10

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 62.43  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 372 DFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVN---SGAILIDGK---NIKEFKQESLRSElsivpQECVLFDDTIY 445
Cdd:PRK09473   34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGReilNLPEKELNKLRAE-----QISMIFQDPMT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 446 NniafSNPKAKRKDvfRAMKFAQLLKIVNNFPKKEKTVVGERGVKL--------------SGGEKQRVSIARAILADKKV 511
Cdd:PRK09473  109 S----LNPYMRVGE--QLMEVLMLHKGMSKAEAFEESVRMLDAVKMpearkrmkmyphefSGGMRQRVMIAMALLCRPKL 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 512 LVLDEATSSLDSETEHEIQADLQKLM-EGRTSII-IAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQL 575
Cdd:PRK09473  183 LIADEPTTALDVTVQAQIMTLLNELKrEFNTAIImITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV 249
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
371-574 2.40e-10

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 63.01  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 371 SDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKeFK--QESLRSELSIVP----QECVLFDDTI 444
Cdd:PRK11288  270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-IRspRDAIRAGIMLCPedrkAEGIIPVHSV 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 445 YNNIAFS------------NPKAKRKDvfrAMKFAQLLKIvnnfpkkeKTVVGERG-VKLSGGEKQRVSIARAILADKKV 511
Cdd:PRK11288  349 ADNINISarrhhlragcliNNRWEAEN---ADRFIRSLNI--------KTPSREQLiMNLSGGNQQKAILGRWLSEDMKV 417

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 512 LVLDEATSSLDSETEHEIQADLQKLME-GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQ 574
Cdd:PRK11288  418 ILLDEPTRGIDVGAKHEIYNVIYELAAqGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
ABC_6TM_CvaB_RaxB_like cd18567
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...
 67-306 3.35e-10

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


Pssm-ID: 350011 [Multi-domain]  Cd Length: 294  Bit Score: 61.32  E-value: 3.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  67 LLSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRI-----IR 141
Cdd:cd18567    33 IVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFgsldeIQ 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 142 G---GSAVERLTDVFVfnfapllfqfTIVAASLLFI-GVIPALISFFVVVVFIAYSYFINNIQQKSNLQLNQAEDEEKAN 217
Cdd:cd18567   113 QtltTGFVEALLDGLM----------AILTLVMMFLySPKLALIVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSH 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 218 ISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWFSVTRFIAEDITIGtMVF 297
Cdd:cd18567   183 FLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVG-MLF 261


                  ....*....
gi 1490918183 298 LFTVFNNLF 306
Cdd:cd18567   262 AFLAYKDQF 270
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 43-254 3.55e-10

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: 61.37  E-value: 3.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  43 TRVINKYLFKEVIDA------STRFSTKALLL-SNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKF 115
Cdd:cd18564    14 LRLLEPWPLKVVIDDvlgdkpLPGLLGLAPLLgPDPLALLLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 116 FNHIIHLSYNFHSTHKTGSLISRIIrggSAVERLTDVFVFNFAPLLFQ-FTIV--AASLLFIGVIPALISFFVV-VVFIA 191
Cdd:cd18564    94 FAHLQRLSLSFHDRRRTGDLLSRLT---GDVGAIQDLLVSGVLPLLTNlLTLVgmLGVMFWLDWQLALIALAVApLLLLA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 192 YSYFINNIQQKSNLQlNQAEDEEKANISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLK 254
Cdd:cd18564   171 ARRFSRRIKEASREQ-RRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLR 232
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
 73-314 4.47e-10

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: 61.04  E-value: 4.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  73 SILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRI-----IR---GGS 144
Cdd:cd18568    39 SLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFqenqkIRrflTRS 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 145 AVERLTDV-FVFNFAPLLFqftivaasllFIGVIPALISFFVVVVFIAYSYFINNIQQKSNLQLNQAEDEEKANISDVFT 223
Cdd:cd18568   119 ALTTILDLlMVFIYLGLMF----------YYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALT 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 224 NIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWFSVTRFIAEDITIGTMVFLFTVFN 303
Cdd:cd18568   189 GIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFG 268

                         250
                  ....*....|.
gi 1490918183 304 NLFGPLFGFVH 314
Cdd:cd18568   269 SVINPLLALVG 279
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 365-570 5.70e-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: 5.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  365 KKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLL------FRLYDvnSGAILIDGKNIKEFKQEsLRSELSIVPQECV 438
Cdd:TIGR00956   72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntdgFHIGV--EGVITYDGITPEEIKKH-YRGDVVYNAETDV 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  439 LFDD-TIYNNIAFS----NPKAKRKDVFR---AMKFAQLLKIVNNFPKKEKTVVGE---RGVklSGGEKQRVSIARAILA 507
Cdd:TIGR00956  149 HFPHlTVGETLDFAarckTPQNRPDGVSReeyAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLG 226

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490918183  508 DKKVLVLDEATSSLDSETEHEIQADLQKLmegrTSIIIAHRLSTIMNA--------DKIIVLDKGKIVQQG 570
Cdd:TIGR00956  227 GAKIQCWDNATRGLDSATALEFIRALKTS----ANILDTTPLVAIYQCsqdayelfDKVIVLYEGYQIYFG 293
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 355-571 6.57e-10

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 59.71  E-value: 6.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFS----------------------DFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAIL 412
Cdd:COG1134     5 IEVENVSKSYRLYHEPSrslkelllrrrrtrreefwalkDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 413 IDGKnikefkqeslrselsIVPqecvLFD------------DTIYNNIAF-----SNPKAKRKDVfraMKFAQLlkivnn 475
Cdd:COG1134    85 VNGR---------------VSA----LLElgagfhpeltgrENIYLNGRLlglsrKEIDEKFDEI---VEFAEL------ 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 476 fpkkektvvGE---RGVK-LSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME-GRTSIIIAHRLS 550
Cdd:COG1134   137 ---------GDfidQPVKtYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELREsGRTVIFVSHSMG 207

                         250       260
                  ....*....|....*....|..
gi 1490918183 551 TIMN-ADKIIVLDKGKIVQQGT 571
Cdd:COG1134   208 AVRRlCDRAIWLEKGRLVMDGD 229
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 370-566 8.55e-10

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 61.22  E-value: 8.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 370 FSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFK-QESLRSELSIVP---QECVLFDDT-- 443
Cdd:PRK15439  279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPedrQSSGLYLDApl 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 444 -------IYNNIAF-SNPKAKRKDVFRamkFAQLLKIvnNFPKKEKTVVGergvkLSGGEKQRVSIARAILADKKVLVLD 515
Cdd:PRK15439  359 awnvcalTHNRRGFwIKPARENAVLER---YRRALNI--KFNHAEQAART-----LSGGNQQKVLIAKCLEASPQLLIVD 428

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1490918183 516 EATSSLDSETEHEIQADLQKLMEGRTSII-IAHRLSTIMN-ADKIIVLDKGKI 566
Cdd:PRK15439  429 EPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQmADRVLVMHQGEI 481
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 379-564 9.94e-10

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 57.38  E-value: 9.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  379 RNKKIALVGPSGSGKTTLIRLLFRLYDVNS-GAILIDGKNIKEFKQESLRselsivpqecvlfddtiynniafsnpkakr 457
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLL------------------------------ 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  458 kdvframkfaqllkivnnfpkkeKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQA------ 531
Cdd:smart00382  51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrl 107

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1490918183  532 DLQKLMEGRTSIIIAH-------RLSTIMNADKIIVLDKG 564
Cdd:smart00382 108 LLLLKSEKNLTVILTTndekdlgPALLRRRFDRRIVLLLI 147
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
 49-254 1.79e-09

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: 58.98  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  49 YLFKEVIDAstrFSTKALLlsnyTSILTIILLVFLAITIFNSAGYWLrmhmINLLDARLILDLKRKFFNHIIHLSYNFHS 128
Cdd:cd18551    20 LLVKNLIDA---LSAGGSS----GGLLALLVALFLLQAVLSALSSYL----LGRTGERVVLDLRRRLWRRLLRLPVSFFD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 129 THKTGSLISRIIrggSAVERLTDVFVFNFAPLLFQFTIVAASLLFIGVIP---ALISFFVVVVFIAYSYFINNIQQKSNL 205
Cdd:cd18551    89 RRRSGDLVSRVT---NDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDwvlTLVTLAVVPLAFLIILPLGRRIRKASK 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1490918183 206 QLNQAEDEEKANISDVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLK 254
Cdd:cd18551   166 RAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLK 214
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 383-567 1.85e-09

