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Conserved domains on  [gi|1907190441|ref|XP_036010083|]
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ATP-binding cassette sub-family B member 10, mitochondrial isoform X1 [Mus musculus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
3-364 4.65e-158

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


:

Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 456.55  E-value: 4.65e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFY 82
Cdd:COG1132   222 ELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVL 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  83 SELMKGLGAGGRLWELLERQPRLPFNEGmVLDEKTFQGALEFRNVHFTYParPEVSVFQDFSLSIPSGSVTALVGPSGSG 162
Cdd:COG1132   302 NQLQRALASAERIFELLDEPPEIPDPPG-AVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSG 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 163 KSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANA 242
Cdd:COG1132   379 KSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD---ATDEEVEEAAKAAQA 455

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 243 AEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRL 322
Cdd:COG1132   456 HEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRL 535

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1907190441 323 STIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKLMNKQS 364
Cdd:COG1132   536 STIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRLQF 576
 
Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
3-364 4.65e-158

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 456.55  E-value: 4.65e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFY 82
Cdd:COG1132   222 ELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVL 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  83 SELMKGLGAGGRLWELLERQPRLPFNEGmVLDEKTFQGALEFRNVHFTYParPEVSVFQDFSLSIPSGSVTALVGPSGSG 162
Cdd:COG1132   302 NQLQRALASAERIFELLDEPPEIPDPPG-AVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSG 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 163 KSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANA 242
Cdd:COG1132   379 KSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD---ATDEEVEEAAKAAQA 455

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 243 AEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRL 322
Cdd:COG1132   456 HEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRL 535

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1907190441 323 STIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKLMNKQS 364
Cdd:COG1132   536 STIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRLQF 576
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 123-363 1.72e-149

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: 421.95  E-value: 1.72e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 123 EFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGT 202
Cdd:cd03249     2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 203 VSQEPVLFSCSVAENIAYGADnlsSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNP 282
Cdd:cd03249    82 VSQEPVLFDGTIAENIRYGKP---DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 283 KILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEElLLKPNGLYRKLMNK 362
Cdd:cd03249   159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDE-LMAQKGVYAKLVKA 237


                  .
gi 1907190441 363 Q 363
Cdd:cd03249   238 Q 238
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 3-359 4.71e-130

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 389.08  E-value: 4.71e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFY 82
Cdd:TIGR00958 362 EASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVY 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  83 SELMKGLGAGGRLWELLERQPRLPfNEGMvLDEKTFQGALEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSG 162
Cdd:TIGR00958 442 SGMMQAVGASEKVFEYLDRKPNIP-LTGT-LAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSG 519

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 163 KSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGadnLSSVTAQQVERAAEVANA 242
Cdd:TIGR00958 520 KSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYG---LTDTPDEEIMAAAKAANA 596

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 243 AEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEalDRLMEGRTVLIIAHRL 322
Cdd:TIGR00958 597 HDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRL 674

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1907190441 323 STIKNANFVAVLDHGKICEHGTHEELLLKPnGLYRKL 359
Cdd:TIGR00958 675 STVERADQILVLKKGSVVEMGTHKQLMEDQ-GCYKHL 710
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
78-363 1.11e-99

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 306.95  E-value: 1.11e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  78 LSSFYSELMKGLGAGGRLWELLERQPRLpfNEGmVLDEKTFQGALEFRNVHFTYPARpEVSVFQDFSLSIPSGSVTALVG 157
Cdd:PRK11176  301 LTNVNAQFQRGMAACQTLFAILDLEQEK--DEG-KRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVG 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 158 PSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNLSSvtAQQVERAA 237
Cdd:PRK11176  377 RSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYS--REQIEEAA 454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 238 EVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLI 317
Cdd:PRK11176  455 RMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLV 534

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907190441 318 IAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKLMNKQ 363
Cdd:PRK11176  535 IAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ-NGVYAQLHKMQ 579
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 140-292 2.73e-44

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: 150.11  E-value: 2.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 140 FQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFS-CSVAENI 218
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190441 219 AYGA---DNLSSVTAQQVERAAEVANAAEFIrsfpqgfDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATS 292
Cdd:pfam00005  81 RLGLllkGLSKREKDARAEEALEKLGLGDLA-------DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
131-334 3.06e-24

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 98.46  E-value: 3.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 131 YPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHdiRQLNPVWLRSKIgtvsqePVLF 210
Cdd:NF040873    2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAYVPQRSEV------PDSL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 211 SCSVAENIAYGA-------DNLSSVTAQQVERAAEVANAAEFIRsfpQGFDTvvgekgilLSGGQKQRIAIARALLKNPK 283
Cdd:NF040873   71 PLTVRDLVAMGRwarrglwRRLTRDDRAAVDDALERVGLADLAG---RQLGE--------LSGGQRQRALLAQGLAQEAD 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907190441 284 ILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKNANFVAVL 334
Cdd:NF040873  140 LLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
GguA NF040905
sugar ABC transporter ATP-binding protein;
122-338 3.51e-15

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 76.75  E-value: 3.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYdPN---SGTVSLDG-----HDIRQLNp 193
Cdd:NF040905    2 LEMRGITKTFPG---VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfKDIRDSE- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 194 vwlRSKIGTVSQE----PVLfscSVAENI-------AYGADNLSSVTAQQVERAAEVAnaaefIRSFPqgfDTVVGEKGI 262
Cdd:NF040905   77 ---ALGIVIIHQElaliPYL---SIAENIflgneraKRGVIDWNETNRRARELLAKVG-----LDESP---DTLVTDIGV 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 263 llsgGQKQRIAIARALLKNPKILLLDEATSAL-DAENEHLvqeaLDRLME----GRTVLIIAHRLSTI-KNANFVAVLDH 336
Cdd:NF040905  143 ----GKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAAL----LDLLLElkaqGITSIIISHKLNEIrRVADSITVLRD 214


                  ..
gi 1907190441 337 GK 338
Cdd:NF040905  215 GR 216
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 149-336 1.78e-14

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: 70.09  E-value: 1.78e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  149 SGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTV-SLDGHDIRQLNPVWLRskigtvsqepvlfscsvaeniaygadnlss 227
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLL------------------------------ 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  228 vtaqqveraaevanaaefirsfpqgfDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALD 307
Cdd:smart00382  51 --------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907190441  308 RLM-------EGRTVLIIAHRLSTIKNANFVAVLDH 336
Cdd:smart00382 105 LRLllllkseKNLTVILTTNDEKDLGPALLRRRFDR 140
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
119-354 1.92e-06

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 49.35  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 119 QGALEFRNV--HFTyparpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVvSLLLRLYDPNSGTVSLDgHDIRQLNPVWL 196
Cdd:NF000106   11 RNAVEVRGLvkHFG-----EVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWR-F*TWCANRRAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 197 RSKIGTvsQEPVlfSCSVAENIAyGADNLSSVTAQ-QVERAAEVANAAEFIRSFpqGFDTVVGEKGILLSGGQKQRIAIA 275
Cdd:NF000106   84 RRTIG*--HRPV--R*GRRESFS-GRENLYMIGR*lDLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 276 RALLKNPKILLLDEATSALDAENEHLV-QEALDRLMEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPN 353
Cdd:NF000106  157 ASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236


                  .
gi 1907190441 354 G 354
Cdd:NF000106  237 G 237
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
142-295 3.37e-06

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 48.97  E-value: 3.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 142 DFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI------RQLNPvwlrsKIGTVSQ------EPVL 209
Cdd:NF033858   19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadarhrRAVCP-----RIAYMPQglgknlYPTL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 210 fscSVAENIA-----YGADnlssvTAQQVERAAEVANA---AEFiRSFPQGfdtvvgeKgilLSGGQKQRIAIARALLKN 281
Cdd:NF033858   94 ---SVFENLDffgrlFGQD-----AAERRRRIDELLRAtglAPF-ADRPAG-------K---LSGGMKQKLGLCCALIHD 154

                         170
                  ....*....|....
gi 1907190441 282 PKILLLDEATSALD 295
Cdd:NF033858  155 PDLLILDEPTTGVD 168
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
140-295 1.43e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 47.04  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 140 FQDF------SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSL-----DGHDIRqlnpvwLRSKIGTVSQEpv 208
Cdd:NF033858  276 FGDFtavdhvSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDIA------TRRRVGYMSQA-- 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 209 lFSC----SVAENIAYGADnLSSVTAQQV-ERAAEVANA---AEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALLK 280
Cdd:NF033858  348 -FSLygelTVRQNLELHAR-LFHLPAAEIaARVAEMLERfdlADVADALPDS-----------LPLGIRQRLSLAVAVIH 414

                         170
                  ....*....|....*
gi 1907190441 281 NPKILLLDEATSALD 295
Cdd:NF033858  415 KPELLILDEPTSGVD 429
GguA NF040905
sugar ABC transporter ATP-binding protein;
121-295 2.25e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 43.24  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRN--VHftYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKS-TVVSLLLRLYDPN-SGTVSLDGHDIRqlnpvwl 196
Cdd:NF040905  257 VFEVKNwtVY--HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRNiSGTVFKDGKEVD------- 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 197 rskIGTVSQepvlfscSVAENIAY--------------------GADNLSSVTAQQV-ERAAEVANAAEF-----IRSfp 250
Cdd:NF040905  328 ---VSTVSD-------AIDAGLAYvtedrkgyglnliddikrniTLANLGKVSRRGViDENEEIKVAEEYrkkmnIKT-- 395

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907190441 251 QGFDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATSALD 295
Cdd:NF040905  396 PSVFQKVGN----LSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
 
Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
3-364 4.65e-158

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 456.55  E-value: 4.65e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFY 82
Cdd:COG1132   222 ELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVL 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  83 SELMKGLGAGGRLWELLERQPRLPFNEGmVLDEKTFQGALEFRNVHFTYParPEVSVFQDFSLSIPSGSVTALVGPSGSG 162
Cdd:COG1132   302 NQLQRALASAERIFELLDEPPEIPDPPG-AVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSG 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 163 KSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANA 242
Cdd:COG1132   379 KSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD---ATDEEVEEAAKAAQA 455

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 243 AEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRL 322
Cdd:COG1132   456 HEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRL 535

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1907190441 323 STIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKLMNKQS 364
Cdd:COG1132   536 STIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRLQF 576
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 123-363 1.72e-149

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: 421.95  E-value: 1.72e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 123 EFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGT 202
Cdd:cd03249     2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 203 VSQEPVLFSCSVAENIAYGADnlsSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNP 282
Cdd:cd03249    82 VSQEPVLFDGTIAENIRYGKP---DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 283 KILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEElLLKPNGLYRKLMNK 362
Cdd:cd03249   159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDE-LMAQKGVYAKLVKA 237


                  .
gi 1907190441 363 Q 363
Cdd:cd03249   238 Q 238
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 3-359 4.71e-130

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 389.08  E-value: 4.71e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFY 82
Cdd:TIGR00958 362 EASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVY 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  83 SELMKGLGAGGRLWELLERQPRLPfNEGMvLDEKTFQGALEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSG 162
Cdd:TIGR00958 442 SGMMQAVGASEKVFEYLDRKPNIP-LTGT-LAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSG 519

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 163 KSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGadnLSSVTAQQVERAAEVANA 242
Cdd:TIGR00958 520 KSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYG---LTDTPDEEIMAAAKAANA 596

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 243 AEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEalDRLMEGRTVLIIAHRL 322
Cdd:TIGR00958 597 HDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRL 674

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1907190441 323 STIKNANFVAVLDHGKICEHGTHEELLLKPnGLYRKL 359
Cdd:TIGR00958 675 STVERADQILVLKKGSVVEMGTHKQLMEDQ-GCYKHL 710
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
 6-363 8.97e-128

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: 379.04  E-value: 8.97e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   6 KYTGRVDQLLQLAQKEALARAGffgaagLSGNLIVLS------VLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLS 79
Cdd:TIGR02204 222 RFGGAVEKAYEAARQRIRTRAL------LTAIVIVLVfgaivgVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLS 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  80 SFYSELMKGLGAGGRLWELLERQPRLPFNEGMVLDEKTFQGALEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPS 159
Cdd:TIGR02204 296 EVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPS 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 160 GSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEV 239
Cdd:TIGR02204 376 GAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPD---ATDEEVEAAARA 452

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 240 ANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIA 319
Cdd:TIGR02204 453 AHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIA 532

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1907190441 320 HRLSTIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKLMNKQ 363
Cdd:TIGR02204 533 HRLATVLKADRIVVMDQGRIVAQGTHAELIAK-GGLYARLARLQ 575
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 5-363 1.66e-123

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: 372.24  E-value: 1.66e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   5 EKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSE 84
Cdd:COG2274   358 RRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQR 437

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  85 LMKGLGAGGRLWELLERQPRLPFNEGMVlDEKTFQGALEFRNVHFTYPARpEVSVFQDFSLSIPSGSVTALVGPSGSGKS 164
Cdd:COG2274   438 FQDAKIALERLDDILDLPPEREEGRSKL-SLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKS 515

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 165 TVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADnlsSVTAQQVERAAEVANAAE 244
Cdd:COG2274   516 TLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDP---DATDEEIIEAARLAGLHD 592

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 245 FIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLST 324
Cdd:COG2274   593 FIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLST 672

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1907190441 325 IKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKLMNKQ 363
Cdd:COG2274   673 IRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAELVQQQ 710
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 122-359 2.65e-121

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: 349.99  E-value: 2.65e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPEvSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 201
Cdd:cd03251     1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKN 281
Cdd:cd03251    80 LVSQDVFLFNDTVAENIAYGRPG---ATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441 282 PKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKL 359
Cdd:cd03251   157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKL 233
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 122-363 1.49e-111

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: 325.34  E-value: 1.49e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYParPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 201
Cdd:cd03253     1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKN 281
Cdd:cd03253    79 VVPQDTVLFNDTIGYNIRYGRPD---ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 282 PKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKLMN 361
Cdd:cd03253   156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK-GGLYAEMWK 234


                  ..
gi 1907190441 362 KQ 363
Cdd:cd03253   235 AQ 236
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 56-364 1.47e-110

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: 335.64  E-value: 1.47e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  56 MTVGELssFLMYAFWVGLSI--GGLSSFYSELMKGLGAGGRLWELLERQPRlpfnegmVLDE------KTFQGALEFRNV 127
Cdd:COG5265   293 MTVGDF--VLVNAYLIQLYIplNFLGFVYREIRQALADMERMFDLLDQPPE-------VADApdapplVVGGGEVRFENV 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 128 HFTY-PARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQE 206
Cdd:COG5265   364 SFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD 440

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 207 PVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILL 286
Cdd:COG5265   441 TVLFNDTIAYNIAYGRPD---ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILI 517

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441 287 LDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKLMNKQS 364
Cdd:COG5265   518 FDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ-GGLYAQMWARQQ 594
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 3-363 1.91e-110

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: 334.38  E-value: 1.91e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFY 82
Cdd:TIGR02203 215 ETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVN 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  83 SELMKGLGAGGRLWELLERQPRLpfNEGMVLDEKTfQGALEFRNVHFTYPARpEVSVFQDFSLSIPSGSVTALVGPSGSG 162
Cdd:TIGR02203 295 APMQRGLAAAESLFTLLDSPPEK--DTGTRAIERA-RGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSG 370

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 163 KSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGAdnLSSVTAQQVERAAEVANA 242
Cdd:TIGR02203 371 KSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR--TEQADRAEIERALAAAYA 448

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 243 AEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRL 322
Cdd:TIGR02203 449 QDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRL 528

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1907190441 323 STIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKLMNKQ 363
Cdd:TIGR02203 529 STIEKADRIVVMDDGRIVERGTHNELLAR-NGLYAQLHNMQ 568
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 120-351 1.84e-105

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: 309.93  E-value: 1.84e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 120 GALEFRNVHFTYpaRPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSK 199
Cdd:cd03254     1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALL 279
Cdd:cd03254    79 IGVVLQDTFLFSGTIMENIRLGRPN---ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAML 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907190441 280 KNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLK 351
Cdd:cd03254   156 RDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 78-349 4.33e-103

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: 315.16  E-value: 4.33e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  78 LSSFYSELMKGLGAGGRLWELLERQPRLPfNEGMVLDEKTFQGALEFRNVHFTYPARPEVsvFQDFSLSIPSGSVTALVG 157
Cdd:COG4988   294 LGSFYHARANGIAAAEKIFALLDAPEPAA-PAGTAPLPAAGPPSIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVG 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 158 PSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAA 237
Cdd:COG4988   371 PSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPD---ASDEELEAAL 447

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 238 EVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLI 317
Cdd:COG4988   448 EAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVIL 527

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907190441 318 IAHRLSTIKNANFVAVLDHGKICEHGTHEELL 349
Cdd:COG4988   528 ITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
78-363 1.11e-99

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 306.95  E-value: 1.11e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  78 LSSFYSELMKGLGAGGRLWELLERQPRLpfNEGmVLDEKTFQGALEFRNVHFTYPARpEVSVFQDFSLSIPSGSVTALVG 157
Cdd:PRK11176  301 LTNVNAQFQRGMAACQTLFAILDLEQEK--DEG-KRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVG 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 158 PSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNLSSvtAQQVERAA 237
Cdd:PRK11176  377 RSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYS--REQIEEAA 454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 238 EVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLI 317
Cdd:PRK11176  455 RMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLV 534

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907190441 318 IAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKLMNKQ 363
Cdd:PRK11176  535 IAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ-NGVYAQLHKMQ 579
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 5-361 2.60e-94

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: 292.83  E-value: 2.60e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   5 EKYTGRVDQLLQ--LAQKEALARAGFFGAA--GLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSS 80
Cdd:COG4987   215 DRALARLDAAEArlAAAQRRLARLSALAQAllQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPA 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  81 FYSELMKGLGAGGRLWELLERQPRLPFNEGMVLDEKtfQGALEFRNVHFTYPARPEvSVFQDFSLSIPSGSVTALVGPSG 160
Cdd:COG4987   295 AAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPG--GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSG 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 161 SGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVA 240
Cdd:COG4987   372 SGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD---ATDEELWAALERV 448

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 241 NAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAH 320
Cdd:COG4987   449 GLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITH 528

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1907190441 321 RLSTIKNANFVAVLDHGKICEHGTHEElLLKPNGLYRKLMN 361
Cdd:COG4987   529 RLAGLERMDRILVLEDGRIVEQGTHEE-LLAQNGRYRQLYQ 568
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 113-339 6.54e-93

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: 277.81  E-value: 6.54e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 113 LDEKTFQGALEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLN 192
Cdd:cd03248     3 LAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 193 PVWLRSKIGTVSQEPVLFSCSVAENIAYGadnLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRI 272
Cdd:cd03248    83 HKYLHSKVSLVGQEPVLFARSLQDNIAYG---LQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190441 273 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKI 339
Cdd:cd03248   160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 31-364 7.90e-92

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


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 289.72  E-value: 7.90e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  31 AAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRLWELLErQPRLPFNEG 110
Cdd:TIGR01846 367 AIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPRSAG 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 111 MVLDEKtFQGALEFRNVHFTY-PARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIR 189
Cdd:TIGR01846 446 LAALPE-LRGAITFENIRFRYaPDSPEV--LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLA 522

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 190 QLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNLSSvtaQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQK 269
Cdd:TIGR01846 523 IADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPF---EHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQR 599

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 270 QRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELL 349
Cdd:TIGR01846 600 QRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELL 679

                         330
                  ....*....|....*
gi 1907190441 350 LKpNGLYRKLMNKQS 364
Cdd:TIGR01846 680 AL-QGLYARLWQQQS 693
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 122-338 1.54e-91

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: 271.95  E-value: 1.54e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPEVsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 201
Cdd:cd03228     1 IEFKNVSFSYPGRPKP-VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLFSCSVAENIaygadnlssvtaqqveraaevanaaefirsfpqgfdtvvgekgilLSGGQKQRIAIARALLKN 281
Cdd:cd03228    80 YVPQDPFLFSGTIRENI---------------------------------------------LSGGQRQRIAIARALLRD 114

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190441 282 PKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGK 338
Cdd:cd03228   115 PPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 122-363 1.39e-90

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: 272.05  E-value: 1.39e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTY-PARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKI 200
Cdd:cd03252     1 ITFEHVRFRYkPDGPVI--LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQEPVLFSCSVAENIAYGADNLSsvtAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLK 280
Cdd:cd03252    79 GVVLQENVLFNRSIRDNIALADPGMS---MERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 281 NPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKLM 360
Cdd:cd03252   156 NPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLY 234


                  ...
gi 1907190441 361 NKQ 363
Cdd:cd03252   235 QLQ 237
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
35-366 1.83e-89

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 280.69  E-value: 1.83e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  35 SGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAfwvGLSIGGL---SSFYSELMKglgAGGRLWELLE-----RQPRLP 106
Cdd:PRK13657  249 ASTITMLAILVLGAALVQKGQLRVGEVVAFVGFA---TLLIGRLdqvVAFINQVFM---AAPKLEEFFEvedavPDVRDP 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 107 FNegmVLDEKTFQGALEFRNVHFTYP-ARPEVSvfqDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDG 185
Cdd:PRK13657  323 PG---AIDLGRVKGAVEFDDVSFSYDnSRQGVE---DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 186 HDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLS 265
Cdd:PRK13657  397 TDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD---ATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLS 473

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 266 GGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTH 345
Cdd:PRK13657  474 GGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSF 553

                         330       340
                  ....*....|....*....|.
gi 1907190441 346 EELLLKpNGLYRKLMNKQSFL 366
Cdd:PRK13657  554 DELVAR-GGRFAALLRAQGML 573
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 120-339 1.26e-76

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: 235.95  E-value: 1.26e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 120 GALEFRNVHFTYPARPEVSVfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSK 199
Cdd:cd03245     1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQEPVLFSCSVAENIAYGAdnlSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALL 279
Cdd:cd03245    80 IGYVPQDVTLFYGTLRDNITLGA---PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 280 KNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKI 339
Cdd:cd03245   157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 43-359 5.86e-74

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: 243.31  E-value: 5.86e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  43 VLYKGGLLMGSAHMTVGELSSFLmyafwvglSIggLSSFYSELMKGLGAGGRLWEL---------LERQPRLPFNE---- 109
Cdd:TIGR03796 394 ILVVGGLRVMEGQLTIGMLVAFQ--------SL--MSSFLEPVNNLVGFGGTLQELegdlnrlddVLRNPVDPLLEepeg 463

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 110 --GMVLDEKTFQGALEFRNVHFTYpARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHD 187
Cdd:TIGR03796 464 saATSEPPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIP 542

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 188 IRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAygadnL--SSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLS 265
Cdd:TIGR03796 543 REEIPREVLANSVAMVDQDIFLFEGTVRDNLT-----LwdPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLS 617

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 266 GGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRlmEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTH 345
Cdd:TIGR03796 618 GGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTH 695

                         330
                  ....*....|....
gi 1907190441 346 EELLLKPnGLYRKL 359
Cdd:TIGR03796 696 EELWAVG-GAYARL 708
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
3-363 1.22e-72

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 236.53  E-value: 1.22e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRvdQLLQLAQKEALARAGFFGAAGLSgNLIVLSvlykGGLLM---GSahMTVGELSSFLMYafwVGLSIG--- 76
Cdd:PRK10789  204 ADAEDTGK--KNMRVARIDARFDPTIYIAIGMA-NLLAIG----GGSWMvvnGS--LTLGQLTSFVMY---LGLMIWpml 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  77 GLSSFYSELMKGLGAGGRLWELLERQPRLPFNEGMVLDEKtfqGALEFRNVHFTYPARpEVSVFQDFSLSIPSGSVTALV 156
Cdd:PRK10789  272 ALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEGR---GELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGIC 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 157 GPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERA 236
Cdd:PRK10789  348 GPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPD---ATQQEIEHV 424

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 237 AEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVL 316
Cdd:PRK10789  425 ARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVI 504

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1907190441 317 IIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPnGLYRKLMNKQ 363
Cdd:PRK10789  505 ISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS-GWYRDMYRYQ 550
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 78-334 1.86e-70

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: 229.87  E-value: 1.86e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  78 LSSFYSELMKGLGAGGRLWELLERQPRlPFNEGMVLDEKTFQgALEFRNVHFTYPARPEVsvFQDFSLSIPSGSVTALVG 157
Cdd:TIGR02857 280 LGAQYHARADGVAAAEALFAVLDAAPR-PLAGKAPVTAAPAS-SLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVG 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 158 PSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGAdnlSSVTAQQVERAA 237
Cdd:TIGR02857 356 PSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR---PDASDAEIREAL 432

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 238 EVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLI 317
Cdd:TIGR02857 433 ERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLL 512

                         250
                  ....*....|....*..
gi 1907190441 318 IAHRLSTIKNANFVAVL 334
Cdd:TIGR02857 513 VTHRLALAALADRIVVL 529
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 120-344 1.55e-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: 217.75  E-value: 1.55e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 120 GALEFRNVHFTYpaRPEVS-VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRS 198
Cdd:cd03244     1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 199 KIGTVSQEPVLFSCSVAENIaygaDNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARAL 278
Cdd:cd03244    79 RISIIPQDPVLFSGTIRSNL----DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARAL 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 279 LKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGT 344
Cdd:cd03244   155 LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
 40-378 5.87e-69

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: 227.46  E-value: 5.87e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  40 VLSVLYKGGLLMGSAHMTVGELSSFLMYAfwvGLSIGGLSSFYSELMKGLGAGGRLWELLE-----RQPRLPFNEGMVld 114
Cdd:TIGR01192 254 MMCILVIGTVLVIKGELSVGEVIAFIGFA---NLLIGRLDQMSGFITQIFEARAKLEDFFDledsvFQREEPADAPEL-- 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 115 eKTFQGALEFRNVHFTYPARPEvSVFqDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV 194
Cdd:TIGR01192 329 -PNVKGAVEFRHITFEFANSSQ-GVF-DVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRE 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 195 WLRSKIGTVSQEPVLFSCSVAENIAYGADnlsSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAI 274
Cdd:TIGR01192 406 SLRKSIATVFQDAGLFNRSIRENIRLGRE---GATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAI 482

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 275 ARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKpNG 354
Cdd:TIGR01192 483 ARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK-DG 561

                         330       340
                  ....*....|....*....|....
gi 1907190441 355 LYRKLMNKQSFLSYNGAEQFLEPA 378
Cdd:TIGR01192 562 RFYKLLRRSGLLTNQPATKPLRKA 585
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 18-349 6.02e-68

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: 223.86  E-value: 6.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  18 AQKEALARAGFFGAAGLSGNLIVLS-VLYKGGLLMGSAHMTVGEL--SSFLMyafwvG-------LSIGGLSSFyselMK 87
Cdd:COG4618   230 LQARASDRAGGFSALSKFLRLLLQSaVLGLGAYLVIQGEITPGAMiaASILM-----GralapieQAIGGWKQF----VS 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  88 GLGAGGRLWELLERQPRLPfnEGMVLdeKTFQGALEFRNVHFTYPARPEVsVFQDFSLSIPSGSVTALVGPSGSGKSTVV 167
Cdd:COG4618   301 ARQAYRRLNELLAAVPAEP--ERMPL--PRPKGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLA 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 168 SLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAygadNLSSVTAQQVERAAEVANAAEFIR 247
Cdd:COG4618   376 RLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA----RFGDADPEKVVAAAKLAGVHEMIL 451

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 248 SFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTIK 326
Cdd:COG4618   452 RLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLA 531

                         330       340
                  ....*....|....*....|...
gi 1907190441 327 NANFVAVLDHGKICEHGTHEELL 349
Cdd:COG4618   532 AVDKLLVLRDGRVQAFGPRDEVL 554
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
17-356 5.94e-67

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 222.29  E-value: 5.94e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  17 LAQKEALARAGFFgaagLSGNLIVLSVLYKGGLLM-----GSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGA 91
Cdd:PRK10790  239 MARMQTLRLDGFL----LRPLLSLFSALILCGLLMlfgfsASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVA 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  92 GGRLWELLERqPRLPFNEgmvlDEKTFQ-GALEFRNVHFTYpaRPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLL 170
Cdd:PRK10790  315 GERVFELMDG-PRQQYGN----DDRPLQsGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLL 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 171 LRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADnlssVTAQQVERAAEVANAAEFIRSFP 250
Cdd:PRK10790  388 MGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD----ISEEQVWQALETVQLAELARSLP 463

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 251 QGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANF 330
Cdd:PRK10790  464 DGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADT 543

                         330       340
                  ....*....|....*....|....*.
gi 1907190441 331 VAVLDHGKICEHGTHEELLLKpNGLY 356
Cdd:PRK10790  544 ILVLHRGQAVEQGTHQQLLAA-QGRY 568
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
 48-363 6.66e-65

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


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 218.67  E-value: 6.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  48 GLLMGSAHMTVGELSSFlMYAF-WVGLSIGGLSSFYSELMKGLGAGGRLWELLERQPRlpfNEGMVLDEKTFQGALEFRN 126
Cdd:TIGR03797 381 ISLLGGAGLSLGSFLAF-NTAFgSFSGAVTQLSNTLISILAVIPLWERAKPILEALPE---VDEAKTDPGKLSGAIEVDR 456

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 127 VHFTYpaRPEVS-VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQ 205
Cdd:TIGR03797 457 VTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQ 534

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 206 EPVLFSCSVAENIAYGAdnlsSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKIL 285
Cdd:TIGR03797 535 NGRLMSGSIFENIAGGA----PLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRIL 610

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441 286 LLDEATSALDAENEHLVQEALDRLMEGRTVliIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPnGLYRKLMNKQ 363
Cdd:TIGR03797 611 LFDEATSALDNRTQAIVSESLERLKVTRIV--IAHRLSTIRNADRIYVLDAGRVVQQGTYDELMARE-GLFAQLARRQ 685
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 94-363 3.69e-63

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 211.61  E-value: 3.69e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  94 RLWELLERQPRLPFNEGMVLDEKtfQGALEFRNVHFTYPARPEvSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRL 173
Cdd:PRK11160  313 RINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRA 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 174 YDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNLS----SVTAQQVERAAEVANaaefirsf 249
Cdd:PRK11160  390 WDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASdealIEVLQQVGLEKLLED-------- 461

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 250 PQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNAN 329
Cdd:PRK11160  462 DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFD 541

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907190441 330 FVAVLDHGKICEHGTHEELLLKpNGLYRKLMNKQ 363
Cdd:PRK11160  542 RICVMDNGQIIEQGTHQELLAQ-QGRYYQLKQRL 574
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 18-351 4.52e-63

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


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 210.67  E-value: 4.52e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  18 AQKEALARAGFFGAAGLSGNLIVLS-VLYKGGLLMGSAHMTVGEL--SSFLMYAFW--VGLSIGGLSSFyselMKGLGAG 92
Cdd:TIGR01842 216 AQSAASDRAGMLSNLSKYFRIVLQSlVLGLGAYLAIDGEITPGMMiaGSILVGRALapIDGAIGGWKQF----SGARQAY 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  93 GRLWELLERQPrlPFNEGMVLDEKtfQGALEFRNVHFTyPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLR 172
Cdd:TIGR01842 292 KRLNELLANYP--SRDPAMPLPEP--EGHLSVENVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVG 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 173 LYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQG 252
Cdd:TIGR01842 367 IWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGEN---ADPEKIIEAAKLAGVHELILRLPDG 443

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 253 FDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTIKNANFV 331
Cdd:TIGR01842 444 YDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKI 523

                         330       340
                  ....*....|....*....|
gi 1907190441 332 AVLDHGKICEHGTHEELLLK 351
Cdd:TIGR01842 524 LVLQDGRIARFGERDEVLAK 543
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 83-367 6.15e-63

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 218.36  E-value: 6.15e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   83 SELMKGLGAGGRLWELLERQPRLPFNEgmvlDEKTFQG--ALEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSG 160
Cdd:PTZ00265   346 TEYMKSLEATNSLYEIINRKPLVENND----DGKKLKDikKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESG 421

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  161 SGKSTVVSLLLRLYDPNSGTVSL-DGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAY------------------G 221
Cdd:PTZ00265   422 CGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedG 501

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  222 ADNLSSVTAQQVERA------------------------------AEVANAA------EFIRSFPQGFDTVVGEKGILLS 265
Cdd:PTZ00265   502 NDSQENKNKRNSCRAkcagdlndmsnttdsneliemrknyqtikdSEVVDVSkkvlihDFVSALPDKYETLVGSNASKLS 581

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  266 GGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM--EGRTVLIIAHRLSTIKNANFVAVL--------- 334
Cdd:PTZ00265   582 GGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrergstv 661

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907190441  335 ------------------DHGK--------------------ICEHGTHEELLLKPNGLYRKLMNKQSFLS 367
Cdd:PTZ00265   662 dvdiigedptkdnkennnKNNKddnnnnnnnnnnkinnagsyIIEQGTHDALMKNKNGIYYTMINNQKVSS 732
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 32-361 2.87e-61

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: 209.21  E-value: 2.87e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  32 AGLSGNLIVLsVLYKGGLLMGSAHMTVGELSSF-LMYAFWVGlSIGGLSSFYSELMKGLGAGGRLWE--LLERQprlpFN 108
Cdd:TIGR01193 386 AVTKLILNVV-ILWTGAYLVMRGKLTLGQLITFnALLSYFLT-PLENIINLQPKLQAARVANNRLNEvyLVDSE----FI 459

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 109 EGMVLDEKT-FQGALEFRNVHFTYPARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHD 187
Cdd:TIGR01193 460 NKKKRTELNnLNGDIVINDVSYSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS 537

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 188 IRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADnlSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGG 267
Cdd:TIGR01193 538 LKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAK--ENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGG 615

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 268 QKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEgRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEE 347
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE 694

                         330
                  ....*....|....
gi 1907190441 348 LLLKpNGLYRKLMN 361
Cdd:TIGR01193 695 LLDR-NGFYASLIH 707
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 119-358 5.05e-60

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 209.89  E-value: 5.05e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  119 QGALEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYD----------------------- 175
Cdd:PTZ00265  1163 KGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdy 1242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  176 -------------------------------PNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADN 224
Cdd:PTZ00265  1243 qgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED 1322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  225 lssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQE 304
Cdd:PTZ00265  1323 ---ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907190441  305 ALDRLME--GRTVLIIAHRLSTIKNANFVAVLDH----GKICE-HGTHEELLLKPNGLYRK 358
Cdd:PTZ00265  1400 TIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSVQDGVYKK 1460
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 122-349 3.87e-57

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: 186.00  E-value: 3.87e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYParPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 201
Cdd:COG1122     1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPV--LFSCSVAENIAYGADNL---SSVTAQQVERAAEVANAAEFIRSFPQgfdtvvgekgiLLSGGQKQRIAIAR 276
Cdd:COG1122    79 LVFQNPDdqLFAPTVEEDVAFGPENLglpREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAG 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907190441 277 ALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEELL 349
Cdd:COG1122   148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVF 222
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 144-363 2.36e-56

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 193.91  E-value: 2.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 144 SLSIPSGSVTALVGPSGSGKSTVVSLLLRlYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGAD 223
Cdd:PRK11174  370 NFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNP 448

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 224 NLSsvtAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQ 303
Cdd:PRK11174  449 DAS---DEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 304 EALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGLYRKLMNKQ 363
Cdd:PRK11174  526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQ 585
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 122-358 3.05e-56

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: 192.04  E-value: 3.05e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARP--EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV---WL 196
Cdd:COG1123   261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrEL 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 197 RSKIGTVSQEPvlFSC-----SVAENIAYGADNLSSVTAQQV-ERAAEVANA----AEFIRSFPQGFdtvvgekgillSG 266
Cdd:COG1123   341 RRRVQMVFQDP--YSSlnprmTVGDIIAEPLRLHGLLSRAERrERVAELLERvglpPDLADRYPHEL-----------SG 407

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 267 GQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHG 343
Cdd:COG1123   408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487

                         250
                  ....*....|....*
gi 1907190441 344 THEELLLKPNGLYRK 358
Cdd:COG1123   488 PTEEVFANPQHPYTR 502
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
122-320 3.34e-55

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 180.40  E-value: 3.34e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 201
Cdd:COG4619     1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLFSCSVAENIAYgadnlssvTAQQVERAAEVANAAEFIRSFpqGFDTVVGEKGI-LLSGGQKQRIAIARALLK 280
Cdd:COG4619    78 YVPQEPALWGGTVRDNLPF--------PFQLRERKFDRERALELLERL--GLPPDILDKPVeRLSGGERQRLALIRALLL 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907190441 281 NPKILLLDEATSALDAENEHLVQEALDRLM--EGRTVLIIAH 320
Cdd:COG4619   148 QPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSH 189
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 122-339 7.79e-54

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: 175.48  E-value: 7.79e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPEVsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 201
Cdd:cd03246     1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLFSCSVAENIaygadnlssvtaqqveraaevanaaefirsfpqgfdtvvgekgilLSGGQKQRIAIARALLKN 281
Cdd:cd03246    80 YLPQDDELFSGSIAENI---------------------------------------------LSGGQRQRLGLARALYGN 114

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 282 PKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTIKNANFVAVLDHGKI 339
Cdd:cd03246   115 PRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 122-348 9.31e-53

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: 174.68  E-value: 9.31e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYD-----PNSGTVSLDGHDIRQL--NPV 194
Cdd:cd03260     1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLdvDVL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 195 WLRSKIGTVSQEPVLFSCSVAENIAYG--------ADNLSSVTAQQVERAA---EVANAAefirsfpqgfdtvvgeKGIL 263
Cdd:cd03260    78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiklKEELDERVEEALRKAAlwdEVKDRL----------------HALG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 264 LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEH 342
Cdd:cd03260   142 LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEF 221


                  ....*.
gi 1907190441 343 GTHEEL 348
Cdd:cd03260   222 GPTEQI 227
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 122-343 9.16e-52

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: 172.31  E-value: 9.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---R 197
Cdd:cd03257     2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 198 SKIGTVSQEPvlFSC-----SVAENIA------YGADNLSSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSG 266
Cdd:cd03257    82 KEIQMVFQDP--MSSlnprmTIGEQIAeplrihGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHE-----------LSG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 267 GQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHG 343
Cdd:cd03257   149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
122-349 1.12e-51

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 172.17  E-value: 1.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPEVsvfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlNPVWLRSKIG 201
Cdd:COG1131     1 IEVRGLTKRYGDKTAL---DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLF-SCSVAENIAYGADnLSSVTAQQVERAAEvanaaEFIRSFpqGFDTVVGEKGILLSGGQKQRIAIARALLK 280
Cdd:COG1131    77 YVPQEPALYpDLTVRENLRFFAR-LYGLPRKEARERID-----ELLELF--GLTDAADRKVGTLSGGMKQRLGLALALLH 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907190441 281 NPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEELL 349
Cdd:COG1131   149 DPELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELK 219
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
122-352 1.21e-51

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 175.27  E-value: 1.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---R 197
Cdd:COG1135     2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 198 SKIGTVSQEPVLF-SCSVAENIAY-----GADnlssvTAQQVERAAEVANA---AEFIRSFP-QgfdtvvgekgilLSGG 267
Cdd:COG1135    82 RKIGMIFQHFNLLsSRTVAENVALpleiaGVP-----KAEIRKRVAELLELvglSDKADAYPsQ------------LSGG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 268 QKQRIAIARALLKNPKILLLDEATSALDAENEH----LVQEALDRLmeGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEH 342
Cdd:COG1135   145 QKQRVGIARALANNPKVLLCDEATSALDPETTRsildLLKDINREL--GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQ 222

                         250
                  ....*....|
gi 1907190441 343 GTHEELLLKP 352
Cdd:COG1135   223 GPVLDVFANP 232
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 121-349 4.66e-51

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: 170.99  E-value: 4.66e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKI 200
Cdd:COG1120     1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQEPVL-FSCSVAENIAYG----ADNLSSVTA---QQVERAAEVANAAEFI-RSFPQgfdtvvgekgilLSGGQKQR 271
Cdd:COG1120    78 AYVPQEPPApFGLTVRELVALGryphLGLFGRPSAedrEAVEEALERTGLEHLAdRPVDE------------LSGGERQR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 272 IAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEEL 348
Cdd:COG1120   146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225


                  .
gi 1907190441 349 L 349
Cdd:COG1120   226 L 226
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 122-352 5.28e-51

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: 170.45  E-value: 5.28e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---R 197
Cdd:cd03258     2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 198 SKIGTVSQEPVLFSC-SVAENIAYGADNLSSVTAQQVERAAEV---ANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIA 273
Cdd:cd03258    82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELlelVGLEDKADAYPAQ-----------LSGGQKQRVG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 274 IARALLKNPKILLLDEATSALDAENehlVQEALDRLME-----GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEE 347
Cdd:cd03258   151 IARALANNPKVLLCDEATSALDPET---TQSILALLRDinrelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227


                  ....*
gi 1907190441 348 LLLKP 352
Cdd:cd03258   228 VFANP 232
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 4-322 3.35e-50

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: 176.40  E-value: 3.35e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   4 VEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYS 83
Cdd:TIGR02868 216 LAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQ 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  84 ELMKGLGAGGRLWELLE-----RQPRLPFNEGMVLDEKTfqgaLEFRNVHFTYPARPEVsvFQDFSLSIPSGSVTALVGP 158
Cdd:TIGR02868 296 QLTRVRAAAERIVEVLDaagpvAEGSAPAAGAVGLGKPT----LELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGP 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 159 SGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAE 238
Cdd:TIGR02868 370 SGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPD---ATDEELWAALE 446

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 239 VANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLII 318
Cdd:TIGR02868 447 RVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLI 526


                  ....
gi 1907190441 319 AHRL 322
Cdd:TIGR02868 527 THHL 530
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 121-355 3.04e-49

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: 173.55  E-value: 3.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARPEVSVfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN---SGTVSLDGHDIRQLNPVWLR 197
Cdd:COG1123     4 LLEVRDLSVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 198 SKIGTVSQEP--VLFSCSVAENIAYGADNLSSVTAQQVERAAEVANA---AEFIRSFPQgfdtvvgekgiLLSGGQKQRI 272
Cdd:COG1123    83 RRIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAvglERRLDRYPH-----------QLSGGQRQRV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 273 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 349
Cdd:COG1123   152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEIL 231


                  ....*.
gi 1907190441 350 LKPNGL 355
Cdd:COG1123   232 AAPQAL 237
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 123-338 7.19e-49

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: 164.18  E-value: 7.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 123 EFRNVHFTYPARPEVsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGT 202
Cdd:cd03225     1 ELKNLSFSYPDGARP-ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 203 VSQEP--VLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAaefirsfpqgfdtvVGEKGIL------LSGGQKQRIAI 274
Cdd:cd03225    80 VFQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALEL--------------VGLEGLRdrspftLSGGQKQRVAI 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 275 ARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHGK 338
Cdd:cd03225   146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 122-338 1.41e-48

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: 1.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPEVSVF--QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdirqlnpvwlrsK 199
Cdd:cd03250     1 ISVEDASFTWDSGEQETSFtlKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQEPVLFSCSVAENIAYGA--DNlssvtaqqvERAAEVANAAEF---IRSFPQGFDTVVGEKGILLSGGQKQRIAI 274
Cdd:cd03250    68 IAYVSQEPWIQNGTIRENILFGKpfDE---------ERYEKVIKACALepdLEILPDGDLTEIGEKGINLSGGQKQRISL 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 275 ARALLKNPKILLLDEATSALDAE-NEHLVQEAL-DRLMEGRTVLIIAHRLSTIKNANFVAVLDHGK 338
Cdd:cd03250   139 ARAVYSDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 111-352 2.46e-47

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 161.74  E-value: 2.46e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 111 MVLDEKTFQGALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYD--PN---SGTVSLDG 185
Cdd:COG1117     1 MTAPASTLEPKIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 186 HDI--RQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGA----DNLSSVTAQQVE----RAA---EVANaaefirsfpqg 252
Cdd:COG1117    78 EDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgIKSKSELDEIVEeslrKAAlwdEVKD----------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 253 fdtVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAH------RLStik 326
Cdd:COG1117   147 ---RLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS--- 220

                         250       260
                  ....*....|....*....|....*.
gi 1907190441 327 naNFVAVLDHGKICEHGTHEELLLKP 352
Cdd:COG1117   221 --DYTAFFYLGELVEFGPTEQIFTNP 244
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 121-349 3.33e-47

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: 160.53  E-value: 3.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP---VWLR 197
Cdd:COG1127     5 MIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 198 SKIGTVSQEPVLF-SCSVAENIAYGADNLSSVTAQQV-ERAAEVANA---AEFIRSFPqgfdtvvGEkgilLSGGQKQRI 272
Cdd:COG1127    82 RRIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIrELVLEKLELvglPGAADKMP-------SE----LSGGMRKRV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 273 AIARALLKNPKILLLDEATSALD----AENEHLVQEALDRLmeGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEE 347
Cdd:COG1127   151 ALARALALDPEILLYDEPTAGLDpitsAVIDELIRELRDEL--GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228


                  ..
gi 1907190441 348 LL 349
Cdd:COG1127   229 LL 230
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 123-338 4.35e-47

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: 157.79  E-value: 4.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 123 EFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGT 202
Cdd:cd00267     1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 203 VSQepvlfscsvaeniaygadnlssvtaqqveraaevanaaefirsfpqgfdtvvgekgilLSGGQKQRIAIARALLKNP 282
Cdd:cd00267    78 VPQ----------------------------------------------------------LSGGQRQRVALARALLLNP 99

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441 283 KILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKNA-NFVAVLDHGK 338
Cdd:cd00267   100 DLLLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 122-352 4.57e-47