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 60.43  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 383 IAlvGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFKQESLRSE-LSIVPQE-----CVLfDDTIYNNIA---FSNP 453
Cdd:COG3845   289 IA--GVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDrlgrgLVP-DMSVAENLIlgrYRRP 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 454 KAKRKDVFR---AMKFAQllKIVNNF---PKKEKTVVGergvKLSGGEKQRVSIARAILADKKVLVLDEATSSLD---SE 524
Cdd:COG3845   366 PFSRGGFLDrkaIRAFAE--ELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDvgaIE 439

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1490918183 525 TEHeiqadlQKLME----GRTSIIIAHRLSTIMN-ADKIIVLDKGKIV 567
Cdd:COG3845   440 FIH------QRLLElrdaGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
 75-243 2.02e-09

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: 58.95  E-value: 2.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  75 LTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRIIrggSAVERLTDVFV 154
Cdd:cd18547    44 LLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVT---NDVDNISQALS 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 155 FNFAPLLFQFTIVAASLLF----------IGVIPALISFFVVVVFIAYS--YFINniQQKSNLQLNqaedeekANISDVF 222
Cdd:cd18547   121 QSLTQLISSILTIVGTLIMmlyisplltlIVLVTVPLSLLVTKFIAKRSqkYFRK--QQKALGELN-------GYIEEMI 191

                         170       180
                  ....*....|....*....|.
gi 1490918183 223 TNIDSIKYFGKENRIKSIYRK 243
Cdd:cd18547   192 SGQKVVKAFNREEEAIEEFDE 212
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
 49-241 2.09e-09

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: 58.80  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  49 YLFKEVIDASTRFST--KALLLSNYTSILTIILLVFLAITIFNSagywLRMHMINLLDARLILDLKRKFFNHIIHLSYNF 126
Cdd:cd18780    17 YFFGQVIDAVTNHSGsgGEEALRALNQAVLILLGVVLIGSIATF----LRSWLFTLAGERVVARLRKRLFSAIIAQEIAF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 127 HSTHKTGSLISR------IIRggSAVERLTDVFVFNFAP----LLFQFTIVAA-SLLFIGVIPALIsffvvVVFIAYSYF 195
Cdd:cd18780    93 FDVTRTGELLNRlssdtqVLQ--NAVTVNLSMLLRYLVQiiggLVFMFTTSWKlTLVMLSVVPPLS-----IGAVIYGKY 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1490918183 196 INNIQQKsnLQLNQAEDEEKANisDVFTNIDSIKYFGKENRIKSIY 241
Cdd:cd18780   166 VRKLSKK--FQDALAAASTVAE--ESISNIRTVRSFAKETKEVSRY 207
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 72-139 3.20e-09

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: 58.26  E-value: 3.20e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183  72 TSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRI 139
Cdd:cd18575    32 TALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRL 99
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 383-578 3.22e-09

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 58.60  E-value: 3.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 383 IALVGPSGSGKTTLIRLLFRLYD----VNSGAILIDGKNIKEFKQESLR----SELSIVPQE-------CVLFDDTIYNN 447
Cdd:PRK11022   36 VGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDpmtslnpCYTVGFQIMEA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 448 IAFSNPKAKRKDVFRAMKFAQLLKI------VNNFPKKektvvgergvkLSGGEKQRVSIARAILADKKVLVLDEATSSL 521
Cdd:PRK11022  116 IKVHQGGNKKTRRQRAIDLLNQVGIpdpasrLDVYPHQ-----------LSGGMSQRVMIAMAIACRPKLLIADEPTTAL 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 522 DSetehEIQA-------DLQKlMEGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLIKE 578
Cdd:PRK11022  185 DV----TIQAqiielllELQQ-KENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDIFRA 244
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 359-540 3.40e-09

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 56.88  E-value: 3.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 359 NVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEfKQESLRSELSIVPQEC- 437
Cdd:PRK13540    6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRSg 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 438 ----VLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQLLkivnNFPKkektvvgerGVkLSGGEKQRVSIARAILADKKVLV 513
Cdd:PRK13540   85 inpyLTLRENCLYDIHFSPGAVGITELCRLFSLEHLI----DYPC---------GL-LSSGQKRQVALLRLWMSKAKLWL 150

                         170       180
                  ....*....|....*....|....*..
gi 1490918183 514 LDEATSSLDsetEHEIQADLQKLMEGR 540
Cdd:PRK13540  151 LDEPLVALD---ELSLLTIITKIQEHR 174
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
 49-243 4.10e-09

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: 57.91  E-value: 4.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  49 YLFKEVID-ASTRFSTKALLLSNYTSILTIILLVFLAitifNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFH 127
Cdd:cd18573    17 FAIGKLIDvASKESGDIEIFGLSLKTFALALLGVFVV----GAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 128 STHKTGSLISRI-----IRGGSAVERLTDvfvfnFAPLLFQFTIVAASLLFIGVIPALISFFVV--VVFIAYSY--FINN 198
Cdd:cd18573    93 DKNKTGELVSRLssdtsVVGKSLTQNLSD-----GLRSLVSGVGGIGMMLYISPKLTLVMLLVVppIAVGAVFYgrYVRK 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1490918183 199 IQQKsnLQlnqaedEEKANISDV----FTNIDSIKYFGKENRIKSIYRK 243
Cdd:cd18573   168 LSKQ--VQ------DALADATKVaeerLSNIRTVRAFAAERKEVERYAK 208
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 355-580 5.05e-09

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 57.11  E-value: 5.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLF--RLYDVNSGAILIDGKNIKEFKQESLRSELSI 432
Cdd:PRK09580    2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAGEGIF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 433 V----PQECVLFDDTIYNNIAFSNPKAKRK----DVFRAMKF----AQLLKIVNNFPKKEKTVvgergvKLSGGEKQRVS 500
Cdd:PRK09580   82 MafqyPVEIPGVSNQFFLQTALNAVRSYRGqeplDRFDFQDLmeekIALLKMPEDLLTRSVNV------GFSGGEKKRND 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 501 IARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTIMN---ADKIIVLDKGKIVQQGTHN--QL 575
Cdd:PRK09580  156 ILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDyikPDYVHVLYQGRIVKSGDFTlvKQ 235


                  ....*
gi 1490918183 576 IKEKG 580
Cdd:PRK09580  236 LEEQG 240
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 355-570 7.16e-09

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 57.02  E-value: 7.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFkYKKRKIFSDFNLKIPRNKKIALVGPSGSGKT-TLIRLLFRL---YDVNSGAILIDGKNIKEfkqESLRSEL 430
Cdd:PRK10418    5 IELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAP---CALRGRK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIvpqecvlfddTIYNN--IAFsNP----KAKRKDVFRAM----KFAQLLKIVNNFPKKE-KTVVGERGVKLSGGEKQRV 499
Cdd:PRK10418   81 IA----------TIMQNprSAF-NPlhtmHTHARETCLALgkpaDDATLTAALEAVGLENaARVLKLYPFEMSGGMLQRM 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490918183 500 SIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTS--IIIAHRLSTIMN-ADKIIVLDKGKIVQQG 570
Cdd:PRK10418  150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
367-562 7.37e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 58.67  E-value: 7.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 367 RKIFSDFNLK-----IPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGK------NIKEFKQESLRSELSIVPQ 435
Cdd:PRK13409  347 TKKLGDFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykpqYIKPDYDGTVEDLLRSITD 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 436 EcvlFDDTIYNNiafsnpkakrkDVFRAMKFAQLLkivnnfpkkektvvgERGVK-LSGGEKQRVSIARAILADKKVLVL 514
Cdd:PRK13409  427 D---LGSSYYKS-----------EIIKPLQLERLL---------------DKNVKdLSGGELQRVAIAACLSRDADLYLL 477

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 515 DEATSSLDSETEHEIQADLQKLMEGR--TSIIIAHRLSTI-MNADKIIVLD 562
Cdd:PRK13409  478 DEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMIdYISDRLMVFE 528
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
 372-571 9.44e-09

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


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 56.47  E-value: 9.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 372 DFNLKIPRNKKIALVGPSGSGKTTLI---------RLLFR------LYDVNSGA------ILIDGKNIKefkqeslRSEL 430
Cdd:cd03271    13 NIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLkkeqpgNHDRIEGLehidkvIVIDQSPIG-------RTPR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 431 SIVPQECVLFDD-----------TIYN-----------NIAfsnpkakrkDVFrAMKFAQLLKIVNNFPK---KEKTVV- 484
Cdd:cd03271    86 SNPATYTGVFDEirelfcevckgKRYNretlevrykgkSIA---------DVL-DMTVEEALEFFENIPKiarKLQTLCd 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 485 --------GERGVKLSGGEKQRVSIARAIL--ADKKVL-VLDEATSSLDSETEHEIQADLQKLME-GRTSIIIAHRLSTI 552
Cdd:cd03271   156 vglgyiklGQPATTLSGGEAQRIKLAKELSkrSTGKTLyILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVI 235