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 160.16  E-value: 4.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLR----LYDPNSGTVSLDGHDI----RQLNP 193
Cdd:COG1126     2 IEIENLHKSFGDLE---VLKGISLDVEKGEVVVIIGPSGSGKST----LLRcinlLEEPDSGTITVDGEDLtdskKDINK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 194 vwLRSKIGTVSQEPVLFS-CSVAENIAYGadnlsSVTAQQVERAAEVANA---------AEFIRSFP-Qgfdtvvgekgi 262
Cdd:COG1126    75 --LRRKVGMVFQQFNLFPhLTVLENVTLA-----PIKVKKMSKAEAEERAmellervglADKADAYPaQ----------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 263 lLSGGQKQRIAIARALLKNPKILLLDEATSALDAEnehLVQEALDrLM-----EGRTVLIIAHRLSTIKN-ANFVAVLDH 336
Cdd:COG1126   137 -LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLD-VMrdlakEGMTMVVVTHEMGFAREvADRVVFMDG 211

                         250
                  ....*....|....*.
gi 1907190441 337 GKICEHGTHEELLLKP 352
Cdd:COG1126   212 GRIVEEGPPEEFFENP 227
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 122-349 5.45e-47

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


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 160.41  E-value: 5.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlNPVWLRSKIG 201
Cdd:COG4555     2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLFS-CSVAENIAYGAdnlssvTAQQVERAAEVANAAEFIRSF--PQGFDTVVGEkgilLSGGQKQRIAIARAL 278
Cdd:COG4555    78 VLPDERGLYDrLTVRENIRYFA------ELYGLFDEELKKRIEELIELLglEEFLDRRVGE----LSTGMKKKVALARAL 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907190441 279 LKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 349
Cdd:COG4555   148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELR 220
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 121-349 5.89e-47

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 160.25  E-value: 5.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnpvwlRSKI 200
Cdd:COG1121     6 AIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQEPVL---FSCSVAENIAYGADN-------LSSVTAQQVERAAEVANAAEFIrsfpqgfDTVVGEkgilLSGGQKQ 270
Cdd:COG1121    78 GYVPQRAEVdwdFPITVRDVVLMGRYGrrglfrrPSRADREAVDEALERVGLEDLA-------DRPIGE----LSGGQQQ 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 271 RIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTI-KNANFVAVLDHGKICeHGTHEEL 348
Cdd:COG1121   147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVrEYFDRVLLLNRGLVA-HGPPEEV 225


                  .
gi 1907190441 349 L 349
Cdd:COG1121   226 L 226
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 121-320 8.32e-47

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 160.26  E-value: 8.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPvwlrsK 199
Cdd:COG1116     7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-----D 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQEPVLFS-CSVAENIAYGADNLSSVTAQQVERAAEVANA---AEFIRSFP-QgfdtvvgekgilLSGGQKQRIAI 274
Cdd:COG1116    82 RGVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELLELvglAGFEDAYPhQ------------LSGGMRQRVAI 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907190441 275 ARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAH 320
Cdd:COG1116   150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTH 197
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 122-352 1.05e-46

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: 159.39  E-value: 1.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPA-RPEVSvfqDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKI 200
Cdd:cd03295     1 IEFENVTKRYGGgKKAVN---NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQEPVLFS-CSVAENIAYGADNLSSVTAQQVERAAEV-----ANAAEFIRSFPqgfdtvvGEkgilLSGGQKQRIAI 274
Cdd:cd03295    78 GYVIQQIGLFPhMTVEENIALVPKLLKWPKEKIRERADELlalvgLDPAEFADRYP-------HE----LSGGQQQRVGV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 275 ARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRL-STIKNANFVAVLDHGKICEHGTHEELLLK 351
Cdd:cd03295   147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226


                  .
gi 1907190441 352 P 352
Cdd:cd03295   227 P 227
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
121-339 2.14e-46

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 158.28  E-value: 2.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPA-RPEVSVFQDFSLSIPSGSVTALVGPSGSGKST---VVSLLLRlydPNSGTVSLDGHDIRQLNP--- 193
Cdd:COG1136     4 LLELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSErel 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 194 -VWLRSKIGTVSQE----PVLfscSVAENIAYGADnLSSVTAQQV-ERAAEVANA---AEFIRSFPqgfdtvvGEkgilL 264
Cdd:COG1136    81 aRLRRRHIGFVFQFfnllPEL---TALENVALPLL-LAGVSRKERrERARELLERvglGDRLDHRP-------SQ----L 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190441 265 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKNANFVAVLDHGKI 339
Cdd:COG1136   146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRI 222
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 122-355 2.69e-46

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: 159.13  E-value: 2.69e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVW-LRSKI 200
Cdd:TIGR04520   1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQEP--VLFSCSVAENIAYGADNL---SSVTAQQVERAAEVANAAEFIRSFPQgfdtvvgekgiLLSGGQKQRIAIA 275
Cdd:TIGR04520  80 GMVFQNPdnQFVGATVEDDVAFGLENLgvpREEMRKRVDEALKLVGMEDFRDREPH-----------LLSGGQKQRVAIA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 276 RALLKNPKILLLDEATSALDAENEHLVQEALDRLM--EGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELL---- 349
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFsqve 228


                  ....*..
gi 1907190441 350 -LKPNGL 355
Cdd:TIGR04520 229 lLKEIGL 235
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 122-343 8.73e-46

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: 155.16  E-value: 8.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPEVsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwLRSKIG 201
Cdd:cd03247     1 LSINNVSFSYPEQEQQ-VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLFSCSVAENIaygadnlssvtaqqveraaevanaaefirsfpqgfdtvvgekGILLSGGQKQRIAIARALLKN 281
Cdd:cd03247    79 VLNQRPYLFDTTLRNNL------------------------------------------GRRFSGGERQRLALARILLQD 116

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907190441 282 PKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHG 343
Cdd:cd03247   117 APIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 122-320 1.06e-45

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: 156.09  E-value: 1.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYP-ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPvwlrsKI 200
Cdd:cd03293     1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQEPVLFS-CSVAENIAYGADNLSSVTAQQVERAAEVANA---AEFIRSFPQGfdtvvgekgilLSGGQKQRIAIAR 276
Cdd:cd03293    76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEELLELvglSGFENAYPHQ-----------LSGGMRQRVALAR 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907190441 277 ALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAH 320
Cdd:cd03293   145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTH 190
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 120-344 3.16e-45

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: 154.49  E-value: 3.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 120 GALEFRNVHFTYpaRPEV-SVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRS 198
Cdd:cd03369     5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 199 KIGTVSQEPVLFSCSVAENIaygaDNLSSVTAQQVERAAEVAnaaefirsfpqgfdtvvgEKGILLSGGQKQRIAIARAL 278
Cdd:cd03369    83 SLTIIPQDPTLFSGTIRSNL----DPFDEYSDEEIYGALRVS------------------EGGLNLSQGQRQLLCLARAL 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 279 LKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGT 344
Cdd:cd03369   141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 121-353 8.29e-45

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 157.95  E-value: 8.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLR----LYDPNSGTVSLDGHDIRQLnPVWL 196
Cdd:COG3842     5 ALELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTT----LLRmiagFETPDSGRILLDGRDVTGL-PPEK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 197 RsKIGTVSQEPVLFS-CSVAENIAYG--ADNLS-SVTAQQVERAAEVANAAEFIRSFPQgfdtvvgekgiLLSGGQKQRI 272
Cdd:COG3842    77 R-NVGMVFQDYALFPhLTVAENVAFGlrMRGVPkAEIRARVAELLELVGLEGLADRYPH-----------QLSGGQQQRV 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 273 AIARALLKNPKILLLDEATSALDAEN-EHLVQEaLDRLME--GRTVLIIAHRLS---TIknANFVAVLDHGKICEHGTHE 346
Cdd:COG3842   145 ALARALAPEPRVLLLDEPLSALDAKLrEEMREE-LRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPE 221


                  ....*..
gi 1907190441 347 ELLLKPN 353
Cdd:COG3842   222 EIYERPA 228
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 122-339 1.99e-44

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: 151.40  E-value: 1.99e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlNPVWLRSKIG 201
Cdd:cd03230     1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLFscsvaeniaygaDNLSsvtaqqveraaevanAAEFIRsfpqgfdtvvgekgilLSGGQKQRIAIARALLKN 281
Cdd:cd03230    77 YLPEEPSLY------------ENLT---------------VRENLK----------------LSGGMKQRLALAQALLHD 113

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 282 PKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHGKI 339
Cdd:cd03230   114 PELLILDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 140-292 2.73e-44

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: 150.11  E-value: 2.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 140 FQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFS-CSVAENI 218
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190441 219 AYGA---DNLSSVTAQQVERAAEVANAAEFIrsfpqgfDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATS 292
Cdd:pfam00005  81 RLGLllkGLSKREKDARAEEALEKLGLGDLA-------DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 122-343 8.86e-44

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: 150.75  E-value: 8.86e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnPVWLRsKIG 201
Cdd:cd03259     1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV-PPERR-NIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLF-SCSVAENIAYGADNLSSVTAQQVERAAEVA---NAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARA 277
Cdd:cd03259    76 MVFQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLelvGLEGLLNRYPHE-----------LSGGQQQRVALARA 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 278 LLKNPKILLLDEATSALDAE-NEHLVQEALDRLME-GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHG 343
Cdd:cd03259   145 LAREPSLLLLDEPLSALDAKlREELREELKELQRElGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 121-349 1.78e-43

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


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 151.11  E-value: 1.78e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARPE-VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSK 199
Cdd:COG1124     1 MLEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQEPVLfSC----SVAENIA-----YGADNlssvTAQQVERAAE-VANAAEFIRSFP-QgfdtvvgekgilLSGGQ 268
Cdd:COG1124    81 VQMVFQDPYA-SLhprhTVDRILAeplriHGLPD----REERIAELLEqVGLPPSFLDRYPhQ------------LSGGQ 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 269 KQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTH 345
Cdd:COG1124   144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTV 223


                  ....
gi 1907190441 346 EELL 349
Cdd:COG1124   224 ADLL 227
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 122-348 2.03e-43

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: 150.73  E-value: 2.03e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---RS 198
Cdd:cd03261     1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 199 KIGTVSQEPVLF-SCSVAENIAY-----GADNLSSVTAQQVERAAEVaNAAEFIRSFPqgfdtvvGEkgilLSGGQKQRI 272
Cdd:cd03261    78 RMGMLFQSGALFdSLTVFENVAFplrehTRLSEEEIREIVLEKLEAV-GLRGAEDLYP-------AE----LSGGMKKRV 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 273 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEEL 348
Cdd:cd03261   146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEEL 224
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 122-338 3.18e-43

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: 148.49  E-value: 3.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLN--PVWLRSK 199
Cdd:cd03229     1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQEPVLFS-CSVAENIAYGadnlssvtaqqveraaevanaaefirsfpqgfdtvvgekgilLSGGQKQRIAIARAL 278
Cdd:cd03229    78 IGMVFQDFALFPhLTVLENIALG------------------------------------------LSGGQQQRVALARAL 115

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907190441 279 LKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLS-TIKNANFVAVLDHGK 338
Cdd:cd03229   116 AMDPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 36-349 3.61e-43

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: 160.88  E-value: 3.61e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   36 GNLIVL-SVLYKgglLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRLWELLERQPRLPFNEGMVLD 114
Cdd:TIGR00957 1199 GNCIVLfAALFA---VISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAP 1275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  115 EKTF--QGALEFRNVHFTYpaRPEVS-VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQL 191
Cdd:TIGR00957 1276 PSGWppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI 1353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  192 NPVWLRSKIGTVSQEPVLFSCSVAENIaygaDNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQR 271
Cdd:TIGR00957 1354 GLHDLRFKITIIPQDPVLFSGSLRMNL----DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQL 1429

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441  272 IAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELL 349
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
 3-95 6.63e-43

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: 151.13  E-value: 6.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFY 82
Cdd:cd18573   202 EVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFY 281

                          90
                  ....*....|...
gi 1907190441  83 SELMKGLGAGGRL 95
Cdd:cd18573   282 SELMKGLGASSRL 294
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 142-353 1.91e-42

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: 148.25  E-value: 1.91e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 142 DFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwlRSKIGTVSQEPVLF-SCSVAENIAY 220
Cdd:cd03299    17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNIAY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 221 GadnLSSVTAQQVERAAEVANAAEFIrsfpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEH 300
Cdd:cd03299    95 G---LKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 301 LVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPN 353
Cdd:cd03299   167 KLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPK 222
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 122-320 5.61e-42

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: 146.48  E-value: 5.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPE-VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---- 196
Cdd:cd03255     1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 197 RSKIGTVSQE----PVLfscSVAENIAYGADNLSSVTAQQVERAAEVANA---AEFIRSFPQGfdtvvgekgilLSGGQK 269
Cdd:cd03255    81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEELLERvglGDRLNHYPSE-----------LSGGQQ 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907190441 270 QRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAH 320
Cdd:cd03255   147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTH 199
PLN03130 PLN03130
ABC transporter C family member; Provisional
 120-359 6.44e-42

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 157.21  E-value: 6.44e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  120 GALEFRNVHFTYpaRPEVS-VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRS 198
Cdd:PLN03130  1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  199 KIGTVSQEPVLFSCSVAENIaygaDNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARAL 278
Cdd:PLN03130  1314 VLGIIPQAPVLFSGTVRFNL----DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARAL 1389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  279 LKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGLYRK 358
Cdd:PLN03130  1390 LRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSK 1469


                   .
gi 1907190441  359 L 359
Cdd:PLN03130  1470 M 1470
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
122-347 8.12e-42

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 145.97  E-value: 8.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP---VWLRS 198
Cdd:COG2884     2 IRFENVSKRYPGGREA--LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreiPYLRR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 199 KIGTVSQE-PVLFSCSVAENIAY-----GADnlSSVTAQQVERAAEVANAAEFIRSFPqgfdtvvgekgILLSGGQKQRI 272
Cdd:COG2884    80 RIGVVFQDfRLLPDRTVYENVALplrvtGKS--RKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGEQQRV 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190441 273 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTIKNANF-VAVLDHGKICEHGTHEE 347
Cdd:COG2884   147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKrVLELEDGRLVRDEARGV 223
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 116-349 2.35e-41

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 146.29  E-value: 2.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 116 KTFQGALEFRNVHFTYPARpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVW 195
Cdd:PRK13632    2 KNKSVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 196 LRSKIGTVSQEP--VLFSCSVAENIAYGADNL---SSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQ 270
Cdd:PRK13632   81 IRKKIGIIFQNPdnQFIGATVEDDIAFGLENKkvpPKKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 271 RIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGR--TVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEEL 348
Cdd:PRK13632  150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229


                  .
gi 1907190441 349 L 349
Cdd:PRK13632  230 L 230
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 122-352 3.68e-41

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: 147.12  E-value: 3.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN---SGTVSLDGHDIRQLNPVWLR 197
Cdd:COG0444     2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 198 S----KIGTVSQE------PVLfscSVAENIAYGADNLSSVTAQQV-ERAAEV------ANAAEFIRSFP-Qgfdtvvge 259
Cdd:COG0444    82 KirgrEIQMIFQDpmtslnPVM---TVGDQIAEPLRIHGGLSKAEArERAIELlervglPDPERRLDRYPhE-------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 260 kgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAenehLVQ-EALDRLME-----GRTVLIIAHRLSTIKN-ANFVA 332
Cdd:COG0444   151 ----LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNLLKDlqrelGLAILFITHDLGVVAEiADRVA 222

                         250       260
                  ....*....|....*....|
gi 1907190441 333 VLDHGKICEHGTHEELLLKP 352
Cdd:COG0444   223 VMYAGRIVEEGPVEELFENP 242
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
122-349 9.22e-41

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 143.74  E-value: 9.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsvfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwlRSKIG 201
Cdd:COG3840     2 LRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLFS-CSVAENIAYGAD---NLSSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARA 277
Cdd:COG3840    75 MLFQENNLFPhLTVAQNIGLGLRpglKLTAEQRAQVEQALERVGLAGLLDRLPGQ-----------LSGGQRQRVALARC 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190441 278 LLKNPKILLLDEATSALD----AENEHLVQEALDRLmeGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 349
Cdd:COG3840   144 LVRKRPILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 123-339 4.54e-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: 140.26  E-value: 4.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 123 EFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGT 202
Cdd:cd03214     1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 203 VSQepvlfscsvaeniaygadnlssvtaqqverAAEVANAAEFIRsfpQGFDTvvgekgilLSGGQKQRIAIARALLKNP 282
Cdd:cd03214    78 VPQ------------------------------ALELLGLAHLAD---RPFNE--------LSGGERQRVLLARALAQEP 116

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 283 KILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLS-TIKNANFVAVLDHGKI 339
Cdd:cd03214   117 PILLLDEPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRI 176
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 121-339 1.34e-39

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 140.96  E-value: 1.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---R 197
Cdd:COG3638     2 MLELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 198 SKIGTVSQEPVLFS-CSVAENIAYGADN--------LSSVTAQQVERAAEVanaaefirsfpqgFDTVvgekGIL----- 263
Cdd:COG3638    80 RRIGMIFQQFNLVPrLSVLTNVLAGRLGrtstwrslLGLFPPEDRERALEA-------------LERV----GLAdkayq 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 264 ----LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDH 336
Cdd:COG3638   143 radqLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRD 222


                  ...
gi 1907190441 337 GKI 339
Cdd:COG3638   223 GRV 225
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 122-348 3.66e-39

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: 139.63  E-value: 3.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPArpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---RS 198
Cdd:cd03256     1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 199 KIGTVSQEPVLFS-CSVAENIAYGADN--------LSSVTAQQVERAAEVANAAEFIRSFPQGFDTvvgekgilLSGGQK 269
Cdd:cd03256    79 QIGMIFQQFNLIErLSVLENVLSGRLGrrstwrslFGLFPKEEKQRALAALERVGLLDKAYQRADQ--------LSGGQQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 270 QRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLSTIK-NANFVAVLDHGKICEHGTHE 346
Cdd:cd03256   151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230


                  ..
gi 1907190441 347 EL 348
Cdd:cd03256   231 EL 232
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 122-352 4.43e-39

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 142.59  E-value: 4.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLR----LYDPNSGTVSLDGHDIrqlnPVWL- 196
Cdd:COG1118     3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTT----LLRiiagLETPDSGRIVLNGRDL----FTNLp 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 197 --RSKIGTVSQEPVLF-SCSVAENIAYGADNLSSVTAQQVERAAE----VaNAAEFIRSFP-QgfdtvvgekgilLSGGQ 268
Cdd:COG1118    72 prERRVGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARVEEllelV-QLEGLADRYPsQ------------LSGGQ 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 269 KQRIAIARALLKNPKILLLDEATSALDA----ENEHLVQEALDRLmeGRTVLIIAH------RLstiknANFVAVLDHGK 338
Cdd:COG1118   139 RQRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDEL--GGTTVFVTHdqeealEL-----ADRVVVMNQGR 211

                         250
                  ....*....|....
gi 1907190441 339 ICEHGTHEELLLKP 352
Cdd:COG1118   212 IEQVGTPDEVYDRP 225
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 123-352 5.07e-39

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 142.25  E-value: 5.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 123 EFRNVHFTYP-ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRS--- 198
Cdd:PRK11153    3 ELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarr 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 199 KIGTVSQE-PVLFSCSVAENIAYgADNLSSVTAQQVERAA----EVANAAEFIRSFP-QgfdtvvgekgilLSGGQKQRI 272
Cdd:PRK11153   83 QIGMIFQHfNLLSSRTVFDNVAL-PLELAGTPKAEIKARVtellELVGLSDKADRYPaQ------------LSGGQKQRV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 273 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 349
Cdd:PRK11153  150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEVF 229


                  ...
gi 1907190441 350 LKP 352
Cdd:PRK11153  230 SHP 232
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 122-339 5.63e-39

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: 138.43  E-value: 5.63e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI----RQLNPvwLR 197
Cdd:cd03262     1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkKNINE--LR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 198 SKIGTVSQEPVLFS-CSVAENIAygadnLSSVTAQQVERAAEVANA---------AEFIRSFPQGfdtvvgekgilLSGG 267
Cdd:cd03262    76 QKVGMVFQQFNLFPhLTVLENIT-----LAPIKVKGMSKAEAEERAlellekvglADKADAYPAQ-----------LSGG 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441 268 QKQRIAIARALLKNPKILLLDEATSALDAEnehLVQEALDrLM-----EGRTVLIIAHRLSTIKN-ANFVAVLDHGKI 339
Cdd:cd03262   140 QQQRVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLD-VMkdlaeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 123-343 6.58e-39

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: 138.05  E-value: 6.58e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 123 EFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnpvwlRSKIGT 202
Cdd:cd03235     1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 203 VSQEPVL---FSCSVAENIAYGAD-------NLSSVTAQQVERAAEVANAAEFI-RSFpqgfdtvvGEkgilLSGGQKQR 271
Cdd:cd03235    73 VPQRRSIdrdFPISVRDVVLMGLYghkglfrRLSKADKAKVDEALERVGLSELAdRQI--------GE----LSGGQQQR 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907190441 272 IAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTI-KNANFVAVLDHGKICeHG 343
Cdd:cd03235   141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRTVVA-SG 213
PLN03232 PLN03232
ABC transporter C family member; Provisional
 120-361 4.77e-38

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 145.89  E-value: 4.77e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  120 GALEFRNVHFTYpaRPEVS-VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRS 198
Cdd:PLN03232  1233 GSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR 1310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  199 KIGTVSQEPVLFSCSVAENIaygaDNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARAL 278
Cdd:PLN03232  1311 VLSIIPQSPVLFSGTVRFNI----DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARAL 1386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  279 LKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGLYRK 358
Cdd:PLN03232  1387 LRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFR 1466


                   ...
gi 1907190441  359 LMN 361
Cdd:PLN03232  1467 MVH 1469
cbiO PRK13640
energy-coupling factor transporter ATPase;
121-362 4.80e-38

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 138.01  E-value: 4.80e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARPEvSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLL--LRLYDPNSGT-VSLDGHDIRQLNpVW-L 196
Cdd:PRK13640    5 IVEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLIngLLLPDDNPNSkITVDGITLTAKT-VWdI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 197 RSKIGTVSQEP--VLFSCSVAENIAYGADNlSSVTAQQ----VERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQ 270
Cdd:PRK13640   83 REKVGIVFQNPdnQFVGATVGDDVAFGLEN-RAVPRPEmikiVRDVLADVGMLDYIDSEPAN-----------LSGGQKQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 271 RIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEEL 348
Cdd:PRK13640  151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230

                         250       260
                  ....*....|....*....|...
gi 1907190441 349 -----LLKPNGL----YRKLMNK 362
Cdd:PRK13640  231 fskveMLKEIGLdipfVYKLKNK 253
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 126-339 1.91e-37

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: 133.92  E-value: 1.91e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 126 NVHFTYPARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdiRQLNPVWLRSKIGTVSQ 205
Cdd:cd03226     4 NISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 206 EP--VLFSCSVAENIAYGADNLSSVtAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALLKNPK 283
Cdd:cd03226    79 DVdyQLFTDSVREELLLGLKELDAG-NEQAETVLKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLSGKD 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441 284 ILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHGKI 339
Cdd:cd03226   147 LLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 147-360 3.48e-37