                         250       260
                  ....*....|....*....|....*
gi 1490918183 553 MNADKIIVL-----DK-GKIVQQGT 571
Cdd:cd03271   236 KCADWIIDLgpeggDGgGQVVASGT 260
ABC_6TM_T1SS_like cd18779
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ...
 72-319 1.04e-08

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


Pssm-ID: 350052 [Multi-domain]  Cd Length: 294  Bit Score: 56.79  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  72 TSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRI-----IR---GG 143
Cdd:cd18779    38 RDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLssnatIRellTS 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 144 SAVERLTD-VFVfnfapLLFQFTIVAASLLFIGVIpALISFFVVVVFIAysyfinniQQKSNLQLNQAEDEEKANIS--- 219
Cdd:cd18779   118 QTLSALLDgTLV-----LGYLALLFAQSPLLGLVV-LGLAALQVALLLA--------TRRRVRELMARELAAQAEAQsyl 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 220 -DVFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWFSVTRFIAEDITIGTMVFL 298
Cdd:cd18779   184 vEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLAL 263

                         250       260
                  ....*....|....*....|.
gi 1490918183 299 FTVFNNLFGPLFGFVHGMRNF 319
Cdd:cd18779   264 NALAGAFLAPLASLVGTAQQL 284
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
 49-254 1.24e-08

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: 56.71  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  49 YLFKEVIDASTRFSTKALLLSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHS 128
Cdd:cd18577    20 IVFGDLFDAFTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 129 THKTGSLISRI------IRGGSAvERLtdvfvfnfaPLLFQF--TIVAA-----------SLLFIGVIPalisfFVVVVF 189
Cdd:cd18577   100 KNGAGELTSRLtsdtnlIQDGIG-EKL---------GLLIQSlsTFIAGfiiafiyswklTLVLLATLP-----LIAIVG 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183 190 IAYSYFINNIQQKSNLQLNQAedeekANISD-VFTNIDSIKYFGKENRIKSIYRKFAVKTRNALLK 254
Cdd:cd18577   165 GIMGKLLSKYTKKEQEAYAKA-----GSIAEeALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIK 225
GguA NF040905
sugar ABC transporter ATP-binding protein;
367-567 1.56e-08

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 57.49  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 367 RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLF-RLYDVN-SGAILIDGKNIkefkqeslrsELSIVPQEC------- 437
Cdd:NF040905  273 RKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgRSYGRNiSGTVFKDGKEV----------DVSTVSDAIdaglayv 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 438 ---------VLfDDTIYNNIAFSN-PKAKRKDVFRAMKfaqLLKIVNNFPKKEKT---VVGERGVKLSGGEKQRVSIARA 504
Cdd:NF040905  343 tedrkgyglNL-IDDIKRNITLANlGKVSRRGVIDENE---EIKVAEEYRKKMNIktpSVFQKVGNLSGGNQQKVVLSKW 418

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490918183 505 ILADKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIV 567
Cdd:NF040905  419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINELAaEGKGVIVISSELPELLGmCDRIYVMNEGRIT 483
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
 59-259 1.63e-08

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: 56.30  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  59 TRFSTKALLLSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISR 138
Cdd:cd18549    25 VRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 139 IIrggsaverlTDVF----VFNFAP---LLFQFTIVAAS--LLFIGVIPALISFFVVVVFIAYSYFINNiqqksnlQLNQ 209
Cdd:cd18549   105 IT---------NDLFdiseLAHHGPedlFISIITIIGSFiiLLTINVPLTLIVFALLPLMIIFTIYFNK-------KMKK 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 210 AEDEEKANISDVFTNI-DSI------KYFGKENRIKsiyRKFAVKTRNALL-KNWNYF 259
Cdd:cd18549   169 AFRRVREKIGEINAQLeDSLsgirvvKAFANEEYEI---EKFDEGNDRFLEsKKKAYK 223
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 358-579 1.93e-08

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 56.94  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 358 KNVSFKYKKRKIfsdfnlkiprnkkIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKefkqesLRSelsivPQec 437
Cdd:PRK10762  269 NDVSFTLRKGEI-------------LGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV------TRS-----PQ-- 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 438 vlfdDTIYNNIAFSNPKAKRKDVFRAM------------KFAQLLKIVNNfpKKEKTVVGER----GVK----------L 491
Cdd:PRK10762  323 ----DGLANGIVYISEDRKRDGLVLGMsvkenmsltalrYFSRAGGSLKH--ADEQQAVSDFirlfNIKtpsmeqaiglL 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 492 SGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIahrLSTIMN-----ADKIIVLDKGKI 566
Cdd:PRK10762  397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIIL---VSSEMPevlgmSDRILVMHEGRI 473

                         250
                  ....*....|...
gi 1490918183 567 VQQGTHNQLIKEK 579
Cdd:PRK10762  474 SGEFTREQATQEK 486
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 491-567 2.04e-08

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 57.27  E-value: 2.04e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 491 LSGGEKQRVSIARAILADKKVLVLDEATSSLDSETeheIQADLQKLMEGRTSII-IAHRLSTIMN-ADKIIVLDKGKIV 567
Cdd:PRK11147  157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET---IEWLEGFLKTFQGSIIfISHDRSFIRNmATRIVDLDRGKLV 232
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 491-576 2.20e-08

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: 57.33  E-value: 2.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 491 LSGGEKQRVSIARAILAD---KKVLVLDEATSSLDSEteheiqaDLQKLME--------GRTSIIIAHRLSTIMNADKII 559
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFD-------DIKKLLEvlqrlvdkGNTVVVIEHNLDVIKTADYII 902

                          90       100
                  ....*....|....*....|...
gi 1490918183 560 VL-----DK-GKIVQQGTHNQLI 576
Cdd:TIGR00630 903 DLgpeggDGgGTVVASGTPEEVA 925
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 290-564 4.12e-08

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 56.66  E-value: 4.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  290 ITIGTMVFLFTV------FNN---LFGPLFGFVHGMRNFYRSMAD----------------FQDLFKYAKIKNEIEDLPN 344
Cdd:TIGR00956  674 IIIGFTVFFFFVyillteFNKgakQKGEILVFRRGSLKRAKKAGEtsasnkndieagevlgSTDLTDESDDVNDEKDMEK 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  345 AGKLKIVHGDIEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYD---VNSGAILIDGKNIkef 421
Cdd:TIGR00956  754 ESGEDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPL--- 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  422 kQESLRSELSIVPQECVlfddtiynniafsnpKAKRKDVFRAMKFAQLLKIVNNFPKKEK------------------TV 483
Cdd:TIGR00956  831 -DSSFQRSIGYVQQQDL---------------HLPTSTVRESLRFSAYLRQPKSVSKSEKmeyveevikllemesyadAV 894

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  484 VGERGVKLSGGEKQRVSIARAILADKKVLV-LDEATSSLDSETEHEIQADLQKLME-GRTSIIIAHRLS-TIMNA-DKII 559
Cdd:TIGR00956  895 VGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSaILFEEfDRLL 974


                   ....*
gi 1490918183  560 VLDKG 564
Cdd:TIGR00956  975 LLQKG 979
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
 77-296 4.90e-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: 54.90  E-value: 4.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  77 IILLVFLAItIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRI-----IR---GGSAVER 148
Cdd:cd18566    44 LVIGVVIAI-LLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLnsleqIReflTGQALLA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 149 LTDV-FVFNFAPLLFqftivaasllFIGVIPALISFFVVVVFIAYSYFINNIQQKSNLQLNQAEDEEKANISDVFTNIDS 227
Cdd:cd18566   123 LLDLpFVLIFLGLIW----------YLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHT 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 228 IKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWFSVTRFIAEDITIGTMV 296
Cdd:cd18566   193 IKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALI 261
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 342-550 6.79e-08

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


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 55.53  E-value: 6.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 342 LPNAGKLKIVHGDIEFKNVSFKYKK-RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNike 420
Cdd:TIGR00954 439 VPGRGIVEYQDNGIKFENIPLVTPNgDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG--- 515

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 421 fkqeslrsELSIVPQECVLFDDTIYNNIAFSNPKAKRKDvfRAMKFAQLLKIVNNFpkkEKTVVGERGVK---------- 490
Cdd:TIGR00954 516 --------KLFYVPQRPYMTLGTLRDQIIYPDSSEDMKR--RGLSDKDLEQILDNV---QLTHILEREGGwsavqdwmdv 582

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 491 LSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLmeGRTSIIIAHRLS 550
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 366-525 7.12e-08

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 55.33  E-value: 7.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 366 KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLfrlydvnSGailIDgkniKEFKQESLRSE---LSIVPQECVLfDD 442
Cdd:TIGR03719  17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---VD----KDFNGEARPQPgikVGYLPQEPQL-DP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 443 TI-------------------YNNI--AFSNPKAKRKDVFRAMkfAQLLKIVNN------------------FPKKEKTV 483
Cdd:TIGR03719  82 TKtvrenveegvaeikdaldrFNEIsaKYAEPDADFDKLAAEQ--AELQEIIDAadawdldsqleiamdalrCPPWDADV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1490918183 484 VgergvKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSET 525
Cdd:TIGR03719 160 T-----KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 360-585 8.28e-08

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 54.32  E-value: 8.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 360 VSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIkeFKQES-LRSELSIV----- 433
Cdd:COG4586    28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVP--FKRRKeFARRIGVVfgqrs 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 434 -------PQECVLFDDTIYNnIafsnPKAKRKDvfRAMKFAQLLKIVnnfPKKEKTVvgeRgvKLSGGEKQRVSIARAIL 506
Cdd:COG4586   106 qlwwdlpAIDSFRLLKAIYR-I----PDAEYKK--RLDELVELLDLG---ELLDTPV---R--QLSLGQRMRCELAAALL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 507 ADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLIKEKGLYK 583
Cdd:COG4586   171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNRerGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYK 250


                  ..
gi 1490918183 584 KL 585
Cdd:COG4586   251 TI 252
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
 80-254 8.50e-08

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


Pssm-ID: 350022 [Multi-domain]  Cd Length: 317  Bit Score: 54.38  E-value: 8.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  80 LVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFH--STHKTGSLISRIIRGGSAVERLTDVFVFNF 157
Cdd:cd18578    56 LMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTDASDVRGLVGDRLGLI 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 158 apllfqftIVAASLLFIGVIPALIS-------FFVVVVFIAYSYFINNIQQKSNLQLNQAEDEEKANI-SDVFTNIDSIK 229
Cdd:cd18578   136 --------LQAIVTLVAGLIIAFVYgwklalvGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIaSEAVSNIRTVA 207

                         170       180
                  ....*....|....*....|....*
gi 1490918183 230 YFGKENRIKSIYRKFAVKTRNALLK 254
Cdd:cd18578   208 SLTLEDYFLEKYEEALEEPLKKGLR 232
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
 72-309 9.12e-08

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: 54.03  E-value: 9.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  72 TSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRIIrggSAVERLTD 151
Cdd:cd18546    35 LGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMT---SDIDALSE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 152 VF---VFNFAPLLFQFTIVAASLLFIGVIPALISF-FVVVVFIAYSYFinniQQKSNLQLNQAEDEEKANISDV---FTN 224
Cdd:cd18546   112 LLqtgLVQLVVSLLTLVGIAVVLLVLDPRLALVALaALPPLALATRWF----RRRSSRAYRRARERIAAVNADLqetLAG 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 225 IDSIKYFGKENRIKSIYRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLVLLVWFSVTRFIAEDITIGTMV-FLFTVfN 303
Cdd:cd18546   188 IRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVaFLLYL-R 266


                  ....*.
gi 1490918183 304 NLFGPL 309
Cdd:cd18546   267 RFFAPI 272
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
 50-194 1.01e-07

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: 53.64  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  50 LFKEVIDASTRFSTkalllsnyTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHST 129
Cdd:cd18543    21 LTRRAIDGPIAHGD--------RSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDR 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 130 HKTGSLISRIIRGGSAVERLtdvfvFNFAPLLF----QFTIVAASLLFIGVIPALISFFVVVVFIAYSY 194
Cdd:cd18543    93 WQSGQLLSRATSDLSLVQRF-----LAFGPFLLgnllTLVVGLVVMLVLSPPLALVALASLPPLVLVAR 156
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
339-524 1.14e-07

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 52.54  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 339 IEDLPNAGKLKIVHGdiefknVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNI 418
Cdd:PRK13543    2 IEPLHTAPPLLAAHA------LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 419 KEFKQESLRSELSIVPQecVLFDDTIYNNIAFSNPKAKRkdvfRAMKF-AQLLKIVnNFPKKEKTVVGErgvkLSGGEKQ 497
Cdd:PRK13543   76 TRGDRSRFMAYLGHLPG--LKADLSTLENLHFLCGLHGR----RAKQMpGSALAIV-GLAGYEDTLVRQ----LSAGQKK 144

                         170       180
                  ....*....|....*....|....*..
gi 1490918183 498 RVSIARAILADKKVLVLDEATSSLDSE 524
Cdd:PRK13543  145 RLALARLWLSPAPLWLLDEPYANLDLE 171
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
367-586 2.04e-07

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 51.73  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 367 RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIK----EFKQESL--------RSELSivP 434
Cdd:PRK13538   14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdEYHQDLLylghqpgiKTELT--A 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QEcvlfddtiynNIAFSNP---KAKRKDVFRAMkfAQllkivnnfpkkektvVGERGVK------LSGGEKQRVSIARAI 505
Cdd:PRK13538   92 LE----------NLRFYQRlhgPGDDEALWEAL--AQ---------------VGLAGFEdvpvrqLSAGQQRRVALARLW 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 506 LADKKVLVLDEATSSLDSETeheiQADLQKLMEgrtsiiiAHrlstimnadkiivLDKGKIVQQGTHNQLIKEKGLYKKL 585
Cdd:PRK13538  145 LTRAPLWILDEPFTAIDKQG----VARLEALLA-------QH-------------AEQGGMVILTTHQDLPVASDKVRKL 200


                  .
gi 1490918183 586 W 586
Cdd:PRK13538  201 R 201
PLN03140 PLN03140
ABC transporter G family member; Provisional
 342-570 2.15e-07

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 54.08  E-value: 2.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  342 LPNAGKlKIVHGDIEFKNVSF-KYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVN---SGAILIDGKN 417
Cdd:PLN03140   153 LPNAAR-NIAESALGMLGINLaKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYR 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  418 IKEFKQEslRSELSIVPQECVLFDDTIYNNIAFS-------------NPKAKRK-----------DVF---RAMKFAQ-- 468
Cdd:PLN03140   232 LNEFVPR--KTSAYISQNDVHVGVMTVKETLDFSarcqgvgtrydllSELARREkdagifpeaevDLFmkaTAMEGVKss 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  469 -----LLKIVNNFPKKEkTVVGE---RGVklSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGR 540
Cdd:PLN03140   310 litdyTLKILGLDICKD-TIVGDemiRGI--SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLT 386

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1490918183  541 TSIIIAHRLS----TIMNADKIIVLDKGKIVQQG 570
Cdd:PLN03140   387 EATVLMSLLQpapeTFDLFDDIILLSEGQIVYQG 420
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 374-570 4.07e-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: 50.40  E-value: 4.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 374 NLKIPRNKKIALVGPSGSGKTTLirllfrlydVNSGailidgknIKEFKQESLRSELSIVPQECVLFDDtiynniafsnp 453
Cdd:cd03238    15 DVSIPLNVLVVVTGVSGSGKSTL---------VNEG--------LYASGKARLISFLPKFSRNKLIFID----------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 454 kakrkdvframkfaQLLKIVNNfpKKEKTVVGERGVKLSGGEKQRVSIARAILADKK--VLVLDEATSSLDSETEHEIQA 531
Cdd:cd03238    67 --------------QLQFLIDV--GLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1490918183 532 DLQKLM-EGRTSIIIAHRLSTIMNADKIIVLDK------GKIVQQG 570
Cdd:cd03238   131 VIKGLIdLGNTVILIEHNLDVLSSADWIIDFGPgsgksgGKVVFSG 176
hmuV PRK13547
heme ABC transporter ATP-binding protein;
367-571 5.26e-07

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 51.37  E-value: 5.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 367 RKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLL-------FRLYDVN-SGAILIDGKNIKEFKQESLRSELSIVPQ--- 435
Cdd:PRK13547   14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltggGAPRGARvTGDVTLNGEPLAAIDAPRLARLRAVLPQaaq 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 436 --------ECVLFDDTIYNNIAFSNPKAKRKDVFRAMKFAQllkivnnfpkkEKTVVGERGVKLSGGEKQRVSIARAI-- 505
Cdd:PRK13547   94 pafafsarEIVLLGRYPHARRAGALTHRDGEIAWQALALAG-----------ATALVGRDVTTLSGGELARVQFARVLaq 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 506 -------LADKKVLVLDEATSSLDSETEHEIQADLQKLME----GRTSIIIAHRLSTiMNADKIIVLDKGKIVQQGT 571
Cdd:PRK13547  163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwnlGVLAIVHDPNLAA-RHADRIAMLADGAIVAHGA 238
uvrA PRK00349
excinuclease ABC subunit UvrA;
491-582 5.74e-07