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: 135.04  E-value: 3.48e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 147 IPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIaygaDNLS 226
Cdd:cd03288    44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL----DPEC 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 227 SVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEAL 306
Cdd:cd03288   120 KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV 199

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907190441 307 DRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGLYRKLM 360
Cdd:cd03288   200 MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 141-352 4.44e-37

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: 135.08  E-value: 4.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 141 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL----RSKIGTVSQEPVLF-SCSVA 215
Cdd:cd03294    41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 216 ENIAYGADnLSSVTAQQ-VERAAEVANA---AEFIRSFPqgfdtvvGEkgilLSGGQKQRIAIARALLKNPKILLLDEAT 291
Cdd:cd03294   121 ENVAFGLE-VQGVPRAErEERAAEALELvglEGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEAF 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907190441 292 SALDAENEHLVQEALDRL--MEGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELLLKP 352
Cdd:cd03294   189 SALDPLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
122-348 2.26e-36

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 133.60  E-value: 2.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYP--ARPEVsvfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdiRQLNP--VW-L 196
Cdd:PRK13635    6 IRVEHISFRYPdaATYAL---KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEetVWdV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 197 RSKIGTVSQEP--VLFSCSVAENIAYGADNLSSVTAQQVER---AAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQR 271
Cdd:PRK13635   80 RRQVGMVFQNPdnQFVGATVQDDVAFGLENIGVPREEMVERvdqALRQVGMEDFLNREPHR-----------LSGGQKQR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 272 IAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEEL 348
Cdd:PRK13635  149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 144-348 3.36e-36

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 134.09  E-value: 3.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 144 SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP---VWLRSKIGTVSQEPvlFSC-----SVA 215
Cdd:COG4608    38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGrelRPLRRRMQMVFQDP--YASlnprmTVG 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 216 ENIAYGADNLSSVTAQQV-ERAAE----VANAAEFIRSFPQGFdtvvgekgillSGGQKQRIAIARALLKNPKILLLDEA 290
Cdd:COG4608   116 DIIAEPLRIHGLASKAERrERVAEllelVGLRPEHADRYPHEF-----------SGGQRQRIGIARALALNPKLIVCDEP 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907190441 291 TSALD----AENEHLVQEALDRLmeGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEEL 348
Cdd:COG4608   185 VSALDvsiqAQVLNLLEDLQDEL--GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 120-356 1.31e-35

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 133.27  E-value: 1.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 120 GALEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLR----LYDPNSGTVSLDGHDIRQLNPVw 195
Cdd:COG3839     2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKST----LLRmiagLEDPTSGEILIGGRDVTDLPPK- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 196 lRSKIGTVSQEPVLF-SCSVAENIAYGadnLS------SVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQ 268
Cdd:COG3839    74 -DRNIAMVFQSYALYpHMTVYENIAFP---LKlrkvpkAEIDRRVREAAELLGLEDLLDRKPKQ-----------LSGGQ 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 269 KQRIAIARALLKNPKILLLDEATSALDAE-NEHLVQEaLDRLME--GRTVLI----------IAHRlstiknanfVAVLD 335
Cdd:COG3839   139 RQRVALGRALVREPKVFLLDEPLSNLDAKlRVEMRAE-IKRLHRrlGTTTIYvthdqveamtLADR---------IAVMN 208

                         250       260
                  ....*....|....*....|.
gi 1907190441 336 HGKICEHGTHEELLLKPNGLY 356
Cdd:COG3839   209 DGRIQQVGTPEELYDRPANLF 229
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 122-353 1.05e-34

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: 127.74  E-value: 1.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPvwLRSKIG 201
Cdd:cd03300     1 IELENVSKFYGGFV---ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP--HKRPVN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLFS-CSVAENIAYG---ADNLSSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARA 277
Cdd:cd03300    76 TVFQNYALFPhLTVFENIAFGlrlKKLPKAEIKERVAEALDLVQLEGYANRKPSQ-----------LSGGQQQRVAIARA 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 278 LLKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELLLKPN 353
Cdd:cd03300   145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 137-347 5.50e-34

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: 126.01  E-value: 5.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 137 VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwLRSKIGTVS--QEPVLF-SCS 213
Cdd:cd03219    13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 214 VAENIAYGADNLSSVTAQQV----ERAAEVANAAEFIRSFpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDE 289
Cdd:cd03219    92 VLENVMVAAQARTGSGLLLArarrEEREARERAEELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907190441 290 ATSAL-DAENEHLVqEALDRL-MEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEE 347
Cdd:cd03219   170 PAAGLnPEETEELA-ELIRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 122-370 8.67e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 126.40  E-value: 8.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPArPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 201
Cdd:PRK13648    8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEP--VLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAEFIR---SFPQGfdtvvgekgilLSGGQKQRIAIAR 276
Cdd:PRK13648   87 IVFQNPdnQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLEradYEPNA-----------LSGGQKQRVAIAG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 277 ALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIA--HRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNG 354
Cdd:PRK13648  156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235

                         250       260
                  ....*....|....*....|....*....
gi 1907190441 355 LY-------------RKLMNKQSFLSYNG 370
Cdd:PRK13648  236 LTrigldlpfpikinQMLGHQTSFLTYEG 264
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 122-343 1.02e-33

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: 124.23  E-value: 1.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARpevSVFQDFSLSIPSGsVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlNPVWLRSKIG 201
Cdd:cd03264     1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLF-SCSVAENIAYGAdNLSSVTA----QQVERAAEVANAAEFIrsfpqgfDTVVGEkgilLSGGQKQRIAIAR 276
Cdd:cd03264    76 YLPQEFGVYpNFTVREFLDYIA-WLKGIPSkevkARVDEVLELVNLGDRA-------KKKIGS----LSGGMRRRVGIAQ 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441 277 ALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHG 343
Cdd:cd03264   144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 122-339 2.00e-33

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


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 123.67  E-value: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYParPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLN----PvWLR 197
Cdd:cd03292     1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraiP-YLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 198 SKIGTVSQE-PVLFSCSVAENIAYG---ADNLSSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIA 273
Cdd:cd03292    78 RKIGVVFQDfRLLPDRNVYENVAFAlevTGVPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVA 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441 274 IARALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTIKNANF-VAVLDHGKI 339
Cdd:cd03292   147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
121-322 5.19e-33

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 128.60  E-value: 5.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV-WLRSK 199
Cdd:COG1129     4 LLEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdAQAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQEPVLFSC-SVAENIAYGADNLSSVTaqqVERAAEVANAAEFIRSFpqGFD----TVVGEkgilLSGGQKQRIAI 274
Cdd:COG1129    81 IAIIHQELNLVPNlSVAENIFLGREPRRGGL---IDWRAMRRRARELLARL--GLDidpdTPVGD----LSVAQQQLVEI 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907190441 275 ARALLKNPKILLLDEATSAL-DAENEHLVqEALDRLM-EGRTVLIIAHRL 322
Cdd:COG1129   152 ARALSRDARVLILDEPTASLtEREVERLF-RIIRRLKaQGVAIIYISHRL 200
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 122-346 5.81e-33

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 122.90  E-value: 5.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 201
Cdd:PRK10247    8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLFSCSVAENIAYGAdnlsSVTAQQVERAAEVANAAEFirsfpqGFDTVVGEKGI-LLSGGQKQRIAIARALLK 280
Cdd:PRK10247   85 YCAQTPTLFGDTVYDNLIFPW----QIRNQQPDPAIFLDDLERF------ALPDTILTKNIaELSGGEKQRISLIRNLQF 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 281 NPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKNANFVAVLD-HGKICEHGTHE 346
Cdd:PRK10247  155 MPKVLLLDEITSALDESNKHNVNEIIHRYVReqNIAVLWVTHDKDEINHADKVITLQpHAGEMQEARYE 223
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 122-349 6.08e-33

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: 122.54  E-value: 6.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP-VWLRSKI 200
Cdd:cd03224     1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQEPVLF-SCSVAENIAYGADNLS-SVTAQQVERAAEVanaaefirsFPQgFDTVVGEKGILLSGGQKQRIAIARAL 278
Cdd:cd03224    78 GYVPEGRRIFpELTVEENLLLGAYARRrAKRKARLERVYEL---------FPR-LKERRKQLAGTLSGGEQQMLAIARAL 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 279 LKNPKILLLDEATSALdAENehLVQEALDRLM----EGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 349
Cdd:cd03224   148 MSRPKLLLLDEPSEGL-APK--IVEEIFEAIRelrdEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
122-352 1.09e-32

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 122.51  E-value: 1.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNV--HFTyparpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIR--QLNPVWLR 197
Cdd:PRK09493    2 IEFKNVskHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 198 SKIGTVSQEPVLFSCSVA-ENIAYGADNLSSVTAQQVERAAEVANA----AEFIRSFPqgfdtvvGEkgilLSGGQKQRI 272
Cdd:PRK09493   77 QEAGMVFQQFYLFPHLTAlENVMFGPLRVRGASKEEAEKQARELLAkvglAERAHHYP-------SE----LSGGQQQRV 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 273 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELLL 350
Cdd:PRK09493  146 AIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIK 225


                  ..
gi 1907190441 351 KP 352
Cdd:PRK09493  226 NP 227
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 121-353 2.24e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 122.54  E-value: 2.24e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKI 200
Cdd:PRK13647    4 IIEVEDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQEP--VLFSCSVAENIAYGADNLsSVTAQQVERAAEVANAA----EFIRSFPQGfdtvvgekgilLSGGQKQRIAI 274
Cdd:PRK13647   82 GLVFQDPddQVFSSTVWDDVAFGPVNM-GLDKDEVERRVEEALKAvrmwDFRDKPPYH-----------LSYGQKKRVAI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 275 ARALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGThEELLLKP 352
Cdd:PRK13647  150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLTDE 228


                  .
gi 1907190441 353 N 353
Cdd:PRK13647  229 D 229
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 121-349 7.79e-32

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 120.65  E-value: 7.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLRL----YDPNSGTVSLDGHDIRQLNPvWL 196
Cdd:PRK13548    2 MLEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKST----LLRAlsgeLSPDSGEVRLNGRPLADWSP-AE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 197 RSKI-GTVSQEPVL-FSCSVAENIAYGADNLSSVTAQQ---VERAAEVANAAEFI-RSFPQgfdtvvgekgilLSGGQKQ 270
Cdd:PRK13548   74 LARRrAVLPQHSSLsFPFTVEEVVAMGRAPHGLSRAEDdalVAAALAQVDLAHLAgRDYPQ------------LSGGEQQ 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 271 RIAIARALL------KNPKILLLDEATSALDAENEHLVQEALDRLM--EGRTVLIIAHRLstikN-----ANFVAVLDHG 337
Cdd:PRK13548  142 RVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAheRGLAVIVVLHDL----NlaaryADRIVLLHQG 217

                         250
                  ....*....|..
gi 1907190441 338 KICEHGTHEELL 349
Cdd:PRK13548  218 RLVADGTPAEVL 229
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 122-360 8.22e-32

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 125.95  E-value: 8.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPAR--------PEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLyDPNSGTVSLDGHDI----- 188
Cdd:COG4172   276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLdglsr 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 189 RQLNPvwLRSKIGTVSQEPvlFSC-----SVAENIAYG----ADNLSSvtAQQVERAA----EVANAAEFIRSFPQGFdt 255
Cdd:COG4172   355 RALRP--LRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSA--AERRARVAealeEVGLDPAARHRYPHEF-- 426

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 256 vvgekgillSGGQKQRIAIARALLKNPKILLLDEATSALDAenehLVQ-EALDRLME-----GRTVLIIAHRLSTIKN-A 328
Cdd:COG4172   427 ---------SGGQRQRIAIARALILEPKLLVLDEPTSALDV----SVQaQILDLLRDlqrehGLAYLFISHDLAVVRAlA 493

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907190441 329 NFVAVLDHGKICEHGTHEELLLKPNGLY-RKLM 360
Cdd:COG4172   494 HRVMVMKDGKVVEQGPTEQVFDAPQHPYtRALL 526
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 122-320 9.00e-32

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: 119.12  E-value: 9.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLR----LYDPNSGTVSLDGHDIRQlNPVWLR 197
Cdd:COG4133     3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTT----LLRilagLLPPSAGEVLWNGEPIRD-AREDYR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 198 SKIGTVSQEPVLF-SCSVAENIAYGADNL-SSVTAQQVERAAEVANAAEFIrsfpqgfDTVVGEkgilLSGGQKQRIAIA 275
Cdd:COG4133    75 RRLAYLGHADGLKpELTVRENLRFWAALYgLRADREAIDEALEAVGLAGLA-------DLPVRQ----LSAGQKRRVALA 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907190441 276 RALLKNPKILLLDEATSALDAENEHLVQEALDR-LMEGRTVLIIAH 320
Cdd:COG4133   144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 141-347 1.22e-31

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: 120.14  E-value: 1.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 141 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPvWLRSKIGtVS---QEPVLF-SCSVAE 216
Cdd:COG0411    21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLG-IArtfQNPRLFpELTVLE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 217 NIAYGA---------DNLSSVTAQQVERAAEVANAAEFIRSFpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLL 287
Cdd:COG0411    99 NVLVAAharlgrgllAALLRLPRARREEREARERAEELLERV--GLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 288 DEATSALdaeNEHLVQEALDRLME-----GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEE 347
Cdd:COG0411   177 DEPAAGL---NPEETEELAELIRRlrderGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 121-373 1.37e-31

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: 126.60  E-value: 1.37e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  121 ALEFRNVHFTYpARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDpnsgtvSLDGHdirqlnpVWLRSKI 200
Cdd:TIGR00957  636 SITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD------KVEGH-------VHMKGSV 701

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  201 GTVSQEPVLFSCSVAENIAYGAdNLSSVTAQQVERAAEVANAAEFIrsfPQGFDTVVGEKGILLSGGQKQRIAIARALLK 280
Cdd:TIGR00957  702 AYVPQQAWIQNDSLRENILFGK-ALNEKYYQQVLEACALLPDLEIL---PSGDRTEIGEKGVNLSGGQKQRVSLARAVYS 777

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  281 NPKILLLDEATSALDAE-NEHLVQEAL--DRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKpNGLYR 357
Cdd:TIGR00957  778 NADIYLFDDPLSAVDAHvGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR-DGAFA 856

                          250
                   ....*....|....*.
gi 1907190441  358 KLMNkqsflSYNGAEQ 373
Cdd:TIGR00957  857 EFLR-----TYAPDEQ 867
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 119-352 2.03e-31

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 119.63  E-value: 2.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 119 QGALEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYD--PN---SGTVSLDGHDIRQLNP 193
Cdd:PRK14247    1 MNKIEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 194 VWLRSKIGTVSQEP-VLFSCSVAENIAYGA--DNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEkgilLSGGQKQ 270
Cdd:PRK14247   78 IELRRRVQMVFQIPnPIPNLSIFENVALGLklNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGK----LSGGQQQ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 271 RIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAH------RLStiknaNFVAVLDHGKICEHGT 344
Cdd:PRK14247  154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGP 228


                  ....*...
gi 1907190441 345 HEELLLKP 352
Cdd:PRK14247  229 TREVFTNP 236
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 144-352 2.06e-31

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 119.50  E-value: 2.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 144 SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN-----SGTVSLDGHDI--RQLNPVWLRSKIGTVSQEPVLFSCSVAE 216
Cdd:PRK14239   25 SLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPMSIYE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 217 NIAYG----ADNLSSVTAQQVERAAEVANAAEFIRSfpQGFDTVVGekgilLSGGQKQRIAIARALLKNPKILLLDEATS 292
Cdd:PRK14239  105 NVVYGlrlkGIKDKQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIARVLATSPKIILLDEPTS 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 293 ALDAENEHLVQEALDRLMEGRTVLIIAH------RLSTiKNANFVAvldhGKICEHGTHEELLLKP 352
Cdd:PRK14239  178 ALDPISAGKIEETLLGLKDDYTMLLVTRsmqqasRISD-RTGFFLD----GDLIEYNDTKQMFMNP 238
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 122-355 2.95e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 120.12  E-value: 2.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARpevSVFQ-----DFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI------RQ 190
Cdd:PRK13634    3 ITFQKVEHRYQYK---TPFErralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkknKK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 191 LNPvwLRSKIGTVSQ--EPVLFSCSVAENIAYGADNLSSVTAQQVERAAE----VANAAEFIRSFPqgFDtvvgekgilL 264
Cdd:PRK13634   80 LKP--LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREmielVGLPEELLARSP--FE---------L 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 265 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICE 341
Cdd:PRK13634  147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARyADQIVVMHKGTVFL 226

                         250
                  ....*....|....
gi 1907190441 342 HGTHEELLLKPNGL 355
Cdd:PRK13634  227 QGTPREIFADPDEL 240
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 121-349 4.40e-31

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 118.65  E-value: 4.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSG-TVSLDGHDIRQLNPVWLRSK 199
Cdd:COG1119     3 LLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVS---QEPVLFSCSVAENIAYGA-DNL---SSVTAQQVERAAEVANA---AEFI-RSFPQgfdtvvgekgilLSGGQ 268
Cdd:COG1119    80 IGLVSpalQLRFPRDETVLDVVLSGFfDSIglyREPTDEQRERARELLELlglAHLAdRPFGT------------LSQGE 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 269 KQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKNA-NFVAVLDHGKICEHGTH 345
Cdd:COG1119   148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPK 227


                  ....
gi 1907190441 346 EELL 349
Cdd:COG1119   228 EEVL 231
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 142-349 6.14e-31

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: 120.59  E-value: 6.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 142 DFSLSIPSGSVTALVGPSGSGKSTVVSL---LLRlydPNSGTVSLDGH-----DIRQLNPVWLRSkIGTVSQEPVLFS-C 212
Cdd:COG4148    17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqdsARGIFLPPHRRR-IGYVFQEARLFPhL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 213 SVAENIAYGAdnlssvtaqqvERAAEVANAAEFirsfpqgfDTVVGEKGI---------LLSGGQKQRIAIARALLKNPK 283
Cdd:COG4148    93 SVRGNLLYGR-----------KRAPRAERRISF--------DEVVELLGIghlldrrpaTLSGGERQRVAIGRALLSSPR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190441 284 ILLLDEATSALDAENEHLVQEALDRLmegRT-----VLIIAH------RLstiknANFVAVLDHGKICEHGTHEELL 349
Cdd:COG4148   154 LLLMDEPLAALDLARKAEILPYLERL---RDeldipILYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVL 222
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 121-353 7.32e-31

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: 117.83  E-value: 7.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARPEVsvfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPvwLRSKI 200
Cdd:cd03296     2 SIEVRNVSKRFGDFVAL---DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV--QERNV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQEPVLFS-CSVAENIAYGAdnlssvtaqQVERAAEVANAAEfIRSFPQGFDTVVGEKGIL------LSGGQKQRIA 273
Cdd:cd03296    77 GFVFQHYALFRhMTVFDNVAFGL---------RVKPRSERPPEAE-IRAKVHELLKLVQLDWLAdrypaqLSGGQRQRVA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 274 IARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELLL 350
Cdd:cd03296   147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYD 226


                  ...
gi 1907190441 351 KPN 353
Cdd:cd03296   227 HPA 229
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
115-356 8.30e-31

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 120.71  E-value: 8.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 115 EKTFQGALEFRNVHFTYPARPEVsvfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPv 194
Cdd:PRK11607   13 RKALTPLLEIRNLTKSFDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 195 wLRSKIGTVSQEPVLFS-CSVAENIAYG--ADNLSSV-TAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQ 270
Cdd:PRK11607   89 -YQRPINMMFQSYALFPhMTVEQNIAFGlkQDKLPKAeIASRVNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 271 RIAIARALLKNPKILLLDEATSALDAE----NEHLVQEALDRLmeGRTVLIIAH-RLSTIKNANFVAVLDHGKICEHGTH 345
Cdd:PRK11607  157 RVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEP 234

                         250
                  ....*....|.
gi 1907190441 346 EELLLKPNGLY 356
Cdd:PRK11607  235 EEIYEHPTTRY 245
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 141-322 1.61e-30

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 117.58  E-value: 1.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 141 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYD--PN---SGTVSLDGHDI--RQLNPVWLRSKIGTVSQEPVLFSCS 213
Cdd:PRK14243   27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 214 VAENIAYGAD------NLSSVTAQQVERAA---EVANAaefirsfpqgfdtvVGEKGILLSGGQKQRIAIARALLKNPKI 284
Cdd:PRK14243  107 IYDNIAYGARingykgDMDELVERSLRQAAlwdEVKDK--------------LKQSGLSLSGGQQQRLCIARAIAVQPEV 172

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907190441 285 LLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRL 322
Cdd:PRK14243  173 ILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 121-338 1.90e-30

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 121.67  E-value: 1.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP-VWLRSK 199
Cdd:COG3845     5 ALELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPrDAIALG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQEPVLF-SCSVAENIAYGADNLSSVtaqQVERAAEVANAAEFIRSFpqGF----DTVVGEkgilLSGGQKQRIAI 274
Cdd:COG3845    82 IGMVHQHFMLVpNLTVAENIVLGLEPTKGG---RLDRKAARARIRELSERY--GLdvdpDAKVED----LSVGEQQRVEI 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190441 275 ARALLKNPKILLLDEATSAL-DAENEHLVqEALDRLM-EGRTVLIIAHRLSTIK-NANFVAVLDHGK 338
Cdd:COG3845   153 LKALYRGARILILDEPTAVLtPQEADELF-EILRRLAaEGKSIIFITHKLREVMaIADRVTVLRRGK 218
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 122-339 2.07e-30

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: 114.06  E-value: 2.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV-WLRSKI 200
Cdd:cd03216     1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQepvlfscsvaeniaygadnlssvtaqqveraaevanaaefirsfpqgfdtvvgekgilLSGGQKQRIAIARALLK 280
Cdd:cd03216    78 AMVYQ----------------------------------------------------------LSVGERQMVEIARALAR 99

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907190441 281 NPKILLLDEATSAL-DAENEHLVqEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHGKI 339
Cdd:cd03216   100 NARLLILDEPTAALtPAEVERLF-KVIRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 122-348 3.77e-30

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: 115.29  E-value: 3.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPEVSVfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlNPVWLRSKIG 201
Cdd:cd03263     1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLFS-CSVAENIAYGAdNLSSVTAQQVEraAEVANAAEFIRSFPQGfDTVVGEkgilLSGGQKQRIAIARALLK 280
Cdd:cd03263    79 YCPQFDALFDeLTVREHLRFYA-RLKGLPKSEIK--EEVELLLRVLGLTDKA-NKRART----LSGGMKRKLSLAIALIG 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 281 NPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEEL 348
Cdd:cd03263   151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 142-343 6.19e-30

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: 114.51  E-value: 6.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 142 DFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwlRSKIGTVSQEPVLFS-CSVAENIAY 220
Cdd:cd03298    16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 221 GAD---NLSSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 297
Cdd:cd03298    94 GLSpglKLTAEDRQAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907190441 298 nehLVQEALDRLME-----GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHG 343
Cdd:cd03298   163 ---LRAEMLDLVLDlhaetKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
121-346 7.48e-30