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 52.77  E-value: 5.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 491 LSGGEKQRVSIARAiLADK---KVL-VLDEATSSLDSEteheiqaDLQKLME--------GRTSIIIAHRLSTIMNADKI 558
Cdd:PRK00349  831 LSGGEAQRVKLAKE-LSKRstgKTLyILDEPTTGLHFE-------DIRKLLEvlhrlvdkGNTVVVIEHNLDVIKTADWI 902

                          90       100       110
                  ....*....|....*....|....*....|
gi 1490918183 559 IVL-----DK-GKIVQQGTHNQLIKEKGLY 582
Cdd:PRK00349  903 IDLgpeggDGgGEIVATGTPEEVAKVEASY 932
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
491-582 1.01e-06

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 51.95  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 491 LSGGEKQRVSIARAiLA----DKKVLVLDEATSSLdseteHEiqADLQKLME--------GRTSIIIAHRLSTIMNADKI 558
Cdd:COG0178   827 LSGGEAQRVKLASE-LSkrstGKTLYILDEPTTGL-----HF--HDIRKLLEvlhrlvdkGNTVVVIEHNLDVIKTADWI 898

                          90       100       110
                  ....*....|....*....|....*....|
gi 1490918183 559 IVL-----DK-GKIVQQGTHNQLIKEKGLY 582
Cdd:COG0178   899 IDLgpeggDGgGEIVAEGTPEEVAKVKASY 928
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 372-570 1.05e-06

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


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 49.95  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 372 DFNLKIPRNKKIALVGPSGSGKTTL-IRLLF----RLY------------------DVN-----SGAILIDGKNIKEfkq 423
Cdd:cd03270    13 NVDVDIPRNKLVVITGVSGSGKSSLaFDTIYaegqRRYveslsayarqflgqmdkpDVDsieglSPAIAIDQKTTSR--- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 424 eSLRSELSIVpqecvlfdDTIYNNIA--FSNPKAKRKdvframkFAQLLKIvnnfpKKEKTVVGERGVKLSGGEKQRVSI 501
Cdd:cd03270    90 -NPRSTVGTV--------TEIYDYLRllFARVGIRER-------LGFLVDV-----GLGYLTLSRSAPTLSGGEAQRIRL 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 502 ARAILAD-KKVL-VLDEATSSLDSETEHEIQADLQKLME-GRTSIIIAHRLSTIMNADKIIVL------DKGKIVQQG 570
Cdd:cd03270   149 ATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 370-561 1.07e-06

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: 50.44  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 370 FSDFNLKIPRNKKI-ALVGPSGSGKTTLIRLLFRLYDVNSGAI--------LID---GKNIKEFKQESLRSELSIV--PQ 435
Cdd:cd03236    15 FKLHRLPVPREGQVlGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDefrGSELQNYFTKLLEGDVKVIvkPQ 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 436 ecvlFDDTIynniafsnPKAKRKDVframkfAQLLKIVNNFPKKEKTV-------VGERGV-KLSGGEKQRVSIARAILA 507
Cdd:cd03236    95 ----YVDLI--------PKAVKGKV------GELLKKKDERGKLDELVdqlelrhVLDRNIdQLSGGELQRVAIAAALAR 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183 508 DKKVLVLDEATSSLDSETEHEIQADLQKLME-GRTSIIIAHRLSTI-MNADKIIVL 561
Cdd:cd03236   157 DADFYFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLAVLdYLSDYIHCL 212
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
 76-254 2.13e-06

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: 49.85  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  76 TIILLVFLAIT--IFNSAGYWLrMHMINlldARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRIirgGSAVERLTDVF 153
Cdd:cd18572    38 AVLLLLLLSVLsgLFSGLRGGC-FSYAG---TRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRL---TSDCQKVSDPL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 154 VFNFApllfqfTIVAASLLFIGVIP---------ALISFFVVVVFIAYSYFINNIQQKsnlqLNQAEDEEKANISDV--- 221
Cdd:cd18572   111 STNLN------VFLRNLVQLVGGLAfmfslswrlTLLAFITVPVIALITKVYGRYYRK----LSKEIQDALAEANQVaee 180

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1490918183 222 -FTNIDSIKYFGKENRIKSIYRKFAVKTRNALLK 254
Cdd:cd18572   181 aLSNIRTVRSFATEEREARRYERALDKALKLSVR 214
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
 67-185 2.33e-06

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


Pssm-ID: 350032 [Multi-domain]  Cd Length: 294  Bit Score: 49.80  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  67 LLSNYTSILTIILLVFLAITIFNSAGYWLR----MHMINLLDARLildlKRKFFNHIIHLSYNFHSTHKTGSLISRI--- 139
Cdd:cd18588    33 LVHRSLSTLDVLAIGLLVVALFEAVLSGLRtylfSHTTNRIDAEL----GARLFRHLLRLPLSYFESRQVGDTVARVrel 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 140 --IRG---GSAVERLTD-VFVFNFAPLLFQF-----TIVAASLLFIgvipALISFFV 185
Cdd:cd18588   109 esIRQfltGSALTLVLDlVFSVVFLAVMFYYsptltLIVLASLPLY----ALLSLLV 161
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
370-561 2.33e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 50.58  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 370 FSDFNLKIPRNKKI-ALVGPSGSGKTTLIRLLfrlydvnSGAI---LIDGKN-------IKEFKqeslRSELsivpQEcv 438
Cdd:PRK13409   88 FKLYGLPIPKEGKVtGILGPNGIGKTTAVKIL-------SGELipnLGDYEEepswdevLKRFR----GTEL----QN-- 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 439 LFDDTIYNNIafsnpKAKRK--------DVFRAmKFAQLLKIVNNFPKKEKTV-------VGERGVK-LSGGEKQRVSIA 502
Cdd:PRK13409  151 YFKKLYNGEI-----KVVHKpqyvdlipKVFKG-KVRELLKKVDERGKLDEVVerlglenILDRDISeLSGGELQRVAIA 224

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 503 RAILADKKVLVLDEATSSLDSETEHEIQADLQKLMEGRTSIIIAHRLSTI-MNADKIIVL 561
Cdd:PRK13409  225 AALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLdYLADNVHIA 284
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
 50-234 2.78e-06

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: 49.51  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  50 LFKEVIDAstrfstkaLLLSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHST 129
Cdd:cd18782    24 LFQVIIDK--------VLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 130 HKTGSLISRI-----IRG---GSAVERLTDV-FVFnfapllfqftIVAASLLFIGVIPALISFFVVVVFIAYSYFINNIQ 200
Cdd:cd18782    96 RPVGELSTRIseldtIRGfltGTALTTLLDVlFSV----------IYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPIL 165

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1490918183 201 QKSNLQLNQAEDEEKANISDVFTNIDSIKYFGKE 234
Cdd:cd18782   166 RRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAE 199
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
485-580 3.62e-06

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 49.35  E-value: 3.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 485 GERGVKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMN-ADKIIVLD 562
Cdd:NF000106  139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGATVLLTTQYMEEAEQlAHELTVID 218

                          90
                  ....*....|....*...
gi 1490918183 563 KGKIVQQGTHNQLIKEKG 580
Cdd:NF000106  219 RGRVIADGKVDELKTKVG 236
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 75-199 4.48e-06

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: 48.63  E-value: 4.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  75 LTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRIIrggSAVERLTDVFV 154
Cdd:cd18540    41 LTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVT---SDTQRLGEIIS 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1490918183 155 FNFAPLLFQFT---IVAASLLFIGVIPALISFFVV-VVFIAYSYFINNI 199
Cdd:cd18540   118 WGLVDLVWGITymiGILIVMLILNWKLALIVLAVVpVLAVVSIYFQKKI 166
ABC_6TM_NHLM_bacteriocin cd18569
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ...
 66-211 4.71e-06

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


Pssm-ID: 350013 [Multi-domain]  Cd Length: 294  Bit Score: 48.63  E-value: 4.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  66 LLLSNYTSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRIirggSA 145
Cdd:cd18569    32 ILVGGLPDWLRPLLLGMALTALLQGLLTWLQQYYLLRLETKLALSSSSRFFWHVLRLPVEFFSQRYAGDIASRV----QS 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 146 VERLTDVFVFNFAPLLFQ-FTIV--AASLLFIGVIPALISFFVVVVFIAYSYFINNIQQKSNLQLNQAE 211
Cdd:cd18569   108 NDRVANLLSGQLATTVLNlVMAVfyALLMLQYDVPLTLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDS 176
PLN03073 PLN03073
ABC transporter F family; Provisional
 355-522 5.35e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 49.47  E-value: 5.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKI-FSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGK-NIKEFKQESLRS-ELS 431
Cdd:PLN03073  509 ISFSDASFGYPGGPLlFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRMAVFSQHHVDGlDLS 588

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 432 ivpqecvlfddtiynniafSNPkakrkdvframkfaqLLKIVNNFP----KKEKTVVGERGVK----------LSGGEKQ 497
Cdd:PLN03073  589 -------------------SNP---------------LLYMMRCFPgvpeQKLRAHLGSFGVTgnlalqpmytLSGGQKS 634

                         170       180
                  ....*....|....*....|....*
gi 1490918183 498 RVSIARAILADKKVLVLDEATSSLD 522
Cdd:PLN03073  635 RVAFAKITFKKPHILLLDEPSNHLD 659
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
385-576 7.00e-06

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 48.26  E-value: 7.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 385 LVGPSGSGKTTLIRLL--------------FRLYDVNSGAIL------IDGKNIKEFKQEslrselsivPQECVLFDDTI 444
Cdd:PRK15093   38 LVGESGSGKSLIAKAIcgvtkdnwrvtadrMRFDDIDLLRLSprerrkLVGHNVSMIFQE---------PQSCLDPSERV 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 445 YNNIAFSNP----KAKRKDVF--RAMKFAQLLKIVNnfPKKEKTVVGERGVKLSGGEKQRVSIARAILADKKVLVLDEAT 518
Cdd:PRK15093  109 GRQLMQNIPgwtyKGRWWQRFgwRKRRAIELLHRVG--IKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPT 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490918183 519 SSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLI 576
Cdd:PRK15093  187 NAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELV 247
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 489-562 1.01e-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: 46.41  E-value: 1.01e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 489 VKLSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQKLME--GRTSIIIAHRLSTIMN-ADKIIVLD 562
Cdd:cd03222    70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 77-234 1.16e-05

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: 47.56  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  77 IILLVFLAITIFNsagyWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRIIRGGSAVERLTDVFVFN 156
Cdd:cd18565    59 LTVAAFLLESLFQ----YLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANS 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 157 FAPLLFQFTIVAASLLFIGVIPALISFFVVVVFIAYSY-FINNIQ------QKSNLQLNqaedeekANISDVFTNIDSIK 229
Cdd:cd18565   135 IIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYwFQRRIEpryravREAVGDLN-------ARLENNLSGIAVIK 207


                  ....*
gi 1490918183 230 YFGKE 234
Cdd:cd18565   208 AFTAE 212
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 370-522 1.82e-05

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 47.47  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 370 FSDFNLKIPRNKKI-ALVGPSGSGKTTLIRLLfrlydvnSGAIL-----IDGKN-----IKEFKQESLRSELSivpqecv 438
Cdd:COG1245    88 FRLYGLPVPKKGKVtGILGPNGIGKSTALKIL-------SGELKpnlgdYDEEPswdevLKRFRGTELQDYFK------- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 439 lfddTIYNNiafsNPKAKRK--------DVFRAmKFAQLLKIVNNFPKKEKTV-------VGERGVK-LSGGEKQRVSIA 502
Cdd:COG1245   154 ----KLANG----EIKVAHKpqyvdlipKVFKG-TVRELLEKVDERGKLDELAeklglenILDRDISeLSGGELQRVAIA 224

                         170       180
                  ....*....|....*....|
gi 1490918183 503 RAILADKKVLVLDEATSSLD 522
Cdd:COG1245   225 AALLRDADFYFFDEPSSYLD 244
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 358-574 2.12e-05

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 46.46  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 358 KNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLF-RL--------YDVNSGAiLIDGKNIKEFKQESL-R 427
Cdd:PRK11701   10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSaRLapdagevhYRMRDGQ-LRDLYALSEAERRRLlR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 428 SELSIVPQecvlfddtiynniafsNPK-AKRKDVF-------RAMkfaqllkivnnfpkkektVVGERG----------- 488
Cdd:PRK11701   89 TEWGFVHQ----------------HPRdGLRMQVSaggnigeRLM------------------AVGARHygdiratagdw 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 489 ---VKL------------SGGEKQRVSIARAILADKKVLVLDEATSSLDSetehEIQADLQKLMEGRTS------IIIAH 547
Cdd:PRK11701  135 lerVEIdaariddlpttfSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV----SVQARLLDLLRGLVRelglavVIVTH 210

                         250       260
                  ....*....|....*....|....*...
gi 1490918183 548 RLSTI-MNADKIIVLDKGKIVQQGTHNQ 574
Cdd:PRK11701  211 DLAVArLLAHRLLVMKQGRVVESGLTDQ 238
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 374-578 2.72e-05

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 46.93  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 374 NLKIPRNKKIALVGPSGSGKTTLIRLLfrlydvnSGA-ILIDGKNIKEFKQESLRS--ELS-IVPQE---------CVLF 440
Cdd:PRK10938   23 SLTLNAGDSWAFVGANGSGKSALARAL-------AGElPLLSGERQSQFSHITRLSfeQLQkLVSDEwqrnntdmlSPGE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 441 DDT-------IYNNIafsnpkakrKDVFRAMKFAQLLKIvnnfpkkeKTVVGERGVKLSGGEKQRVSIARAILADKKVLV 513
Cdd:PRK10938   96 DDTgrttaeiIQDEV---------KDPARCEQLAQQFGI--------TALLDRRFKYLSTGETRKTLLCQALMSEPDLLI 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490918183 514 LDEATSSLDSETEHEIQADLQKLM-EGRTSIIIAHRLSTIMN-ADKIIVLDKGKIVQQGTHNQLIKE 578
Cdd:PRK10938  159 LDEPFDGLDVASRQQLAELLASLHqSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 356-574 3.82e-05

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 46.65  E-value: 3.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 356 EFKNVSFKYKKRKIfsdfnlkiprnkkIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFK-QESLRSELSIVP 434
Cdd:PRK10982  263 SIRDVSFDLHKGEI-------------LGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVT 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QE----------CVLFDDTIYNNIAFSNP---------KAKRKDVFRAMKFAQllkivnnfpKKEKTVVGErgvkLSGGE 495
Cdd:PRK10982  330 EErrstgiyaylDIGFNSLISNIRNYKNKvglldnsrmKSDTQWVIDSMRVKT---------PGHRTQIGS----LSGGN 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 496 KQRVSIARAILADKKVLVLDEATSSLDSETEHEI-QADLQKLMEGRTSIIIAHRLSTIMN-ADKIIVLDKGK---IVQQG 570
Cdd:PRK10982  397 QQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLvagIVDTK 476


                  ....
gi 1490918183 571 THNQ 574
Cdd:PRK10982  477 TTTQ 480
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 366-525 3.88e-05

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 46.65  E-value: 3.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 366 KRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSG-AILIDG---------------KNIKEFKQESLRSE 429
Cdd:PRK11819   19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPGikvgylpqepqldpeKTVRENVEEGVAEV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 430 LSIVPQecvlFDDtIYNniAFSNPKAKRKDVFRAMkfAQLLKIVNNF------------------PKKEKTVVgergvKL 491
Cdd:PRK11819   99 KAALDR----FNE-IYA--AYAEPDADFDALAAEQ--GELQEIIDAAdawdldsqleiamdalrcPPWDAKVT-----KL 164

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1490918183 492 SGGEKQRVSIARAILADKKVLVLDEATSSLDSET 525
Cdd:PRK11819  165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
 45-309 5.90e-05

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: 45.49  E-value: 5.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  45 VINKYLFKEVIDAStrfstkALLLSNYTSILTIILLVFLAI-TIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLS 123
Cdd:cd18554    20 LILKYIVDDVIQGS------SLTLDEKVYKLFTIIGIMFFIfLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLS 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 124 YNFHSTHKTGSLISRIIrggSAVERLTDVFVFNFAPLLFQ---FTIVAASLLFIGVIPALISFFVVVVFIAYSYFINNIQ 200
Cdd:cd18554    94 LRYYANNRSGEIISRVI---NDVEQTKDFITTGLMNIWLDmitIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 201 QKSNLQLNQAEDEEKANISDVFTNIDSIKYFGKENRIKsiyRKFAVKTRNALLKNWNYFRWLDSGQLLILGIGLV---LL 277
Cdd:cd18554   171 RKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQ---KQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLaplLV 247

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1490918183 278 VWFSVTRFIAEDITIGTMVFLFTVFNNLFGPL 309
Cdd:cd18554   248 IGFAAYLVIEGNLTVGTLVAFVGYMERMYSPL 279
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 491-561 7.78e-05