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 115.11  E-value: 7.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI---RQLNP---V 194
Cdd:COG4161     2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEkaiR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 195 WLRSKIGTVSQE----PVLfscSVAEN-IAYGADNLSSVTAQQVERAAEVANA---AEFIRSFPQgfdtvvgekgiLLSG 266
Cdd:COG4161    79 LLRQKVGMVFQQynlwPHL---TVMENlIEAPCKVLGLSKEQAREKAMKLLARlrlTDKADRFPL-----------HLSG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 267 GQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGT 344
Cdd:COG4161   145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFArKVASQVVYMEKGRIIEQGD 224


                  ..
gi 1907190441 345 HE 346
Cdd:COG4161   225 AS 226
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 135-337 9.09e-30

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: 114.35  E-value: 9.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 135 PEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLL--------RLYDPNSGTVSLDGHDIRQLNpvwlRSKIGTVSQE 206
Cdd:cd03290    12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILgemqtlegKVHWSNKNESEPSFEATRSRN----RYSVAYAAQK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 207 PVLFSCSVAENIAYGadnlSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILL 286
Cdd:cd03290    88 PWLLNATVEENITFG----SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907190441 287 LDEATSALDAE-NEHLVQEALDRLM--EGRTVLIIAHRLSTIKNANFVAVLDHG 337
Cdd:cd03290   164 LDDPFSALDIHlSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
122-356 1.05e-29

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 117.74  E-value: 1.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwlRSKIG 201
Cdd:PRK09452   15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLFS-CSVAENIAYGAdNLSSVTAQQVERaaEVANAAEFIRsfpqgFDTVVGEKGILLSGGQKQRIAIARALLK 280
Cdd:PRK09452   90 TVFQSYALFPhMTVFENVAFGL-RMQKTPAAEITP--RVMEALRMVQ-----LEEFAQRKPHQLSGGQQQRVAIARAVVN 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 281 NPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAH-RLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGLY 356
Cdd:PRK09452  162 KPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLF 240
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 122-339 1.41e-29

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: 113.50  E-value: 1.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwlRSKIG 201
Cdd:cd03301     1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLF-SCSVAENIAYGadnLSSVTAQQVERAAEVANAAEFIrsfpqGFDTVVGEKGILLSGGQKQRIAIARALLK 280
Cdd:cd03301    76 MVFQNYALYpHMTVYDNIAFG---LKLRKVPKDEIDERVREVAELL-----QIEHLLDRKPKQLSGGQRQRVALGRAIVR 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907190441 281 NPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAH-RLSTIKNANFVAVLDHGKI 339
Cdd:cd03301   148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
cbiO PRK13641
energy-coupling factor transporter ATPase;
121-355 1.84e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 115.31  E-value: 1.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTY-PARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIR----QLNPV 194
Cdd:PRK13641    2 SIKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 195 WLRSKIGTVSQ--EPVLFSCSVAENIAYGADNLSsVTAQQVERAAevanaAEFIRSFpqGFDTVVGEKGIL-LSGGQKQR 271
Cdd:PRK13641   82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFG-FSEDEAKEKA-----LKWLKKV--GLSEDLISKSPFeLSGGQMRR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 272 IAIARALLKNPKILLLDEATSALDAENEH-LVQEALDRLMEGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEELL 349
Cdd:PRK13641  154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIF 233


                  ....*.
gi 1907190441 350 LKPNGL 355
Cdd:PRK13641  234 SDKEWL 239
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 142-323 1.84e-29

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: 113.16  E-value: 1.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 142 DFSLSIP---SGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDG---HDIRQ-LNPVWLRSKIGTVSQEPVLFS-CS 213
Cdd:cd03297    12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKkINLPPQQRKIGLVFQQYALFPhLN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 214 VAENIAYGADNLS-SVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALLKNPKILLLDEATS 292
Cdd:cd03297    92 VRENLAFGLKRKRnREDRISVDELLDLLGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEPFS 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907190441 293 ALDAENEHLVQEALDRLME--GRTVLIIAHRLS 323
Cdd:cd03297   161 ALDRALRLQLLPELKQIKKnlNIPVIFVTHDLS 193
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
121-320 2.39e-29

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 114.19  E-value: 2.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPA-RPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlnPVWLRsk 199
Cdd:COG4525     3 MLTVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADR-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 iGTVSQEPVLFS-CSVAENIAYGadnlssVTAQQVERAAEVANAAEFIRSFP-QGFdtvvGEKGIL-LSGGQKQRIAIAR 276
Cdd:COG4525    79 -GVVFQKDALLPwLNVLDNVAFG------LRLRGVPKAERRARAEELLALVGlADF----ARRRIWqLSGGMRQRVGIAR 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907190441 277 ALLKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAH 320
Cdd:COG4525   148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITH 193
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 139-343 4.65e-29

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: 111.93  E-value: 4.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 139 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWlrSKIGTVSQEPVLF-SCSVAEN 217
Cdd:cd03268    15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYpNLTAREN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 218 IAYGAdNLSSVTAQQVERAAEVAnaaefirsfpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 297
Cdd:cd03268    93 LRLLA-RLLGIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907190441 298 NEHLVQEALDRLM-EGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHG 343
Cdd:cd03268   161 GIKELRELILSLRdQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
138-349 5.07e-29

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 113.19  E-value: 5.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 138 SVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVL-FSCSVAE 216
Cdd:PRK11231   16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 217 NIAYGAD-------NLSSVTAQQVERAAEVANAAEFIrsfpqgfDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDE 289
Cdd:PRK11231   96 LVAYGRSpwlslwgRLSAEDNARVNQAMEQTRINHLA-------DRRLTD----LSGGQRQRAFLAMVLAQDTPVVLLDE 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 290 ATSALDAenEHLVQeaLDRLM-----EGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELL 349
Cdd:PRK11231  165 PTTYLDI--NHQVE--LMRLMrelntQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVM 226
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
122-355 5.08e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 113.64  E-value: 5.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPEVS---VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVW-LR 197
Cdd:PRK13633    5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 198 SKIGTVSQEP--VLFSCSVAENIAYGADNL---SSVTAQQVERAAEVANAAEFIRSFPQgfdtvvgekgiLLSGGQKQRI 272
Cdd:PRK13633   85 NKAGMVFQNPdnQIVATIVEEDVAFGPENLgipPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 273 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEEL-- 348
Cdd:PRK13633  154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIfk 233

                         250
                  ....*....|
gi 1907190441 349 ---LLKPNGL 355
Cdd:PRK13633  234 eveMMKKIGL 243
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 121-346 6.55e-29

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 112.41  E-value: 6.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARpevSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH-----------DIR 189
Cdd:PRK11124    2 SIQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpsdkAIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 190 QLnpvwlRSKIGTVSQE----PVLfscSVAENIAYGADNLSSVTAQQ-VERAAEVANA---AEFIRSFPQGfdtvvgekg 261
Cdd:PRK11124   79 EL-----RRNVGMVFQQynlwPHL---TVQQNLIEAPCRVLGLSKDQaLARAEKLLERlrlKPYADRFPLH--------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 262 ilLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTI-KNANFVAVLDHGKI 339
Cdd:PRK11124  142 --LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVArKTASRVVYMENGHI 219


                  ....*..
gi 1907190441 340 CEHGTHE 346
Cdd:PRK11124  220 VEQGDAS 226
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
139-356 6.79e-29

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 115.20  E-value: 6.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 139 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlnpvwlRS----KIGTVSQEPVLFS-CS 213
Cdd:PRK11432   21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSiqqrDICMVFQSYALFPhMS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 214 VAENIAYGADNL---SSVTAQQVERAAEVANAAefirsfpqGF-DTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDE 289
Cdd:PRK11432   95 LGENVGYGLKMLgvpKEERKQRVKEALELVDLA--------GFeDRYVDQ----ISGGQQQRVALARALILKPKVLLFDE 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 290 ATSALDAENEHLVQEALDRLME--GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELLLKPNGLY 356
Cdd:PRK11432  163 PLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
cbiO PRK13649
energy-coupling factor transporter ATPase;
121-344 7.06e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 113.30  E-value: 7.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPA-RP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI------RQLN 192
Cdd:PRK13649    2 GINLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsknKDIK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 193 PVwlRSKIGTVSQ--EPVLFSCSVAENIAYGADN--LSSVTAQQV--ERAAEVANAAEFIRSFPqgFDtvvgekgilLSG 266
Cdd:PRK13649   82 QI--RKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALarEKLALVGISESLFEKNP--FE---------LSG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 267 GQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGT 344
Cdd:PRK13649  149 GQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 122-324 9.26e-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: 110.72  E-value: 9.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPEVSVFQ---DFSLSIPSGSVTALVGPSGSGKSTVVSLL--LRLYDPNSGTVSLDGHDIRqlnPVWL 196
Cdd:cd03213     4 LSFRNLTVTVKSSPSKSGKQllkNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 197 RSKIGTVSQEPVLFSC-SVAENIAYGAdNLSSvtaqqveraaevanaaefirsfpqgfdtvvgekgilLSGGQKQRIAIA 275
Cdd:cd03213    81 RKIIGYVPQDDILHPTlTVRETLMFAA-KLRG------------------------------------LSGGERKRVSIA 123

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907190441 276 RALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLST 324
Cdd:cd03213   124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPSS 173
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 138-352 9.48e-29

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 112.45  E-value: 9.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 138 SVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH------DIRQLNPVWLRSKIGTVSQEPVLFS 211
Cdd:PRK14246   24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 212 -CSVAENIAYGADNLSSVTAQQVERAAEvanaaEFIRS---FPQGFDTVvGEKGILLSGGQKQRIAIARALLKNPKILLL 287
Cdd:PRK14246  104 hLSIYDNIAYPLKSHGIKEKREIKKIVE-----ECLRKvglWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLM 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 288 DEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEELLLKP 352
Cdd:PRK14246  178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTSP 243
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
139-352 1.23e-28

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 114.41  E-value: 1.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 139 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPvwlRS-KIGTVSQEPVLFS-CSVAE 216
Cdd:PRK10851   17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---RDrKVGFVFQHYALFRhMTVFD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 217 NIAYGADNL-------SSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALLKNPKILLLDE 289
Cdd:PRK10851   94 NIAFGLTVLprrerpnAAAIKAKVTQLLEMVQLAHLADRYPAQ-----------LSGGQKQRVALARALAVEPQILLLDE 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 290 ATSALDAENEHLVQEALDRLMEG---RTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKP 352
Cdd:PRK10851  163 PFGALDAQVRKELRRWLRQLHEElkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 122-349 1.32e-28

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


Pssm-ID: 440179 [Multi-domain]  Cd Length: 236  Bit Score: 111.23  E-value: 1.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnPVWLRSK-- 199
Cdd:COG0410     4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL-PPHRIARlg 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQEPVLF-SCSVAENI---AYGADNLSSVtAQQVERAAEVanaaefirsFPqgfdtVVGE----KGILLSGGQKQR 271
Cdd:COG0410    80 IGYVPEGRRIFpSLTVEENLllgAYARRDRAEV-RADLERVYEL---------FP-----RLKErrrqRAGTLSGGEQQM 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 272 IAIARALLKNPKILLLDEATSALdAENehLVQE---ALDRLM-EGRTVLII---AHRLSTIknANFVAVLDHGKICEHGT 344
Cdd:COG0410   145 LAIGRALMSRPKLLLLDEPSLGL-APL--IVEEifeIIRRLNrEGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGT 219


                  ....*
gi 1907190441 345 HEELL 349
Cdd:COG0410   220 AAELL 224
cbiO PRK13650
energy-coupling factor transporter ATPase;
122-355 1.52e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 112.52  E-value: 1.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNpVW-LRSKI 200
Cdd:PRK13650    5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN-VWdIRHKI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQEP--VLFSCSVAENIAYGADNLSSVTAQQVERaaeVANAAEFIrsfpqGFDTVVGEKGILLSGGQKQRIAIARAL 278
Cdd:PRK13650   84 GMVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKER---VNEALELV-----GMQDFKEREPARLSGGQKQRVAIAGAV 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 279 LKNPKILLLDEATSALDAENE-HLVQEALD-RLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGL 355
Cdd:PRK13650  156 AMRPKIIILDEATSMLDPEGRlELIKTIKGiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDL 234
PLN03232 PLN03232
ABC transporter C family member; Provisional
 121-360 1.65e-28

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 117.77  E-value: 1.65e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  121 ALEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYdPNSGTVSLDghdirqlnpvwLRSKI 200
Cdd:PLN03232   614 AISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL-SHAETSSVV-----------IRGSV 681

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  201 GTVSQEPVLFSCSVAENIAYGADNLSSvtaqQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLK 280
Cdd:PLN03232   682 AYVPQVSWIFNATVRENILFGSDFESE----RYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYS 757

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  281 NPKILLLDEATSALDAeneHLVQEALDRLM----EGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEElLLKPNGLY 356
Cdd:PLN03232   758 NSDIYIFDDPLSALDA---HVAHQVFDSCMkdelKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLF 833


                   ....
gi 1907190441  357 RKLM 360
Cdd:PLN03232   834 KKLM 837
PTZ00243 PTZ00243
ABC transporter; Provisional
 120-380 3.05e-28

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 116.80  E-value: 3.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  120 GALEFRNVHFTYpaRPEVS-VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRS 198
Cdd:PTZ00243  1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  199 KIGTVSQEPVLFSCSVAENIaygaDNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARAL 278
Cdd:PTZ00243  1385 QFSMIPQDPVLFDGTVRQNV----DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARAL 1460

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  279 LK-NPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGLYR 357
Cdd:PTZ00243  1461 LKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFH 1540

                          250       260
                   ....*....|....*....|...
gi 1907190441  358 KLMNKqsfLSYNGAEQFLEPARA 380
Cdd:PTZ00243  1541 SMVEA---LGRSEAKRFLQLVGR 1560
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 122-341 3.64e-28

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: 111.05  E-value: 3.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYP------ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVW 195
Cdd:TIGR02769   3 LEVRDVTHTYRtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 196 ---LRSKIGTVSQE---PVLFSCSVAENIAYGADNLSSVT-AQQVERAAEVANA----AEFIRSFPQGFdtvvgekgill 264
Cdd:TIGR02769  83 rraFRRDVQLVFQDspsAVNPRMTVRQIIGEPLRHLTSLDeSEQKARIAELLDMvglrSEDADKLPRQL----------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 265 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICE 341
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
PLN03130 PLN03130
ABC transporter C family member; Provisional
 94-362 4.51e-28

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 116.38  E-value: 4.51e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   94 RLWELL---ER--QPRLPFNEGmvldektfQGALEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVS 168
Cdd:PLN03130   590 RLEELLlaeERvlLPNPPLEPG--------LPAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIS 661

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  169 LLLRLYDPNSGTVsldghdirqlnpVWLRSKIGTVSQEPVLFSCSVAENIAYGADnlssVTAQQVERAAEVANAAEFIRS 248
Cdd:PLN03130   662 AMLGELPPRSDAS------------VVIRGTVAYVPQVSWIFNATVRDNILFGSP----FDPERYERAIDVTALQHDLDL 725

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  249 FPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneHLVQEALDRL----MEGRTVLIIAHRLST 324
Cdd:PLN03130   726 LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA---HVGRQVFDKCikdeLRGKTRVLVTNQLHF 802

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1907190441  325 IKNANFVAVLDHGKICEHGTHEELLlkPNG-LYRKLMNK 362
Cdd:PLN03130   803 LSQVDRIILVHEGMIKEEGTYEELS--NNGpLFQKLMEN 839
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 122-297 4.75e-28

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 109.11  E-value: 4.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN---SGTVSLDGHDIRQLNPvwLRS 198
Cdd:COG4136     2 LSLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA--EQR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 199 KIGTVSQEPVLFS-CSVAENIAYGADNlsSVT----AQQVERAAEVANAAEFIRSFPqgfDTvvgekgilLSGGQKQRIA 273
Cdd:COG4136    77 RIGILFQDDLLFPhLSVGENLAFALPP--TIGraqrRARVEQALEEAGLAGFADRDP---AT--------LSGGQRARVA 143

                         170       180
                  ....*....|....*....|....
gi 1907190441 274 IARALLKNPKILLLDEATSALDAE 297
Cdd:COG4136   144 LLRALLAEPRALLLDEPFSKLDAA 167
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 122-339 6.08e-28

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 110.56  E-value: 6.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFT-YPARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnPVWLRSK 199
Cdd:COG1101     2 LELKNLSKTfNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 -IGTVSQEPVLFSC---SVAEN--IAYG---ADNLS-SVTAQQVERAAEvanaaeFIRSFPQGF----DTVVGekgiLLS 265
Cdd:COG1101    81 yIGRVFQDPMMGTApsmTIEENlaLAYRrgkRRGLRrGLTKKRRELFRE------LLATLGLGLenrlDTKVG----LLS 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190441 266 GGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGR--TVLIIAHRLS-TIKNANFVAVLDHGKI 339
Cdd:COG1101   151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRI 227
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 139-352 1.07e-27

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 109.45  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 139 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV--------WLRSKIGTVSQEPVLF 210
Cdd:PRK11264   18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqqkglirQLRQHVGFVFQNFNLF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 211 SC-SVAENIAYGadnlsSVTAQQVERAAEVANAAEFI---------RSFPQgfdtvvgekgiLLSGGQKQRIAIARALLK 280
Cdd:PRK11264   98 PHrTVLENIIEG-----PVIVKGEPKEEATARARELLakvglagkeTSYPR-----------RLSGGQQQRVAIARALAM 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190441 281 NPKILLLDEATSALDAEnehLVQEALDRLM----EGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKP 352
Cdd:PRK11264  162 RPEVILFDEPTSALDPE---LVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADP 235
PTZ00243 PTZ00243
ABC transporter; Provisional
 131-359 2.68e-27

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 114.11  E-value: 2.68e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  131 YPARPEVsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVsldghdirqlnpvWLRSKIGTVSQEPVLF 210
Cdd:PTZ00243   668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  211 SCSVAENIAYGADnlssvtaqqvERAAEVANAAEF------IRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKI 284
Cdd:PTZ00243   734 NATVRGNILFFDE----------EDAARLADAVRVsqleadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDV 803

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441  285 LLLDEATSALDAE-NEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPngLYRKL 359
Cdd:PTZ00243   804 YLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS--LYATL 877
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 123-349 3.50e-27

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 107.86  E-value: 3.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 123 EFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGT 202
Cdd:COG4604     3 EIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 203 VSQEPVLFS-CSVAENIAYG-----ADNLSSVTAQQVERAAEVANAAEFIRSFpqgFDTvvgekgilLSGGQKQRIAIAR 276
Cdd:COG4604    80 LRQENHINSrLTVRELVAFGrfpysKGRLTAEDREIIDEAIAYLDLEDLADRY---LDE--------LSGGQRQRAFIAM 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 277 ALLKNPKILLLDEATSALDAenEHLVQ--EALDRLME--GRTVLIIAHRLstiknaNFVAVL-DH------GKICEHGTH 345
Cdd:COG4604   149 VLAQDTDYVLLDEPLNNLDM--KHSVQmmKLLRRLADelGKTVVIVLHDI------NFASCYaDHivamkdGRVVAQGTP 220


                  ....
gi 1907190441 346 EELL 349
Cdd:COG4604   221 EEII 224
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 137-348 4.02e-27

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: 107.07  E-value: 4.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 137 VSVFQDF------SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlNPVWLRSKIGTVSQEPVLf 210
Cdd:cd03265     7 VKKYGDFeavrgvSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 211 scsvaENIAYGADNL----------SSVTAQQVERAAEVANAAEFIrsfpqgfDTVVGEkgilLSGGQKQRIAIARALLK 280
Cdd:cd03265    85 -----DDELTGWENLyiharlygvpGAERRERIDELLDFVGLLEAA-------DRLVKT----YSGGMRRRLEIARSLVH 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907190441 281 NPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEEL 348
Cdd:cd03265   149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 122-349 7.19e-27

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: 106.47  E-value: 7.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnPVWLRSK-- 199
Cdd:cd03218     1 LRAENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL-PMHKRARlg 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQEPVLF-SCSVAENIAYGADNLSSVTAQQVERAAEVAnaAEFirsfpqGFDTVVGEKGILLSGGQKQRIAIARAL 278
Cdd:cd03218    77 IGYLPQEASIFrKLTVEENILAVLEIRGLSKKEREEKLEELL--EEF------HITHLRKSKASSLSGGERRRVEIARAL 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907190441 279 LKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELL 349
Cdd:cd03218   149 ATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDrGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 136-352 7.22e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 108.78  E-value: 7.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 136 EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLD----GHDIRQLNPVW------------LRSK 199
Cdd:PRK13631   38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITnpyskkiknfkeLRRR 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQEP--VLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAEFIRSF----PQGfdtvvgekgilLSGGQKQRIA 273
Cdd:PRK13631  118 VSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYlersPFG-----------LSGGQKRRVA 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 274 IARALLKNPKILLLDEATSALDAENEH-LVQEALDRLMEGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEELLLK 351
Cdd:PRK13631  187 IAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTD 266


                  .
gi 1907190441 352 P 352
Cdd:PRK13631  267 Q 267
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 122-348 1.32e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 107.09  E-value: 1.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL--RSK 199
Cdd:PRK13639    2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQEP--VLFSCSVAENIAYGADNLSsVTAQQVERAAEVANAAEFIrsfpQGFDTVVGEKgilLSGGQKQRIAIARA 277
Cdd:PRK13639   80 VGIVFQNPddQLFAPTVEEDVAFGPLNLG-LSKEEVEKRVKEALKAVGM----EGFENKPPHH---LSGGQKKRVAIAGI 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907190441 278 LLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEEL 348
Cdd:PRK13639  152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 121-320 1.97e-26

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: 105.59  E-value: 1.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYP-ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLN----PVW 195
Cdd:COG4181     8 IIELRGLTKTVGtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 196 LRSKIGTVSQ-EPVLFSCSVAENIAY-----GADNlssvtAQQveRAAEVANA---AEFIRSFPQGfdtvvgekgilLSG 266
Cdd:COG4181    88 RARHVGFVFQsFQLLPTLTALENVMLplelaGRRD-----ARA--RARALLERvglGHRLDHYPAQ-----------LSG 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 267 GQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAH 320
Cdd:COG4181   150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRerGTTLVLVTH 205
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 142-353 2.32e-26

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


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 107.89  E-value: 2.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 142 DFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDG---HDIRQ---LNPVwlRSKIGTVSQEPVLFS-CSV 214
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgifLPPE--KRRIGYVFQEARLFPhLSV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 215 AENIAYGadnLSSVTAQQVEraaevANAAEFIRSFpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSAL 294
Cdd:TIGR02142  93 RGNLRYG---MKRARPSERR-----ISFERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907190441 295 DAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPN 353
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPD 224
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 122-349 2.88e-26

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 105.11  E-value: 2.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnPVWLRSK-- 199
Cdd:COG1137     4 LEAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-PMHKRARlg 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQEPVLF-SCSVAENIAYGADNLSSVTAQQVERAAEVAnaAEFirsfpqGFDTVVGEKGILLSGGQKQRIAIARAL 278
Cdd:COG1137    80 IGYLPQEASIFrKLTVEDNILAVLELRKLSKKEREERLEELL--EEF------GITHLRKSKAYSLSGGERRRVEIARAL 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 279 LKNPKILLLDEATSALD----AENEHLVQEALDRlmeGRTVLIIAHR----LSTIKNAnfvAVLDHGKICEHGTHEELL 349
Cdd:COG1137   152 ATNPKFILLDEPFAGVDpiavADIQKIIRHLKER---GIGVLITDHNvretLGICDRA---YIISEGKVLAEGTPEEIL 224
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 121-352 3.20e-26

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 105.89  E-value: 3.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARpevSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNS-----GTVSLDGHDI--RQLNP 193
Cdd:PRK14258    7 AIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 194 VWLRSKIGTVSQEPVLFSCSVAENIAYGADNLSSVTAQQVERAAEVA-NAAEFirsfpqgFDTV---VGEKGILLSGGQK 269
Cdd:PRK14258   84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESAlKDADL-------WDEIkhkIHKSALDLSGGQQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 270 QRIAIARALLKNPKILLLDEATSALDA----ENEHLVQEAldRLMEGRTVLIIAHRLSTIKN-ANFVAVLDH-----GKI 339
Cdd:PRK14258  157 QRLCIARALAVKPKVLLMDEPCFGLDPiasmKVESLIQSL--RLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQL 234

                         250
                  ....*....|...
gi 1907190441 340 CEHGTHEELLLKP 352
Cdd:PRK14258  235 VEFGLTKKIFNSP 247
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 122-357 3.97e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 105.66  E-value: 3.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYpaRPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 201
Cdd:PRK13652    4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEP--VLFSCSVAENIAYGADNL---SSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIAR 276
Cdd:PRK13652   82 LVFQNPddQIFSPTVEQDIAFGPINLgldEETVAHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIAG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 277 ALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPN 353
Cdd:PRK13652  151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD 230


                  ....
gi 1907190441 354 GLYR 357
Cdd:PRK13652  231 LLAR 234
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 122-343 4.16e-26

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: 104.37  E-value: 4.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTY-PARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlNPVWLRSKI 200
Cdd:cd03266     2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQEPVLFS-CSVAENIAYGADnLSSVTAQQ----VERAAEVANAAEFIrsfpqgfDTVVGEkgilLSGGQKQRIAIA 275
Cdd:cd03266    81 GFVSDSTGLYDrLTARENLEYFAG-LYGLKGDEltarLEELADRLGMEELL-------DRRVGG----FSTGMRQKVAIA 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 276 RALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHG 343
Cdd:cd03266   149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
cbiO PRK13637
energy-coupling factor transporter ATPase;
126-347 7.19e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 105.51  E-value: 7.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 126 NVHFTY-PARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI--RQLNPVWLRSKIG 201
Cdd:PRK13637    7 NLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEP--VLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAEFirsfpqGFDTVVGEKGILLSGGQKQRIAIARALL 279
Cdd:PRK13637   87 LVFQYPeyQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGL------DYEDYKDKSPFELSGGQKRRVAIAGVVA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907190441 280 KNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEE 347
Cdd:PRK13637  161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
141-356 8.42e-26

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 107.43  E-value: 8.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 141 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRS----KIGTVSQEPVLFS-CSVA 215
Cdd:PRK10070   45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTVL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 216 ENIAYGADnLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVvgekgilLSGGQKQRIAIARALLKNPKILLLDEATSALD 295
Cdd:PRK10070  125 DNTAFGME-LAGINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907190441 296 AENEHLVQEALDRLM--EGRTVLIIAHRL-STIKNANFVAVLDHGKICEHGTHEELLLKPNGLY 356
Cdd:PRK10070  197 PLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 94-321 8.59e-26

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 108.74  E-value: 8.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  94 RLWEL---LERQPRLPFNEGMVLDEKtfQGALEFRNVHFTYPA-RPevsVFQDFSLSIPSGSVTALVGPSGSGKSTvvsl 169
Cdd:COG4178   334 RLAGFeeaLEAADALPEAASRIETSE--DGALALEDLTLRTPDgRP---LLEDLSLSLKPGERLLITGPSGSGKST---- 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 170 LLR----LYDPNSGTVSL-DGHDIrqlnpVWLrskigtvSQEPVLFSCSVAENIAYGADNlSSVTAQQVERAAEVANAAE 244
Cdd:COG4178   405 LLRaiagLWPYGSGRIARpAGARV-----LFL-------PQRPYLPLGTLREALLYPATA-EAFSDAELREALEAVGLGH 471

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190441 245 FIrsfpQGFDTVVgEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHR 321
Cdd:COG4178   472 LA----ERLDEEA-DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 121-352 1.04e-25

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 104.15  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARpevSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN-----SGTVSLDGHDI--RQLNP 193
Cdd:PRK14267    4 AIETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 194 VWLRSKIGTVSQEPVLFS-CSVAENIAYGA---------DNLSSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgil 263
Cdd:PRK14267   81 IEVRREVGMVFQYPNPFPhLTIYDNVAIGVklnglvkskKELDERVEWALKKAALWDEVKDRLNDYPSN----------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 264 LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHR-LSTIKNANFVAVLDHGKICEH 342
Cdd:PRK14267  150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEV 229

                         250
                  ....*....|
gi 1907190441 343 GTHEELLLKP 352
Cdd:PRK14267  230 GPTRKVFENP 239
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
133-341 1.41e-25

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 104.00  E-value: 1.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 133 ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQL--------------------- 191
Cdd:PRK10419   21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraqrkafrrdiqmvfqdsis 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 192 --NPvwlRSKIGTVSQEPV--LFSCSVAENIAYGADNLssvtaQQVERAAEVANaaefiRSFPQgfdtvvgekgilLSGG 267
Cdd:PRK10419  101 avNP---RKTVREIIREPLrhLLSLDKAERLARASEML-----RAVDLDDSVLD-----KRPPQ------------LSGG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 268 QKQRIAIARALLKNPKILLLDEATSALDAeneHLVQEALDRLME-----GRTVLIIAHRLSTIKN-ANFVAVLDHGKICE 341
Cdd:PRK10419  156 QLQRVCLARALAVEPKLLILDEAVSNLDL---VLQAGVIRLLKKlqqqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 122-348 1.71e-25

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: 102.99  E-value: 1.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL-RSKI 200
Cdd:TIGR03410   1 LEVSNLNVYYGQSH---ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQEPVLFS-CSVAENIAYGADNLSSVTAQQVERAAEVanaaefirsFPQGFDtVVGEKGILLSGGQKQRIAIARALL 279
Cdd:TIGR03410  78 AYVPQGREIFPrLTVEENLLTGLAALPRRSRKIPDEIYEL---------FPVLKE-MLGRRGGDLSGGQQQQLAIARALV 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907190441 280 KNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEEL 348
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 122-351 1.74e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 104.16  E-value: 1.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH--DIRQLNPVWLRSK 199
Cdd:PRK13636    6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQEP--VLFSCSVAENIAYGADNL---SSVTAQQVERAAEvANAAEFIRSFPQGFdtvvgekgilLSGGQKQRIAI 274
Cdd:PRK13636   84 VGMVFQDPdnQLFSASVYQDVSFGAVNLklpEDEVRKRVDNALK-RTGIEHLKDKPTHC----------LSFGQKKRVAI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 275 ARALLKNPKILLLDEATSALD----AENEHLVQEALDRLmeGRTVLIIAHRLSTIK-NANFVAVLDHGKICEHGTHEELL 349
Cdd:PRK13636  153 AGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230


                  ..
gi 1907190441 350 LK 351
Cdd:PRK13636  231 AE 232
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
 3-95 1.75e-25

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: 104.18  E-value: 1.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFY 82
Cdd:cd18557   197 EIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLL 276

                          90
                  ....*....|...
gi 1907190441  83 SELMKGLGAGGRL 95
Cdd:cd18557   277 ADIMKALGASERV 289
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
121-346 2.19e-25

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 104.50  E-value: 2.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARpevSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwLRSKI 200
Cdd:PRK13537    7 PIDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQ----EPvlfSCSVAENI-AYGadNLSSVTAQQVEraAEVANAAEFIRsFPQGFDTVVGEkgilLSGGQKQRIAIA 275
Cdd:PRK13537   83 GVVPQfdnlDP---DFTVRENLlVFG--RYFGLSAAAAR--ALVPPLLEFAK-LENKADAKVGE----LSGGMKRRLTLA 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907190441 276 RALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHG-KICEHGTHE 346
Cdd:PRK13537  151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGrKIAEGAPHA 224
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 122-352 2.30e-25

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 104.66  E-value: 2.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPAR-----PE--VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI------ 188
Cdd:PRK11308    6 LQAIDLKKHYPVKrglfkPErlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpe 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 189 -----RQ------------LNPvwlRSKIGTVSQEPVLFSCsvaeniaygadNLSSvtAQQVERAAE----VANAAEFIR 247
Cdd:PRK11308   86 aqkllRQkiqivfqnpygsLNP---RKKVGQILEEPLLINT-----------SLSA--AERREKALAmmakVGLRPEHYD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 248 SFPQGFdtvvgekgillSGGQKQRIAIARALLKNPKILLLDEATSALDAEnehlVQ-EALDRLME-----GRTVLIIAHR 321
Cdd:PRK11308  150 RYPHMF-----------SGGQRQRIAIARALMLDPDVVVADEPVSALDVS----VQaQVLNLMMDlqqelGLSYVFISHD 214

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907190441 322 LSTIKN-ANFVAVLDHGKICEHGTHEELLLKP 352
Cdd:PRK11308  215 LSVVEHiADEVMVMYLGRCVEKGTKEQIFNNP 246
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 122-361 2.37e-25

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: 107.08  E-value: 2.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRN--VHFTYPARpEVSVFQDFSLSIPSGSVTALVGPSGSGKStVVSL-LLRLYDPN----SGTVSLDGHDIRQLNPV 194
Cdd:COG4172     7 LSVEDlsVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKS-VTALsILRLLPDPaahpSGSILFDGQDLLGLSER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 195 WLR----SKIGTVSQEPV-----LFSCS--VAENIAYGAdNLSSVTAQQveRAAE------VANAAEFIRSFP-Qgfdtv 256
Cdd:COG4172    85 ELRrirgNRIAMIFQEPMtslnpLHTIGkqIAEVLRLHR-GLSGAAARA--RALEllervgIPDPERRLDAYPhQ----- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 257 vgekgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAenehLVQ-EALDRLME-----GRTVLIIAHRLSTIKN-AN 329
Cdd:COG4172   157 -------LSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaQILDLLKDlqrelGMALLLITHDLGVVRRfAD 225

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907190441 330 FVAVLDHGKICEHGTHEELLLKPNGLY-RKLMN 361
Cdd:COG4172   226 RVAVMRQGEIVEQGPTAELFAAPQHPYtRKLLA 258
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
121-346 7.79e-25

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 103.76  E-value: 7.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARPEVSvfqDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdirqlNPV-----W 195
Cdd:PRK13536   41 AIDLAGVSKSYGDKAVVN---GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG------VPVpararL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 196 LRSKIGTVSQEPVL-FSCSVAEN-IAYGadNLSSVTAQQVEraAEVANAAEFIRsFPQGFDTVVGEkgilLSGGQKQRIA 273
Cdd:PRK13536  112 ARARIGVVPQFDNLdLEFTVRENlLVFG--RYFGMSTREIE--AVIPSLLEFAR-LESKADARVSD----LSGGMKRRLT 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 274 IARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHG-KICEHGTHE 346
Cdd:PRK13536  183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPHA 258
cbiO PRK13642
energy-coupling factor transporter ATPase;
122-349 8.68e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 102.09  E-value: 8.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNpVW-LRSKI 200
Cdd:PRK13642    5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN-VWnLRRKI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQEP--VLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAEFIrsfpqGFDTvvgEKGILLSGGQKQRIAIARAL 278
Cdd:PRK13642   84 GMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML-----DFKT---REPARLSGGQKQRVAVAGII 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907190441 279 LKNPKILLLDEATSALD----AENEHLVQEALDRLMegRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELL 349
Cdd:PRK13642  156 ALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
cbiO PRK13643
energy-coupling factor transporter ATPase;
122-349 1.33e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 102.12  E-value: 1.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTY-PARPEVS-VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDghDI--------RQL 191
Cdd:PRK13643    2 IKFEKVNYTYqPNSPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstskqKEI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 192 NPVwlRSKIGTVSQEP--VLFSCSVAENIAYGADNLsSVTAQQVERAAevANAAEFIrsfpqGFDTVVGEKGIL-LSGGQ 268
Cdd:PRK13643   80 KPV--RKKVGVVFQFPesQLFEETVLKDVAFGPQNF-GIPKEKAEKIA--AEKLEMV-----GLADEFWEKSPFeLSGGQ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 269 KQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHE 346
Cdd:PRK13643  150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPS 229


                  ...
gi 1907190441 347 ELL 349
Cdd:PRK13643  230 DVF 232
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 124-339 1.50e-24

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: 1.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 124 FRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhDIRqlnpvwlrskIGTV 203
Cdd:COG0488     1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 204 SQEPVLFS-CSVAENIAYGADNLSSVTAQQVE--------------------------------RAAEVANAAEFIRSFp 250
Cdd:COG0488    67 PQEPPLDDdLTVLDTVLDGDAELRALEAELEEleaklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPEED- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 251 qgFDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-----EHLVQEaldrlmEGrTVLIIAH-R--L 322
Cdd:COG0488   146 --LDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNY------PG-TVLVVSHdRyfL 212

                         250
                  ....*....|....*..
gi 1907190441 323 STIknANFVAVLDHGKI 339
Cdd:COG0488   213 DRV--ATRILELDRGKL 227
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 138-352 1.70e-24

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 101.33  E-value: 1.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 138 SVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDP-----NSGTVSLDGHDIRQLNPVW-LRSKIGTVSQEPVLFS 211
Cdd:PRK14271   35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLeFRRRVGMLFQRPNPFP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 212 CSVAENIAYGAdnlssvtaqqveRAAEVANAAEFiRSFPQGFDTVVG----------EKGILLSGGQKQRIAIARALLKN 281
Cdd:PRK14271  115 MSIMDNVLAGV------------RAHKLVPRKEF-RGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVN 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907190441 282 PKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELLLKP 352
Cdd:PRK14271  182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSSP 253
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 122-349 1.91e-24

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: 99.14  E-value: 1.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFtypARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRL--YDPNSGTVSLDGHDIRQLnPVWLRSK 199
Cdd:cd03217     1 LEIKDLHV---SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDL-PPEERAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IG-TVS-QEPVLFScsvaeniaygadnlssvtaqqveraaEVANAaEFIRSFPQGFdtvvgekgillSGGQKQRIAIARA 277
Cdd:cd03217    77 LGiFLAfQYPPEIP--------------------------GVKNA-DFLRYVNEGF-----------SGGEKKRNEILQL 118

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907190441 278 LLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAH--RLSTIKNANFVAVLDHGKICEHGTHEELL 349
Cdd:cd03217   119 LLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELAL 193
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 136-352 2.02e-24

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 103.38  E-value: 2.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 136 EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVL-FSCSV 214
Cdd:PRK09536   15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 215 AENIAYGA-------DNLSSVTAQQVERAAEVANAAEFIrsfPQGFDTvvgekgilLSGGQKQRIAIARALLKNPKILLL 287
Cdd:PRK09536   95 RQVVEMGRtphrsrfDTWTETDRAAVERAMERTGVAQFA---DRPVTS--------LSGGERQRVLLARALAQATPVLLL 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 288 DEATSALDAenEHLVQ--EALDRLME-GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELLLKP 352
Cdd:PRK09536  164 DEPTASLDI--NHQVRtlELVRRLVDdGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTAD 230
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
131-334 3.06e-24

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 98.46  E-value: 3.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 131 YPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHdiRQLNPVWLRSKIgtvsqePVLF 210
Cdd:NF040873    2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAYVPQRSEV------PDSL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 211 SCSVAENIAYGA-------DNLSSVTAQQVERAAEVANAAEFIRsfpQGFDTvvgekgilLSGGQKQRIAIARALLKNPK 283
Cdd:NF040873   71 PLTVRDLVAMGRwarrglwRRLTRDDRAAVDDALERVGLADLAG---RQLGE--------LSGGQRQRALLAQGLAQEAD 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907190441 284 ILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKNANFVAVL 334
Cdd:NF040873  140 LLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
136-367 3.36e-24

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 100.04  E-value: 3.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 136 EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIR-------QLNPV------WLRSKIGT 202
Cdd:PRK10619   17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVAdknqlrLLRTRLTM 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 203 VSQEPVLFS-CSVAENIAYGADNLSSVTAQQV-ERAAEVANAAefirsfpqGFD-TVVGEKGILLSGGQKQRIAIARALL 279
Cdd:PRK10619   97 VFQHFNLWShMTVLENVMEAPIQVLGLSKQEArERAVKYLAKV--------GIDeRAQGKYPVHLSGGQQQRVSIARALA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 280 KNPKILLLDEATSALDAEnehLVQEALdRLM-----EGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPn 353
Cdd:PRK10619  169 MEPEVLLFDEPTSALDPE---LVGEVL-RIMqqlaeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNP- 243

                         250
                  ....*....|....
gi 1907190441 354 glyrKLMNKQSFLS 367
Cdd:PRK10619  244 ----QSPRLQQFLK 253
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 122-351 3.39e-24

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 99.76  E-value: 3.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHftypARPE-VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLL--RLYDPNSGTVSLDGHDIRQLnPVWLRS 198
Cdd:COG0396     1 LEIKNLH----VSVEgKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILEL-SPDERA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 199 K--IGTVSQEPVLFS-CSVAE--NIAYGADNLSSVTAQQV-----ERAAEVANAAEFI-RSFPQGFdtvvgekgillSGG 267
Cdd:COG0396    76 RagIFLAFQYPVEIPgVSVSNflRTALNARRGEELSAREFlkllkEKMKELGLDEDFLdRYVNEGF-----------SGG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 268 QKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAH--RLSTIKNANFVAVLDHGKICEHGT 344
Cdd:COG0396   145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224


                  ....*..
gi 1907190441 345 hEELLLK 351
Cdd:COG0396   225 -KELALE 230
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 121-348 7.06e-24

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 100.18  E-value: 7.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARPEVsvfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNpvwlRSKI 200
Cdd:COG4152     1 MLELKGLTKRFGDKTAV---DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQEPVLF-SCSVAENIAYGADnLSSVTAQQVERAA-------EVANAAefirsfpqgfDTVVGEkgilLSGGQKQRI 272
Cdd:COG4152    74 GYLPEERGLYpKMKVGEQLVYLAR-LKGLSKAEAKRRAdewlerlGLGDRA----------NKKVEE----LSKGNQQKV 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441 273 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEEL 348
Cdd:COG4152   139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 133-320 9.24e-24

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: 98.11  E-value: 9.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 133 ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKST---VVSLLLRLYDPNSGTVSLDGhdiRQLNPVWLRSKIGTVSQEPVL 209
Cdd:cd03234    16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDIL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 210 FSC-SVAENIAYGADNLSSVTAQQVERAAEVAnaaefIRSFPQGFDTVVGE---KGIllSGGQKQRIAIARALLKNPKIL 285
Cdd:cd03234    93 LPGlTVRETLTYTAILRLPRKSSDAIRKKRVE-----DVLLRDLALTRIGGnlvKGI--SGGERRRVSIAVQLLWDPKVL 165

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907190441 286 LLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAH 320
Cdd:cd03234   166 ILDEPTSGLDSFTALNLVSTLSQLArRNRIVILTIH 201
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
122-320 9.41e-24

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 102.88  E-value: 9.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPE-VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---- 196
Cdd:PRK10535    5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 197 RSKIGTVSQEPVLFS-CSVAENIAYGADNLSSVTAQQVERAAEVANAAefirsfpqGFDTVVGEKGILLSGGQKQRIAIA 275
Cdd:PRK10535   85 REHFGFIFQRYHLLShLTAAQNVEVPAVYAGLERKQRLLRAQELLQRL--------GLEDRVEYQPSQLSGGQQQRVSIA 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907190441 276 RALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAH 320
Cdd:PRK10535  157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTH 202
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 136-320 2.63e-23

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: 96.73  E-value: 2.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 136 EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH----DIRQLNPVWL----RSKIGTVSQ-- 205
Cdd:COG4778    23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPREIlalrRRTIGYVSQfl 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 206 -------------EPVLfscsvaeniaygadnlssvtAQQVERAAEVANAAEFIRSF----------PQGFdtvvgekgi 262
Cdd:COG4778   103 rviprvsaldvvaEPLL--------------------ERGVDREEARARARELLARLnlperlwdlpPATF--------- 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 263 llSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAH 320
Cdd:COG4778   154 --SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKaRGTAIIGIFH 210
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
143-349 2.71e-23

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 96.96  E-value: 2.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 143 FSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwlRSKIGTVSQEPVLFS-CSVAENIAYG 221
Cdd:PRK10771   18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 222 AD---NLSSVTAQQVERAAEVANAAEFIRSFPqgfdtvvGEkgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAEn 298
Cdd:PRK10771   96 LNpglKLNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPA- 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190441 299 ehLVQEALDRLME-----GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELL 349
Cdd:PRK10771  164 --LRQEMLTLVSQvcqerQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
cbiO PRK13644
energy-coupling factor transporter ATPase;
122-353 2.83e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 97.75  E-value: 2.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYParPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTV---SLDGHDIRQLNPVwlRS 198
Cdd:PRK13644    2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsGIDTGDFSKLQGI--RK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 199 KIGTVSQEP--VLFSCSVAENIAYGADNL---SSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIA 273
Cdd:PRK13644   78 LVGIVFQNPetQFVGRTVEEDLAFGPENLclpPIEIRKRVDRALAEIGLEKYRHRSPKT-----------LSGGQGQCVA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 274 IARALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKP 352
Cdd:PRK13644  147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226


                  .
gi 1907190441 353 N 353
Cdd:PRK13644  227 S 227
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
121-332 6.82e-23

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 96.31  E-value: 6.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdIRQLNPVWLRski 200
Cdd:PRK11248    1 MLQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG--KPVEGPGAER--- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQ-EPVLFSCSVAENIAYGadnlssVTAQQVERAAEVANAAEFIRSFP-QGFdtvvGEKGIL-LSGGQKQRIAIARA 277
Cdd:PRK11248   73 GVVFQnEGLLPWRNVQDNVAFG------LQLAGVEKMQRLEIAHQMLKKVGlEGA----EKRYIWqLSGGQRQRVGIARA 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190441 278 LLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHrlsTIKNANFVA 332
Cdd:PRK11248  143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH---DIEEAVFMA 196
cbiO PRK13646
energy-coupling factor transporter ATPase;
122-348 7.22e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 97.16  E-value: 7.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTY-PARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI------RQLNP 193
Cdd:PRK13646    3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkdKYIRP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 194 VwlRSKIGTVSQ--EPVLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAEFIRSfpqgfdtVVGEKGILLSGGQKQR 271
Cdd:PRK13646   83 V--RKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRD-------VMSQSPFQMSGGQMRK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 272 IAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM--EGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEEL 348
Cdd:PRK13646  154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
145-347 8.48e-23