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 45.98  E-value: 7.78e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183  491 LSGGEKQRVSIARAILADKK---VLVLDEATSSLDSeteHEIQADLQKLM----EGRTSIIIAHRLSTIMNADKIIVL 561
Cdd:PRK00635   810 LSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHT---HDIKALIYVLQslthQGHTVVIIEHNMHVVKVADYVLEL 884
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 307-579 1.11e-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: 45.39  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 307 GPLFGFVHGMRNFYRSMadFQDLFKYAKI--KNEIEDLPNAGKLKIVHGD----IEFKNVSFKYKKRKIFSDFNLKIPRN 380
Cdd:TIGR00630 306 GAIVPFKKSTTSYYRQM--FASLAEHLGFdlDTPWKDLPEEAQKAILYGSgeevIVVKYRNGGGETFRYHKPFEGVIPEL 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 381 KKIALVGPSGSGKTTLIRLL----------FRLYDvNSGAILIDGKNIKEFkqeslrSELSIvpQECVLFDDTIYNNiaf 450
Cdd:TIGR00630 384 ERRYLETESESMREYLEKFMserpcpscggTRLKP-EALAVTVGGKSIADV------SELSI--REAHEFFNQLTLT--- 451

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 451 SNPKAKRKDVFRAMKfaQLLKIVNNfpkkektvVG------ERGVK-LSGGEKQRVSIARAILAD-KKVL-VLDEATSSL 521
Cdd:TIGR00630 452 PEEKKIAEEVLKEIR--ERLGFLID--------VGldylslSRAAGtLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGL 521

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490918183 522 dseteHeiQADLQKLME--------GRTSIIIAHRLSTIMNADKIIVLDK------GKIVQQGTHNQLIKEK 579
Cdd:TIGR00630 522 -----H--QRDNRRLINtlkrlrdlGNTLIVVEHDEDTIRAADYVIDIGPgagehgGEVVASGTPEEILANP 586
ABC_6TM_ABCC_D1 cd18579
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ...
 116-320 1.16e-04

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


Pssm-ID: 350023 [Multi-domain]  Cd Length: 289  Bit Score: 44.40  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 116 FNHIIHLSYNFHSTHKTGSLISRIirgGSAVERLTDVFVF--NFAPLLFQFTIVAASL-LFIGViPALISFFVVVVFIAY 192
Cdd:cd18579    79 YRKALRLSSSARQETSTGEIVNLM---SVDVQRIEDFFLFlhYLWSAPLQIIVALYLLyRLLGW-AALAGLGVLLLLIPL 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 193 SYFINNIQQKSNLQLNQAEDEEKANISDVFTNIDSIKYFGKENriksIYRKFAVKTRNALLKNWNYFRWLDSGQllilgi 272
Cdd:cd18579   155 QAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEK----PFLKRIEELRKKELKALRKFGYLRALN------ 224

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 273 glvLLVWFSVTRFIAEdITIGTMVFL---------FTV---FNNLFGPLFGFVHGMRNFY 320
Cdd:cd18579   225 ---SFLFFSTPVLVSL-ATFATYVLLgnpltaakvFTAlslFNLLRFPLLMLPQAISSLI 280
ABC_6TM_McjD_like cd18556
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ...
 68-199 2.54e-04

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


Pssm-ID: 350000  Cd Length: 298  Bit Score: 43.40  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  68 LSNYTSILTIILLVFLAITIFnsAGYWLrMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRIIRGGSAVE 147
Cdd:cd18556    39 SYNYIVVLAALYVITISATKL--LGFLS-LYLQSSLRVELIISISSSYFRYLYEQPKTFFVKENSGDITQRLNQASNDLY 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1490918183 148 RLTDVFVFNFAPLLFQFTIVAASLLFIGvipaliSFFVVVVFIAY--SYFINNI 199
Cdd:cd18556   116 TLVRNLSTNILPPLLQLIIAIVVILSSG------DYFVAALFLLYavLFVINNT 163
AAA_22 pfam13401
AAA domain;
383-414 4.49e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 40.40  E-value: 4.49e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1490918183 383 IALVGPSGSGKTTLIRLLFRLYD-VNSGAILID 414
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQLPeVRDSVVFVD 40
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
491-579 7.17e-04

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 42.71  E-value: 7.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 491 LSGGEKQRVSIARAI---LADkkVL-VLDEATSSLdseteHeiQADLQKLME--------GRTSIIIAHRLSTIMNADKI 558
Cdd:COG0178   486 LSGGEAQRIRLATQIgsgLVG--VLyVLDEPSIGL-----H--QRDNDRLIEtlkrlrdlGNTVIVVEHDEDTIRAADYI 556

                          90       100
                  ....*....|....*....|....*....
gi 1490918183 559 IvlD--------KGKIVQQGTHNQLIKEK 579
Cdd:COG0178   557 I--DigpgagehGGEVVAQGTPEEILKNP 583
ABC_6TM_NdvA_beta-glucan_exporter_like cd18562
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ...
 50-239 8.90e-04

Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. 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: 350006 [Multi-domain]  Cd Length: 289  Bit Score: 41.46  E-value: 8.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  50 LFKEVIDASTRFSTKALLLSNYT--SILTIILLVFLAItifnsagywlrmhMINLLDARLILDLKRKFFNHIIHLSYNFH 127
Cdd:cd18562    21 LFGRVVDALSSGGDAFPLLALWAalGLFSILAGVLVAL-------------LADRLAHRRRLAVMASYFEHVITLPLSFH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 128 STHKTGSLISRIIRGGSAVERLTDVFVFNFAPLLFQFTIVAASLLFIGVIPALISFFVVVVFIAYSYFInniqqKSNLQL 207
Cdd:cd18562    88 SQRGSGRLLRIMLRGTDALFGLWLGFFREHLAALVSLIVLLPVALWMNWRLALLLVVLAAVYAALNRLV-----MRRTKA 162

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1490918183 208 NQAEDEEK-----ANISDVFTNIDSIKYFgkeNRIKS 239
Cdd:cd18562   163 GQAAVEEHhsalsGRVGDVIGNVTVVQSY---TRLAA 196
ABC_6TM_PrtD_LapB_HlyB_like cd18783
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
 72-229 1.51e-03

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


Pssm-ID: 350056 [Multi-domain]  Cd Length: 294  Bit Score: 40.96  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  72 TSILTIILLVFLAITIFNSAGYWLRMHMINLLDARLILDLKRKFFNHIIHLSYNFHSTHKTGSLISRI-----IRG---G 143
Cdd:cd18783    38 YSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMqqierIRQfltG 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 144 SAVERLTDVF-VFNFAPLLFQFTIVAAS--LLFIGVIpALISFFVVvvfiaysyfinNIQQKSNLQLNQAEDEEKANISD 220
Cdd:cd18783   118 QLFGTLLDATsLLVFLPVLFFYSPTLALvvLAFSALI-ALIILAFL-----------PPFRRRLQALYRAEGERQAFLVE 185


                  ....*....
gi 1490918183 221 VFTNIDSIK 229
Cdd:cd18783   186 TVHGIRTVK 194
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 371-411 1.67e-03

Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 41.57  E-value: 1.67e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1490918183 371 SDFNLKIPRNkkIALVGPSGSGKTTLI-RLLFrlydvNSGAI 411
Cdd:COG0480     2 AEYPLEKIRN--IGIVAHIDAGKTTLTeRILF-----YTGAI 36
flhA PRK06012
flagellar type III secretion system protein FlhA;
132-245 1.89e-03

flagellar type III secretion system protein FlhA;


Pssm-ID: 235672 [Multi-domain]  Cd Length: 697  Bit Score: 41.26  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 132 TGSLISRIIRGGSAVERLTDVFvFNFAPLLFqftIVAASLLFIGVIPAL--ISFFVV-VVFIAYSYFINNIQQKSNLQLN 208
Cdd:PRK06012  263 AGIIVTRVSSDGDVGEQIVGQL-FANPKALY---IAAGVLFLLGLVPGMphLPFLLLaGLLGFLAYRLRKREKKAAELAA 338

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1490918183 209 ------QAEDEEKANISDVfTNIDSIK-YFGKE--------------NRIKSIYRKFA 245
Cdd:PRK06012  339 eeaeeeEAAEPEEESWDDV-LPVDPLElEVGYGliplvdenqggellDRIRSIRKKIA 395
ftsH CHL00176
cell division protein; Validated
 171-396 2.01e-03