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 98.02  E-value: 8.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 145 LSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH---DIRQlnPVWL---RSKIGTVSQEPVLFS-CSVAEN 217
Cdd:PRK11144   19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEK--GICLppeKRRIGYVFQDARLFPhYKVRGN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 218 IAYGADnlssvtaqqveraaevanaaefiRSFPQGFDTVVGEKGI---------LLSGGQKQRIAIARALLKNPKILLLD 288
Cdd:PRK11144   97 LRYGMA-----------------------KSMVAQFDKIVALLGIeplldrypgSLSGGEKQRVAIGRALLTAPELLLMD 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907190441 289 EATSALDAENEHLVQEALDRLmeGRTV----LIIAHRLSTI-KNANFVAVLDHGKICEHGTHEE 347
Cdd:PRK11144  154 EPLASLDLPRKRELLPYLERL--AREInipiLYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
124-356 1.37e-22

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 97.79  E-value: 1.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 124 FRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwlRSKIGTV 203
Cdd:PRK11000    6 LRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 204 SQEPVLFS-CSVAENIAYG---ADNLSSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALL 279
Cdd:PRK11000   81 FQSYALYPhLSVAENMSFGlklAGAKKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 280 KNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAH-RLSTIKNANFVAVLDHGKICEHGtheelllKPNGLY 356
Cdd:PRK11000  150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG-------KPLELY 222
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 138-349 5.97e-22

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: 98.06  E-value: 5.97e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  138 SVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDpNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAEN 217
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN 1311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  218 IaygaDNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 297
Cdd:TIGR01271 1312 L----DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPV 1387

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907190441  298 NEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELL 349
Cdd:TIGR01271 1388 TLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 122-320 6.03e-22

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 97.06  E-value: 6.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLdGHDIrqlnpvwlrsKIG 201
Cdd:COG0488   316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIG 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLFSC--SVAENIAYGADNLSSVTaqqveraaevanaaefIRSFPQGF-------DTVVGEkgilLSGGQKQRI 272
Cdd:COG0488   382 YFDQHQEELDPdkTVLDELRDGAPGGTEQE----------------VRGYLGRFlfsgddaFKPVGV----LSGGEKARL 441

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907190441 273 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRLmEGrTVLIIAH 320
Cdd:COG0488   442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSH 487
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 138-349 7.13e-22

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: 94.15  E-value: 7.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 138 SVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDpNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAEN 217
Cdd:cd03289    18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 218 IaygaDNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 297
Cdd:cd03289    97 L----DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907190441 298 NEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELL 349
Cdd:cd03289   173 TYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 122-343 8.07e-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: 92.34  E-value: 8.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNpvwlRSKIG 201
Cdd:cd03269     1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQEPVLF-SCSVAENIAYGADnLSSVTAQQveraaevanAAEFIRSFPQGFDTVVGEKGIL--LSGGQKQRIAIARAL 278
Cdd:cd03269    74 YLPEERGLYpKMKVIDQLVYLAQ-LKGLKKEE---------ARRRIDEWLERLELSEYANKRVeeLSKGNQQKVQFIAAV 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190441 279 LKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHG 343
Cdd:cd03269   144 IHDPELLILDEPFSGLDPVNVELLKDVIRELARaGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 121-364 1.05e-21

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 92.84  E-value: 1.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYP-------------------ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTV 181
Cdd:COG1134     4 MIEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 182 SLDGhdirqlNPVWLrskIG-TVSQEPVLfscSVAENI-----AYGadnlssVTAQQV-ERAAEVANAAEfIRSFpqgFD 254
Cdd:COG1134    84 EVNG------RVSAL---LElGAGFHPEL---TGRENIylngrLLG------LSRKEIdEKFDEIVEFAE-LGDF---ID 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 255 TVVGekgiLLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneHLVQEALDRLME----GRTVLIIAHRLSTIKN-AN 329
Cdd:COG1134   142 QPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDA---AFQKKCLARIRElresGRTVIFVSHSMGAVRRlCD 214

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907190441 330 FVAVLDHGKICEHGTHEELLlkpnGLYRKLMNKQS 364
Cdd:COG1134   215 RAIWLEKGRLVMDGDPEEVI----AAYEALLAGRE 245
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
138-349 1.37e-21

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 93.13  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 138 SVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVL-FSCSVAE 216
Cdd:PRK10253   21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 217 NIA---YGADNLSSVTAQQVERAAEVANAAEFIRSFP-QGFDTvvgekgilLSGGQKQRIAIARALLKNPKILLLDEATS 292
Cdd:PRK10253  101 LVArgrYPHQPLFTRWRKEDEEAVTKAMQATGITHLAdQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTT 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 293 ALDAENEHLVQEALDRL--MEGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELL 349
Cdd:PRK10253  173 WLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 116-343 1.38e-21

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: 91.83  E-value: 1.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 116 KTFQGALEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdirqlNPVW 195
Cdd:cd03220    14 KGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 196 LrskIG-TVSQEPVLfscSVAENI-----AYGADNlssvtaqqveraAEVANAAEFIRSF---PQGFDTVVGEkgilLSG 266
Cdd:cd03220    88 L---LGlGGGFNPEL---TGRENIylngrLLGLSR------------KEIDEKIDEIIEFselGDFIDLPVKT----YSS 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 267 GQKQRIAIARALLKNPKILLLDEATSALDAeneHLVQEALDRLME----GRTVLIIAHRLSTIKN-ANFVAVLDHGKICE 341
Cdd:cd03220   146 GMKARLAFAIATALEPDILLIDEVLAVGDA---AFQEKCQRRLREllkqGKTVILVSHDPSSIKRlCDRALVLEKGKIRF 222


                  ..
gi 1907190441 342 HG 343
Cdd:cd03220   223 DG 224
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 122-360 1.43e-21

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 95.93  E-value: 1.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARP--------EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYdPNSGTVSLDGHDIRQLNP 193
Cdd:PRK15134  276 LDVEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 194 ---VWLRSKIGTVSQEPvlFSC-----SVAENIAYGAD-NLSSVTAQQVERA-----AEVANAAEFIRSFPQGFdtvvge 259
Cdd:PRK15134  355 rqlLPVRHRIQVVFQDP--NSSlnprlNVLQIIEEGLRvHQPTLSAAQREQQviavmEEVGLDPETRHRYPAEF------ 426

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 260 kgillSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTV--LIIAHRLSTIKN-ANFVAVLDH 336
Cdd:PRK15134  427 -----SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQ 501

                         250       260
                  ....*....|....*....|....*
gi 1907190441 337 GKICEHGTHEELLLKPNGLY-RKLM 360
Cdd:PRK15134  502 GEVVEQGDCERVFAAPQQEYtRQLL 526
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 139-365 1.59e-21

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: 93.38  E-value: 1.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 139 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdirqlnpvwlrsKIGTVSQEPVLFSCSVAENI 218
Cdd:cd03291    52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 219 AYGADN-----LSSVTAQQVEraaevanaaEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSA 293
Cdd:cd03291   119 IFGVSYdeyryKSVVKACQLE---------EDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGY 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907190441 294 LDAENEHLVQEA-LDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGLYRKLMNKQSF 365
Cdd:cd03291   190 LDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTF 262
cbiO PRK13645
energy-coupling factor transporter ATPase;
117-362 2.68e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 92.76  E-value: 2.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 117 TFQGALEFRNVHFTYPARP--EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH----DIRQ 190
Cdd:PRK13645    2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipaNLKK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 191 LNPVW-LRSKIGTVSQEP--VLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAEFIRSFpqgfdtvVGEKGILLSGG 267
Cdd:PRK13645   82 IKEVKrLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDY-------VKRSPFELSGG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 268 QKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTI-KNANFVAVLDHGKICEHG- 343
Cdd:PRK13645  155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGs 234

                         250       260
                  ....*....|....*....|....*...
gi 1907190441 344 -----THEELLLK----PNGLYrKLMNK 362
Cdd:PRK13645  235 pfeifSNQELLTKieidPPKLY-QLMYK 261
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 139-368 5.62e-21

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: 94.98  E-value: 5.62e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  139 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdirqlnpvwlrsKIGTVSQEPVLFSCSVAENI 218
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  219 AYGADN-----LSSVTAQQVEraaevanaaEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSA 293
Cdd:TIGR01271  508 IFGLSYdeyryTSVIKACQLE---------EDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTH 578

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441  294 LDAENEHLVQEA-LDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGLYRKLMNKQSFLSY 368
Cdd:TIGR01271  579 LDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAFDNF 654
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 141-320 5.89e-21

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


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 90.60  E-value: 5.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 141 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLrskigTVSQEPVLFS-CSVAENIA 219
Cdd:TIGR01184   2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENIA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 220 YGADNLSSvTAQQVERAAEVANAAEFIrsfpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENE 299
Cdd:TIGR01184  77 LAVDRVLP-DLSKSERRAIVEEHIALV-----GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150

                         170       180
                  ....*....|....*....|...
gi 1907190441 300 HLVQEALDRLME--GRTVLIIAH 320
Cdd:TIGR01184 151 GNLQEELMQIWEehRVTVLMVTH 173
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
 3-94 8.43e-21

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: 91.54  E-value: 8.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFY 82
Cdd:cd18780   203 EVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLY 282

                          90
                  ....*....|..
gi 1907190441  83 SELMKGLGAGGR 94
Cdd:cd18780   283 GDFMQAVGASVR 294
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 122-339 1.08e-20

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 90.12  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARpevSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVsLDG----HDIRQlnpvwlr 197
Cdd:PRK11247   13 LLLNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGtaplAEARE------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 198 sKIGTVSQEPVLFSC-SVAENIAYGadnLSSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIAR 276
Cdd:PRK11247   82 -DTRLMFQDARLLPWkKVIDNVGLG---LKGQWRDAALQALAAVGLADRANEWPAA-----------LSGGQKQRVALAR 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 277 ALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLS-TIKNANFVAVLDHGKI 339
Cdd:PRK11247  147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 128-339 1.18e-20

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


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 89.70  E-value: 1.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 128 HFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHD--IRQLNpvwLRSKIGTV-- 203
Cdd:cd03267    25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwKRRKK---FLRRIGVVfg 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 204 SQEPVLFSCSVAENIAYGAD--NLSSVTAQQ-VERAAEVANAAEFIrsfpqgfDTVVGEkgilLSGGQKQRIAIARALLK 280
Cdd:cd03267   102 QKTQLWWDLPVIDSFYLLAAiyDLPPARFKKrLDELSELLDLEELL-------DTPVRQ----LSLGQRMRAEIAAALLH 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907190441 281 NPKILLLDEATSALDAENEHLVQEALDRLMEGR--TVLIIAHRLSTI-KNANFVAVLDHGKI 339
Cdd:cd03267   171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRL 232
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 122-348 1.66e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 90.92  E-value: 1.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARP--EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSL---DGHDIRQLNPVW- 195
Cdd:PRK13651    3 IKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEk 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 196 --------------------LRSKIGTVSQ--EPVLFSCSVAENIAYGADNLSSVTAQQVERAAE----VANAAEFIRSF 249
Cdd:PRK13651   83 vleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKyielVGLDESYLQRS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 250 PqgFDtvvgekgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAENehlVQEALDRL----MEGRTVLIIAHRL-ST 324
Cdd:PRK13651  163 P--FE---------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQG---VKEILEIFdnlnKQGKTIILVTHDLdNV 228

                         250       260
                  ....*....|....*....|....*
gi 1907190441 325 IKNANFVAVLDHGKICEHG-THEEL 348
Cdd:PRK13651  229 LEWTKRTIFFKDGKIIKDGdTYDIL 253
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
122-372 1.75e-20

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 89.90  E-value: 1.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTY------PARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH--------- 186
Cdd:COG4167     5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdyky 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 187 ---DIR--------QLNPvwlRSKIGTVSQEPVLFScsvaeniaygadnlSSVTAQqvERAAEVANA----------AEF 245
Cdd:COG4167    85 rckHIRmifqdpntSLNP---RLNIGQILEEPLRLN--------------TDLTAE--EREERIFATlrlvgllpehANF 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 246 irsFPQgfdtvvgekgiLLSGGQKQRIAIARALLKNPKILLLDEATSALDAE------NEHL-VQEALdrlmeGRTVLII 318
Cdd:COG4167   146 ---YPH-----------MLSSGQKQRVALARALILQPKIIIADEALAALDMSvrsqiiNLMLeLQEKL-----GISYIYV 206

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 319 AHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKP-NGLYRKLMNKQsFLSYNGAE 372
Cdd:COG4167   207 SQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFANPqHEVTKRLIESH-FGEALTAD 261
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 139-349 2.79e-20

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 88.80  E-value: 2.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 139 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnPVWLRSK--IGTVSQEPVLFS-CSVA 215
Cdd:PRK10895   18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL-PLHARARrgIGYLPQEASIFRrLSVY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 216 ENIAYGADNLSSVTAQQVERAAEvanaaEFIRSFpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALD 295
Cdd:PRK10895   97 DNLMAVLQIRDDLSAEQREDRAN-----ELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 296 AENEHLVQEALDRLME-GRTVLIIAHRL-STIKNANFVAVLDHGKICEHGTHEELL 349
Cdd:PRK10895  170 PISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 122-320 4.59e-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: 85.58  E-value: 4.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdirqlnpvwlrskig 201
Cdd:cd03221     1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 tvsqepvlfscsvAENIAYgadnlssvtaqqveraaevanaaefirsFPQgfdtvvgekgilLSGGQKQRIAIARALLKN 281
Cdd:cd03221    62 -------------TVKIGY----------------------------FEQ------------LSGGEKMRLALAKLLLEN 88

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907190441 282 PKILLLDEATSALDAENEHLVQEALDRLmeGRTVLIIAH 320
Cdd:cd03221    89 PNLLLLDEPTNHLDLESIEALEEALKEY--PGTVILVSH 125
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
121-296 7.60e-20

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 89.52  E-value: 7.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVHFTYPARpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLR----LYDPNSGTVSLDGHDIRQLNPVwL 196
Cdd:PRK11650    3 GLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKST----LLRmvagLERITSGEIWIGGRVVNELEPA-D 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 197 RSkIGTVSQEPVLFS-CSVAENIAYGADNLSSVTAQQVERAAEVANAAEfIRSFPQgfdtvvgEKGILLSGGQKQRIAIA 275
Cdd:PRK11650   76 RD-IAMVFQNYALYPhMSVRENMAYGLKIRGMPKAEIEERVAEAARILE-LEPLLD-------RKPRELSGGQRQRVAMG 146

                         170       180
                  ....*....|....*....|.
gi 1907190441 276 RALLKNPKILLLDEATSALDA 296
Cdd:PRK11650  147 RAIVREPAVFLFDEPLSNLDA 167
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
119-325 7.83e-20

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 90.74  E-value: 7.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 119 QGALEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV-WLR 197
Cdd:PRK11288    2 SPYLSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 198 SKIGTVSQE----PVLfscSVAENIAYGAdnLSSvTAQQVERAAEVANAAEFIRSFPQGFD--TVVGEkgilLSGGQKQR 271
Cdd:PRK11288   79 AGVAIIYQElhlvPEM---TVAENLYLGQ--LPH-KGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQM 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 272 IAIARALLKNPKILLLDEATSALDA-ENEHLVQeALDRLM-EGRTVLIIAHRLSTI 325
Cdd:PRK11288  149 VEIAKALARNARVIAFDEPTSSLSArEIEQLFR-VIRELRaEGRVILYVSHRMEEI 203
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
129-349 9.28e-20

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 88.14  E-value: 9.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 129 FTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH--DIRQLNPVWLRSKIGTVSQE 206
Cdd:PRK13638    9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 207 P--VLFSCSVAENIAYGADNL---SSVTAQQVERAAEVANAAEFIRSFPQgfdtvvgekgiLLSGGQKQRIAIARALLKN 281
Cdd:PRK13638   86 PeqQIFYTDIDSDIAFSLRNLgvpEAEITRRVDEALTLVDAQHFRHQPIQ-----------CLSHGQKKRVAIAGALVLQ 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 282 PKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 349
Cdd:PRK13638  155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVF 224
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 144-360 1.43e-19

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 88.61  E-value: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 144 SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV-WL--RSKIGTVSQEPvLFSC----SVAE 216
Cdd:PRK15079   41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDeWRavRSDIQMIFQDP-LASLnprmTIGE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 217 NIAygaDNLSS----VTAQQVE---RA--AEVANAAEFIRSFPQGFdtvvgekgillSGGQKQRIAIARALLKNPKILLL 287
Cdd:PRK15079  120 IIA---EPLRTyhpkLSRQEVKdrvKAmmLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPKLIIC 185

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 288 DEATSALD----AENEHLVQEaLDRLMeGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPNGLYRK-LM 360
Cdd:PRK15079  186 DEPVSALDvsiqAQVVNLLQQ-LQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLHPYTKaLM 262
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
139-323 1.49e-19

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 86.41  E-value: 1.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 139 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQL---NPVWLRS-KIGTVSQ-EPVLFSCS 213
Cdd:PRK11629   24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNqKLGFIYQfHHLLPDFT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 214 VAENIAYGADNLSSVTAQQVERAAEVANAAefirsfpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSA 293
Cdd:PRK11629  104 ALENVAMPLLIGKKKPAEINSRALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907190441 294 LDAENEHLVQEALDRL--MEGRTVLIIAHRLS 323
Cdd:PRK11629  176 LDARNADSIFQLLGELnrLQGTAFLVVTHDLQ 207
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 122-352 4.15e-19

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 85.91  E-value: 4.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFtYPARPEVSvfqDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN----SGTVSLDGhdiRQLNPVWLR 197
Cdd:PRK10418    5 IELRNIAL-QAAQPLVH---GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDG---KPVAPCALR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 198 SK-IGTVSQEPVLFSCSVAENIAYGADNLSSV-------TAQQVERAAEVANAAEFIRSFPqgFDtvvgekgilLSGGQK 269
Cdd:PRK10418   78 GRkIATIMQNPRSAFNPLHTMHTHARETCLALgkpaddaTLTAALEAVGLENAARVLKLYP--FE---------MSGGML 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 270 QRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRT--VLIIAHRLSTI-KNANFVAVLDHGKICEHGTHE 346
Cdd:PRK10418  147 QRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVE 226


                  ....*.
gi 1907190441 347 ELLLKP 352
Cdd:PRK10418  227 TLFNAP 232
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 3-95 6.31e-19

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: 86.00  E-value: 6.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFY 82
Cdd:cd18576   197 EIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLY 276

                          90
                  ....*....|...
gi 1907190441  83 SELMKGLGAGGRL 95
Cdd:cd18576   277 GQLQKALGASERV 289
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
115-349 1.01e-18

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 84.84  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 115 EKTFQgaleFRNVHFTYPARpevSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV 194
Cdd:PRK10575    9 DTTFA----LRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 195 WLRSKIGTVSQE-PVLFSCSVAENIAYGA-------DNLSSVTAQQVERAAevanaaefirsfpqgfdTVVGEKGIL--- 263
Cdd:PRK10575   82 AFARKVAYLPQQlPAAEGMTVRELVAIGRypwhgalGRFGAADREKVEEAI-----------------SLVGLKPLAhrl 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 264 ---LSGGQKQRIAIARALLKNPKILLLDEATSALDAenEHLVQealdrlmegrtVLIIAHRLSTIKNANFVAVL------ 334
Cdd:PRK10575  145 vdsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI--AHQVD-----------VLALVHRLSQERGLTVIAVLhdinma 211

                         250       260
                  ....*....|....*....|....*
gi 1907190441 335 ----DH------GKICEHGTHEELL 349
Cdd:PRK10575  212 arycDYlvalrgGEMIAQGTPAELM 236
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 122-348 1.06e-18

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 87.41  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwLRSKIG 201
Cdd:PRK15439   12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 T--VSQEPVLF-SCSVAENIAYG----ADNLSSVTAQQVERAAEV---ANAAefirsfpqgfdtvvgekgiLLSGGQKQR 271
Cdd:PRK15439   88 IylVPQEPLLFpNLSVKENILFGlpkrQASMQKMKQLLAALGCQLdldSSAG-------------------SLEVADRQI 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 272 IAIARALLKNPKILLLDEATSALD-AENEHLVQEALDRLMEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEEL 348
Cdd:PRK15439  149 VEILRGLMRDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
125-348 1.14e-18

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 87.38  E-value: 1.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 125 RNVHFTYPARP--------EVS------VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQ 190
Cdd:COG1129   239 RELEDLFPKRAaapgevvlEVEglsvggVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRI 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 191 LNPV-WLRSKIGTVS----QEPVLFSCSVAENIAYGadNLSSVT-AQQVERAAEVANAAEFIRSF---PQGFDTVVGEkg 261
Cdd:COG1129   319 RSPRdAIRAGIAYVPedrkGEGLVLDLSIRENITLA--SLDRLSrGGLLDRRRERALAEEYIKRLrikTPSPEQPVGN-- 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 262 ilLSGGQKQRIAIARALLKNPKILLLDEATSALD--AENE--HLVQEALDrlmEGRTVLII----------AHRlstikn 327
Cdd:COG1129   395 --LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAEiyRLIRELAA---EGKAVIVIsselpellglSDR------ 463

                         250       260
                  ....*....|....*....|.
gi 1907190441 328 anfVAVLDHGKICEHGTHEEL 348
Cdd:COG1129   464 ---ILVMREGRIVGELDREEA 481
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 122-360 1.46e-18

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 87.22  E-value: 1.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARP--------EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI----- 188
Cdd:PRK10261  314 LQVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlsp 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 189 RQLNPvwLRSKIGTVSQEPVLfSCSVAENIAYG------------ADNLSSVTAQQVERaaeVANAAEFIRSFPQGFdtv 256
Cdd:PRK10261  394 GKLQA--LRRDIQFIFQDPYA-SLDPRQTVGDSimeplrvhgllpGKAAAARVAWLLER---VGLLPEHAWRYPHEF--- 464

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 257 vgekgillSGGQKQRIAIARALLKNPKILLLDEATSALDAE-NEHLVQEALDRLME-GRTVLIIAHRLSTIKN-ANFVAV 333
Cdd:PRK10261  465 --------SGGQRQRICIARALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAV 536

                         250       260
                  ....*....|....*....|....*...
gi 1907190441 334 LDHGKICEHGTHEELLLKPNGLY-RKLM 360
Cdd:PRK10261  537 MYLGQIVEIGPRRAVFENPQHPYtRKLM 564
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 139-339 1.62e-18

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: 82.48  E-value: 1.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 139 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP-VWLRSKIGTVSQEP----VLFSCS 213
Cdd:cd03215    15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 214 VAENIAYGadnlssvtaqqveraaevanaaefirsfpqgfdtvvgekgILLSGGQKQRIAIARALLKNPKILLLDEATSA 293
Cdd:cd03215    95 VAENIALS----------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRG 134