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 41.19  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 171 LLFIGVIPALISFFVVVVFIaYSYFINNIQQKSNLQLNQAEDEEK--------------ANISDVFTN--IDSIKYFGKE 234
Cdd:CHL00176    8 AILISLPLIVEKFTVWDVFY-YSSVEDGLKSPNNPDVVQNKASSRmtygrfleyldmgwIKKVDLYDNgrTAIVEASSPE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 235 --NRIKSIYRKFAVKTRNALLKNWNYFRWLDSgqlliLGIGLVLLVWFSVTRFIAEDITIGTMVFLFTVFNNLFGplfGF 312
Cdd:CHL00176   87 lgNRPQRIRVELPVGASELIQKLKEANIDFDA-----HPPVLKSNIVTILSNLLLPLILIGVLWFFFQRSSNFKG---GP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 313 VHGMRNFYRSMADFQDLFKYAKIKNEIEDLPNAGKlkivhgdiEFKNVSFKYKKRKIFSDFNLKIPrnKKIALVGPSGSG 392
Cdd:CHL00176  159 GQNLMNFGKSKARFQMEADTGITFRDIAGIEEAKE--------EFEEVVSFLKKPERFTAVGAKIP--KGVLLVGPPGTG 228


                  ....
gi 1490918183 393 KTTL 396
Cdd:CHL00176  229 KTLL 232
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 383-432 2.37e-03

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 40.27  E-value: 2.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1490918183 383 IALVGPSGSGKTTLIR-LLFRlydvnSGAI-----LIDGKNIKEFKQESLRSELSI 432
Cdd:cd04170     2 IALVGHSGSGKTTLAEaLLYA-----TGAIdrlgrVEDGNTVSDYDPEEKKRKMSI 52
COG4639 COG4639
Predicted kinase [General function prediction only];
383-406 2.76e-03

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 38.66  E-value: 2.76e-03
                          10        20
                  ....*....|....*....|....
gi 1490918183 383 IALVGPSGSGKTTLIRLLFRLYDV 406
Cdd:COG4639     5 VVLIGLPGSGKSTFARRLFAPTEV 28
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
 356-547 3.80e-03

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


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 39.17  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 356 EFKNVSFKYKKRKIfsDFNlKIPRNKKIALVGPSGSGKTTLIR-LLFRLYdvnsgailidGKNIKEFKQESLRSELSivP 434
Cdd:cd03279     7 ELKNFGPFREEQVI--DFT-GLDNNGLFLICGPTGAGKSTILDaITYALY----------GKTPRYGRQENLRSVFA--P 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 435 QECVLfddtiynNIAFS---NPKAKRKDVFRAMKFAQLLKIVnNFPKKEKTVVGERGVK-LSGGEKQRVSIARAI-LADK 509
Cdd:cd03279    72 GEDTA-------EVSFTfqlGGKKYRVERSRGLDYDQFTRIV-LLPQGEFDRFLARPVStLSGGETFLASLSLALaLSEV 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1490918183 510 ---------KVLVLDEATSSLDSETEHEIQADLQKL-MEGRTSIIIAH 547
Cdd:cd03279   144 lqnrggarlEALFIDEGFGTLDPEALEAVATALELIrTENRMVGVISH 191
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 489-559 4.45e-03

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: 38.11  E-value: 4.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490918183 489 VKLSGGEKQRVSIARAI-LADKK---VLVLDEATSSLDSEtehEIQADLQKLME----GRTSIIIAHRLSTIMNADKII 559
Cdd:cd03227    76 LQLSGGEKELSALALILaLASLKprpLYILDEIDRGLDPR---DGQALAEAILEhlvkGAQVIVITHLPELAELADKLI 151
PLN03140 PLN03140
ABC transporter G family member; Provisional
 384-564 5.42e-03

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 39.83  E-value: 5.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  384 ALVGPSGSGKTTLIRLLF--RLYDVNSGAILIDG--KNIKEFKQESLRSELSIV--PQECVLfDDTIYNniAFSN-PKAK 456
Cdd:PLN03140   910 ALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGfpKKQETFARISGYCEQNDIhsPQVTVR-ESLIYS--AFLRlPKEV 986

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183  457 RKDvfRAMKFA-QLLKIVNNFPKKEkTVVGERGVK-LSGGEKQRVSIARAILADKKVLVLDEATSSLDSETEHEIQADLQ 534
Cdd:PLN03140   987 SKE--EKMMFVdEVMELVELDNLKD-AIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVR 1063

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1490918183  535 KLME-GRTSIIIAHRLST-IMNA-DKIIVLDKG 564
Cdd:PLN03140  1064 NTVDtGRTVVCTIHQPSIdIFEAfDELLLMKRG 1096
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
355-400 5.69e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 39.72  E-value: 5.69e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1490918183 355 IEFKNVSFKYKKRKIFSDFNLKIPRNKKIALVGPSGSGKTTLIRLL 400
Cdd:NF033858    2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI 47
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 370-448 5.72e-03

Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 39.23  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 370 FSDFNLKIPR--NKK-----IALVGPSGSGKTTLIRLLFrlydvnsGAILIDGKNIKEFKQESLRSELSIVPQECVLFDD 442
Cdd:COG5019     6 ISNLPNQRHRklSKKgidftIMVVGESGLGKTTFINTLF-------GTSLVDETEIDDIRAEGTSPTLEIKITKAELEED 78


                  ....*.
gi 1490918183 443 TIYNNI 448
Cdd:COG5019    79 GFHLNL 84
uvrA PRK00349
excinuclease ABC subunit UvrA;
410-579 6.09e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 39.67  E-value: 6.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 410 AILIDGKNIKEFkqeslrSELSIvpQECVLFddtiYNNIAFSNpkakrkdvfRAMKFAQL--------LKIVNNfpkkek 481
Cdd:PRK00349  423 AVKVGGKNIGEV------SELSI--GEALEF----FENLKLSE---------QEAKIAEPilkeirerLKFLVD------ 475

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 482 tvVG------ERGVK-LSGGEKQRVSIARAI---LADkkVL-VLDEATSSLdseteHeiQADLQKLME--------GRTS 542
Cdd:PRK00349  476 --VGldyltlSRSAGtLSGGEAQRIRLATQIgsgLTG--VLyVLDEPSIGL-----H--QRDNDRLIEtlkhlrdlGNTL 544

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1490918183 543 IIIAHRLSTIMNADKIIvlD--------KGKIVQQGTHNQLIKEK 579
Cdd:PRK00349  545 IVVEHDEDTIRAADYIV--DigpgagvhGGEVVASGTPEEIMKNP 587
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 379-414 6.10e-03

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


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 38.53  E-value: 6.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 379 RNKKIALVGPSGSGKTTLIRLLF------------------------RLYDVNSGAILID 414
Cdd:cd01854    84 KGKTSVLVGQSGVGKSTLLNALLpelvlatgeiseklgrgrhttthrELFPLPGGGLIID 143
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
372-396 6.51e-03

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 39.62  E-value: 6.51e-03
                          10        20
                  ....*....|....*....|....*
gi 1490918183 372 DFNLKIPRNKKIALVGPSGSGKTTL 396
Cdd:COG0178    18 NIDVDIPRNKLVVITGLSGSGKSSL 42
AAA_28 pfam13521
AAA domain;
382-404 7.57e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 37.63  E-value: 7.57e-03
                          10        20
                  ....*....|....*....|...
gi 1490918183 382 KIALVGPSGSGKTTLIRLLFRLY 404
Cdd:pfam13521   1 RIVITGGPSTGKTTLAEALAARF 23
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 355-524 7.76e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 37.93  E-value: 7.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 355 IEFKNVSFKYKKRKIFsDFNLKIPRNKKIALVGPSGSGKTTLIRLLFRLYDVNSGAILIDGKNIKEFK---------QES 425
Cdd:PRK13541    2 LSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpyctyighNLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490918183 426 LRSELSIvpQECVLFDDTIYNNIAFsnpkakrkdVFRAMKFAQLLKIVNnfpkkektvvgERGVKLSGGEKQRVSIARAI 505
Cdd:PRK13541   81 LKLEMTV--FENLKFWSEIYNSAET---------LYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLI 138

                         170
                  ....*....|....*....
gi 1490918183 506 LADKKVLVLDEATSSLDSE 524
Cdd:PRK13541  139 ACQSDLWLLDEVETNLSKE 157
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 381-406 7.93e-03

Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 442405 [Multi-domain]  Cd Length: 178  Bit Score: 37.88  E-value: 7.93e-03
                          10        20
                  ....*....|....*....|....*.
gi 1490918183 381 KKIALVGPSGSGKTTLIRLLFRLYDV 406
Cdd:COG3172     9 KKIVLLGAESTGKTTLARALAAHYNT 34
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
379-404 9.99e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 37.27  E-value: 9.99e-03
                          10        20
                  ....*....|....*....|....*.
gi 1490918183 379 RNKKIALVGPSGSGKTTLIRLLFRLY 404
Cdd:COG1100     2 GEKKIVVVGTGGVGKTSLVNRLVGDI 27
 
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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