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907190441 294 LDAENEHLVQEALDRL-MEGRTVLIIahrlST-----IKNANFVAVLDHGKI 339
Cdd:cd03215   135 VDVGAKAEIYRLIRELaDAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 133-320 1.85e-18

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 83.00  E-value: 1.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 133 ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQ-EPVLfs 211
Cdd:PRK13539   11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAmKPAL-- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 212 cSVAENIAYGADNLSSvtaqqveRAAEVANAAEFIrsfpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEAT 291
Cdd:PRK13539   89 -TVAENLEFWAAFLGG-------EELDIAAALEAV-----GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155

                         170       180       190
                  ....*....|....*....|....*....|
gi 1907190441 292 SALDAENEHLVQEAL-DRLMEGRTVLIIAH 320
Cdd:PRK13539  156 AALDAAAVALFAELIrAHLAQGGIVIAATH 185
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
135-326 2.65e-18

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 86.38  E-value: 2.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 135 PEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP-VWLRSKIGTVSQE-PVLFSC 212
Cdd:PRK09700   16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHkLAAQLGIGIIYQElSVIDEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 213 SVAENIAYGADNLSSVTAQQV-------ERAAEVANAAEFIRSfpqgFDTVVGEkgilLSGGQKQRIAIARALLKNPKIL 285
Cdd:PRK09700   96 TVLENLYIGRHLTKKVCGVNIidwremrVRAAMMLLRVGLKVD----LDEKVAN----LSISHKQMLEIAKTLMLDAKVI 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907190441 286 LLDEATSAL-DAENEHLVQeALDRLM-EGRTVLIIAHRLSTIK 326
Cdd:PRK09700  168 IMDEPTSSLtNKEVDYLFL-IMNQLRkEGTAIVYISHKLAEIR 209
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
140-345 5.16e-18

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 81.84  E-value: 5.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 140 FQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV---WLRSKIGTVSQEP-VLFSCSVA 215
Cdd:PRK10908   18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRRQIGMIFQDHhLLMDRTVY 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 216 ENIAY-----GADnlSSVTAQQVERAAEVANAAEFIRSFPqgfdtvvgekgILLSGGQKQRIAIARALLKNPKILLLDEA 290
Cdd:PRK10908   98 DNVAIpliiaGAS--GDDIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADEP 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907190441 291 TSALDAEnehlVQEALDRLME-----GRTVLIIAHRLSTIKNANF-VAVLDHGKIceHGTH 345
Cdd:PRK10908  165 TGNLDDA----LSEGILRLFEefnrvGVTVLMATHDIGLISRRSYrMLTLSDGHL--HGGV 219
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 139-361 1.20e-17

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 84.37  E-value: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 139 VFQDFSLSIPSGSVTALVGPSGSGKS-TVVSLLLRLYDPN----SGTVSLDGHDIRQLNPVWLR----SKIGTVSQEPV- 208
Cdd:PRK15134   24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMv 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 209 -LFSCSVAENIAYGADNLSSVTAQQVERAAEVA--------NAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALL 279
Cdd:PRK15134  104 sLNPLHTLEKQLYEVLSLHRGMRREAARGEILNcldrvgirQAAKRLTDYPHQ-----------LSGGERQRVMIAMALL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 280 KNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPNGLY 356
Cdd:PRK15134  173 TRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAPTHPY 252


                  ....*.
gi 1907190441 357 -RKLMN 361
Cdd:PRK15134  253 tQKLLN 258
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
122-348 1.63e-17

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 81.74  E-value: 1.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTypaRPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---RS 198
Cdd:PRK11831    8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 199 KIGTVSQEPVLFS-CSVAENIAY--------GADNLSSVTAQQVErAAEVANAAEFIRSfpqgfdtvvgekgiLLSGGQK 269
Cdd:PRK11831   85 RMSMLFQSGALFTdMNVFDNVAYplrehtqlPAPLLHSTVMMKLE-AVGLRGAAKLMPS--------------ELSGGMA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 270 QRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHE 346
Cdd:PRK11831  150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQ 229


                  ..
gi 1907190441 347 EL 348
Cdd:PRK11831  230 AL 231
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 139-321 3.68e-17

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 79.62  E-value: 3.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 139 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLY--DPNSGTVSLDGHDIrqlnpvwlrskigtvSQEpvlfsCSVAE 216
Cdd:COG2401    45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE-----ASLID 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 217 NIAYGADnlssvTAQQVER--AAEVANAAEFIRSFPQgfdtvvgekgilLSGGQKQRIAIARALLKNPKILLLDEATSAL 294
Cdd:COG2401   105 AIGRKGD-----FKDAVELlnAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907190441 295 DAEN----EHLVQEALDRLmeGRTVLIIAHR 321
Cdd:COG2401   168 DRQTakrvARNLQKLARRA--GITLVVATHH 196
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 122-336 3.93e-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: 77.96  E-value: 3.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPA-RPEVSvfqDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHdirqlnpvwlrSKI 200
Cdd:cd03223     1 IELENLSLATPDgRVLLK---DLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GTVSQEPVLFSCSVAENIAYgadnlssvtaqqveraaevanaaefirsfPqgFDTVvgekgilLSGGQKQRIAIARALLK 280
Cdd:cd03223    67 LFLPQRPYLPLGTLREQLIY-----------------------------P--WDDV-------LSGGEQQRLAFARLLLH 108

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 281 NPKILLLDEATSALDAENEHLVQEALDRlmEGRTVLIIAHRLSTIKNANFVAVLDH 336
Cdd:cd03223   109 KPKFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHRPSLWKFHDRVLDLDG 162
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
145-322 4.66e-17

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 80.06  E-value: 4.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 145 LSIPSGSVTALVGPSGSGKSTVVSLLLRLY--DPNSGT-VSLDGH----------DIRQLnpvwlRSKIGTVSQEPVLFS 211
Cdd:PRK09984   25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRtvqregrlarDIRKS-----RANTGYIFQQFNLVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 212 -CSVAENIAYGA--------DNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTvvgekgilLSGGQKQRIAIARALLKNP 282
Cdd:PRK09984  100 rLSVLENVLIGAlgstpfwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVST--------LSGGQQQRVAIARALMQQA 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907190441 283 KILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRL 322
Cdd:PRK09984  172 KVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQV 213
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 134-349 5.14e-17

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 82.40  E-value: 5.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 134 RPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN---SGTVSLDGHDIrqlNPVWLRSKIGTVSQEPVLF 210
Cdd:TIGR00955  35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDLFI 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 211 -SCSVAENIAYGA-----DNLSSVtaQQVERAAEV------ANAAefirsfpqgfDTVVGEKGIL--LSGGQKQRIAIAR 276
Cdd:TIGR00955 112 pTLTVREHLMFQAhlrmpRRVTKK--EKRERVDEVlqalglRKCA----------NTRIGVPGRVkgLSGGERKRLAFAS 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 277 ALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTIKNANF--VAVLDHGKICEHGTHEELL 349
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSELFELFdkIILMAEGRVAYLGSPDQAV 255
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 129-364 8.21e-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: 82.37  E-value: 8.21e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  129 FTYPARPEVSvfqDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIrQLNPVWLRSKIGTVSQEPV 208
Cdd:TIGR01257  938 FEPSGRPAVD---RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNI 1013

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  209 LFS-CSVAENIAYGAD-NLSSVTAQQVERAAEVANAaefirsfpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILL 286
Cdd:TIGR01257 1014 LFHhLTVAEHILFYAQlKGRSWEEAQLEMEAMLEDT---------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  287 LDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTheELLLKP---NGLY----RK 358
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT--PLFLKNcfgTGFYltlvRK 1162


                   ....*.
gi 1907190441  359 LMNKQS 364
Cdd:TIGR01257 1163 MKNIQS 1168
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 116-320 5.52e-16

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: 79.46  E-value: 5.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 116 KTFQgALEFRNVHFTYPARPEVSVFQ--DFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP 193
Cdd:COG4615   323 ADFQ-TLELRGVTYRYPGEDGDEGFTlgPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNR 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 194 VWLRSKIGTVSQEPVLFscsvaeniaygaDNLssvtaQQVERAAEVANAAEFIRSFpqGFDTVVG-EKGIL----LSGGQ 268
Cdd:COG4615   402 EAYRQLFSAVFSDFHLF------------DRL-----LGLDGEADPARARELLERL--ELDHKVSvEDGRFsttdLSQGQ 462

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907190441 269 KQRIAIARALLKNPKILLLDEATSALDAENEHLV-QEALDRLME-GRTVLIIAH 320
Cdd:COG4615   463 RKRLALLVALLEDRPILVFDEWAADQDPEFRRVFyTELLPELKArGKTVIAISH 516
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 121-339 6.25e-16

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 78.92  E-value: 6.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRNVhfTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLR-SK 199
Cdd:COG3845   257 VLEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLG 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQEP-----VLfSCSVAENIA---YGADNLSSvtAQQVERAAEVANAAEFIRSF---PQGFDTVVGekgiLLSGGQ 268
Cdd:COG3845   335 VAYIPEDRlgrglVP-DMSVAENLIlgrYRRPPFSR--GGFLDRKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGN 407

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 269 KQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLII----------AHRlstiknanfVAVLDHG 337
Cdd:COG3845   408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLIsedldeilalSDR---------IAVMYEG 478


                  ..
gi 1907190441 338 KI 339
Cdd:COG3845   479 RI 480
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
 141-331 8.62e-16

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: 76.50  E-value: 8.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 141 QDFSLSIPSGSVTALVGPSGSGKSTVV------SLLLRLYdpNSGTVSLDGHDIRQLNPVwlrSKIGTVSQEPV------ 208
Cdd:cd03271    12 KNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLH--LKKEQPGNHDRIEGLEHI---DKVIVIDQSPIgrtprs 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 209 --------------LFsCSVAE---------NIAYGADNLSSVTAQQVERAAE----VANAAEFIRSFPQ-GFDTV-VGE 259
Cdd:cd03271    87 npatytgvfdeireLF-CEVCKgkrynretlEVRYKGKSIADVLDMTVEEALEffenIPKIARKLQTLCDvGLGYIkLGQ 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 260 KGILLSGGQKQRIAIARALLK---NPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKNANFV 331
Cdd:cd03271   166 PATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWI 241
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
122-349 1.21e-15

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 75.69  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlnpvW-----L 196
Cdd:PRK11614    6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD----WqtakiM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 197 RSKIGTVSQEPVLFS-CSVAENIAYGADNLSSVTAQQ-VERAAEVanaaefirsFPQGFDTVVGEKGILlSGGQKQRIAI 274
Cdd:PRK11614   79 REAVAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQErIKWVYEL---------FPRLHERRIQRAGTM-SGGEQQMLAI 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 275 ARALLKNPKILLLDEATSALDAEnehLVQEALDRLM----EGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELL 349
Cdd:PRK11614  149 GRALMSQPRLLLLDEPSLGLAPI---IIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALL 225
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 144-348 1.97e-15

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 75.41  E-value: 1.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 144 SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnPVWLRSKIGTVS--QEPVLF-SCSVAENI-- 218
Cdd:PRK11300   25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQIARMGVVRtfQHVRLFrEMTVIENLlv 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 219 --------AYGADNLSSVTAQQVERAAeVANAAEFIRSFpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEA 290
Cdd:PRK11300  104 aqhqqlktGLFSGLLKTPAFRRAESEA-LDRAATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907190441 291 TSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEEL 348
Cdd:PRK11300  181 AAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 133-306 2.05e-15

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 74.07  E-value: 2.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 133 ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSC 212
Cdd:cd03231     9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 213 SVAENIAYGADNLSSvtaQQVERAAEVANAAEFirsfpqgFDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATS 292
Cdd:cd03231    89 SVLENLRFWHADHSD---EQVEEALARVGLNGF-------EDRPVAQ----LSAGQQRRVALARLLLSGRPLWILDEPTT 154

                         170
                  ....*....|....
gi 1907190441 293 ALDAENEHLVQEAL 306
Cdd:cd03231   155 ALDKAGVARFAEAM 168
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 143-349 3.10e-15

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 74.49  E-value: 3.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 143 FSLSIPSGSVTALVGPSGSGKSTvvsLLLRLYD--PNSGTVSLDGHDIRQLNPVWLRSKIGTVSQE-PVLFSCSVAENIA 219
Cdd:COG4138    15 ISAQVNAGELIHLIGPNGAGKST---LLARMAGllPGQGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQYLA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 220 -YGADNLSSVTAQQVerAAEVANAAEFI----RSFPQgfdtvvgekgilLSGGQKQRIAIARALLK-----NP--KILLL 287
Cdd:COG4138    92 lHQPAGASSEAVEQL--LAQLAEALGLEdklsRPLTQ------------LSGGEWQRVRLAAVLLQvwptiNPegQLLLL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 288 DEATSALD-AEnehlvQEALDRLME-----GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELL 349
Cdd:COG4138   158 DEPMNSLDvAQ-----QAALDRLLRelcqqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
GguA NF040905
sugar ABC transporter ATP-binding protein;
122-338 3.51e-15

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 76.75  E-value: 3.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYdPN---SGTVSLDG-----HDIRQLNp 193
Cdd:NF040905    2 LEMRGITKTFPG---VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfKDIRDSE- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 194 vwlRSKIGTVSQE----PVLfscSVAENI-------AYGADNLSSVTAQQVERAAEVAnaaefIRSFPqgfDTVVGEKGI 262
Cdd:NF040905   77 ---ALGIVIIHQElaliPYL---SIAENIflgneraKRGVIDWNETNRRARELLAKVG-----LDESP---DTLVTDIGV 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 263 llsgGQKQRIAIARALLKNPKILLLDEATSAL-DAENEHLvqeaLDRLME----GRTVLIIAHRLSTI-KNANFVAVLDH 336
Cdd:NF040905  143 ----GKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAAL----LDLLLElkaqGITSIIISHKLNEIrRVADSITVLRD 214


                  ..
gi 1907190441 337 GK 338
Cdd:NF040905  215 GR 216
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 133-320 4.12e-15

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 73.16  E-value: 4.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 133 ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSC 212
Cdd:TIGR01189   9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 213 SVAENIAYGADNLSSVtaqqvERAAEVANAAEFIRSFPqgfDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATS 292
Cdd:TIGR01189  89 SALENLHFWAAIHGGA-----QRTIEDALAAVGLTGFE---DLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTT 156

                         170       180
                  ....*....|....*....|....*....
gi 1907190441 293 ALDAENEHLVQEAL-DRLMEGRTVLIIAH 320
Cdd:TIGR01189 157 ALDKAGVALLAGLLrAHLARGGIVLLTTH 185
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
137-352 5.87e-15

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 74.94  E-value: 5.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 137 VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN----SGTVSLDGHDIRQLNPV----WLRSKIGTVSQEPV 208
Cdd:COG4170    20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRerrkIIGREIAMIFQEPS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 209 lfSC-----SVAENIAYGADNlSSVTA-------QQVERAAE------VANAAEFIRSFPQGfdtvvgekgilLSGGQKQ 270
Cdd:COG4170   100 --SCldpsaKIGDQLIEAIPS-WTFKGkwwqrfkWRKKRAIEllhrvgIKDHKDIMNSYPHE-----------LTEGECQ 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 271 RIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEE 347
Cdd:COG4170   166 KVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnqLQGTSILLISHDLESISQwADTITVLYCGQTVESGPTEQ 245


                  ....*
gi 1907190441 348 LLLKP 352
Cdd:COG4170   246 ILKSP 250
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 122-346 7.61e-15

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 73.52  E-value: 7.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLL--RLYDPNSGTVSLDGHDIRQLNPVwLRSK 199
Cdd:CHL00131    8 LEIKNLHASVN---ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEPE-ERAH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGT------------VSQEPVLFSCSVAENIAYGADNLSSVTAQQV--ERAAEVANAAEFI-RSFPQGFdtvvgekgill 264
Cdd:CHL00131   84 LGIflafqypieipgVSNADFLRLAYNSKRKFQGLPELDPLEFLEIinEKLKLVGMDPSFLsRNVNEGF----------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 265 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAH--RLSTIKNANFVAVLDHGKICE 341
Cdd:CHL00131  153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIK 232


                  ....*
gi 1907190441 342 HGTHE 346
Cdd:CHL00131  233 TGDAE 237
hmuV PRK13547
heme ABC transporter ATP-binding protein;
126-349 1.27e-14

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 73.32  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 126 NVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLRLY--------DPN----SGTVSLDGHDIRQLNP 193
Cdd:PRK13547    3 TADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKST----LLKALagdltgggAPRgarvTGDVTLNGEPLAAIDA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 194 VWLRSKIGTVSQ--EPVlFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAeFIRSfpqGFDTVVGEKGILLSGGQKQR 271
Cdd:PRK13547   79 PRLARLRAVLPQaaQPA-FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQA-LALA---GATALVGRDVTTLSGGELAR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 272 IAIARALLK---------NPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLS-TIKNANFVAVLDHGKI 339
Cdd:PRK13547  154 VQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAI 233

                         250
                  ....*....|
gi 1907190441 340 CEHGTHEELL 349
Cdd:PRK13547  234 VAHGAPADVL 243
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 149-336 1.78e-14

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: 70.09  E-value: 1.78e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  149 SGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTV-SLDGHDIRQLNPVWLRskigtvsqepvlfscsvaeniaygadnlss 227
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLL------------------------------ 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  228 vtaqqveraaevanaaefirsfpqgfDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALD 307
Cdd:smart00382  51 --------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907190441  308 RLM-------EGRTVLIIAHRLSTIKNANFVAVLDH 336
Cdd:smart00382 105 LRLllllkseKNLTVILTTNDEKDLGPALLRRRFDR 140
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 142-367 2.28e-14

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 72.06  E-value: 2.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 142 DFSLSIPSGS-----VTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIrQLNPVWLRSKI-GTVSqepvlfscsva 215
Cdd:cd03237    12 EFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKADYeGTVR----------- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 216 eniaygaDNLSSVTAQQVERA---AEVANaaefirsfPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATS 292
Cdd:cd03237    80 -------DLLSSITKDFYTHPyfkTEIAK--------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSA 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441 293 ALDAENEHLVQEALDRLMEG--RTVLIIAHRLSTIKN-ANFVAVLDhGKICEHGTheelLLKPNGLyRKLMNKqsFLS 367
Cdd:cd03237   145 YLDVEQRLMASKVIRRFAENneKTAFVVEHDIIMIDYlADRLIVFE-GEPSVNGV----ANPPQSL-RSGMNR--FLK 214
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 140-360 3.10e-14

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 71.88  E-value: 3.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 140 FQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDiRQLNPVW----------LRSKIGTVSQEP-- 207
Cdd:PRK11701   22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD-GQLRDLYalseaerrrlLRTEWGFVHQHPrd 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 208 -VLFSCSVAENI-----AYGADNLSSVTAQQVERAAEVANAAEFIRSFPQGFdtvvgekgillSGGQKQRIAIARALLKN 281
Cdd:PRK11701  101 gLRMQVSAGGNIgerlmAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTF-----------SGGMQQRLQIARNLVTH 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 282 PKILLLDEATSALDAEnehlVQEALDRLMEGRT------VLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPNG 354
Cdd:PRK11701  170 PRLVFMDEPTGGLDVS----VQARLLDLLRGLVrelglaVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVLDDPQH 245


                  ....*.
gi 1907190441 355 LYRKLM 360
Cdd:PRK11701  246 PYTQLL 251
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 141-349 6.06e-14

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 72.04  E-value: 6.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 141 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRsKIGTV----SQ----EPVLFSC 212
Cdd:COG4586    39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQlwwdLPAIDSF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 213 SVAENIaYGADNlsSVTAQQVERAAEVANAAEFIrsfpqgfDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATS 292
Cdd:COG4586   118 RLLKAI-YRIPD--AEYKKRLDELVELLDLGELL-------DTPVRQ----LSLGQRMRCELAAALLHRPKILFLDEPTI 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 293 ALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 349
Cdd:COG4586   184 GLDVVSKEAIREFLKEYNRerGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELK 243
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 136-295 6.48e-14

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 70.58  E-value: 6.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 136 EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP---VWLRSK-IGTVSQEPVLF- 210
Cdd:PRK10584   22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRAKhVGFVFQSFMLIp 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 211 SCSVAENIAYGADNLSSVTAQQVERAAEVANA---AEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALLKNPKILLL 287
Cdd:PRK10584  102 TLNALENVELPALLRGESSRQSRNGAKALLEQlglGKRLDHLPAQ-----------LSGGEQQRVALARAFNGRPDVLFA 170


                  ....*...
gi 1907190441 288 DEATSALD 295
Cdd:PRK10584  171 DEPTGNLD 178
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 122-338 6.94e-14

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 72.65  E-value: 6.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYdPN---SGTVSLDG-----HDIRQLNp 193
Cdd:PRK13549    6 LEMKNITKTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGeelqaSNIRDTE- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 194 vwlRSKIGTVSQEPVLFS-CSVAENIAYGADnlsSVTAQQVERAAEVANAAEFIRSFPQGFD--TVVGEkgilLSGGQKQ 270
Cdd:PRK13549   81 ---RAGIAIIHQELALVKeLSVLENIFLGNE---ITPGGIMDYDAMYLRAQKLLAQLKLDINpaTPVGN----LGLGQQQ 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 271 RIAIARALLKNPKILLLDEATSAL-DAENEHLVQEALDRLMEGRTVLIIAHRLSTIKN-ANFVAVLDHGK 338
Cdd:PRK13549  151 LVEIAKALNKQARLLILDEPTASLtESETAVLLDIIRDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 126-358 8.00e-14

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 72.97  E-value: 8.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 126 NVHFtYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP--VWLRSK---- 199
Cdd:PRK10261   19 NIAF-MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRqvIELSEQsaaq 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 --------IGTVSQEPV-----LFScsVAENIAygadnlSSVTAQQ----VERAAEVANAAEFIRsFPQGfDTVVGEKGI 262
Cdd:PRK10261   98 mrhvrgadMAMIFQEPMtslnpVFT--VGEQIA------ESIRLHQgasrEEAMVEAKRMLDQVR-IPEA-QTILSRYPH 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 263 LLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRT--VLIIAHRLSTIKN-ANFVAVLDHGKI 339
Cdd:PRK10261  168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEA 247

                         250
                  ....*....|....*....
gi 1907190441 340 CEHGTHEELLLKPNGLYRK 358
Cdd:PRK10261  248 VETGSVEQIFHAPQHPYTR 266
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 126-356 1.01e-13

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 71.29  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 126 NVHFTYPaRPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN---SGTVSLDGHDI-----RQLNPvwLR 197
Cdd:PRK09473   19 RVTFSTP-DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlnlpeKELNK--LR 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 198 S-KIGTVSQEPVlfsCSVAENIAYGaDNLSSV--------TAQQVER------AAEVANAAEFIRSFPQGFdtvvgekgi 262
Cdd:PRK09473   96 AeQISMIFQDPM---TSLNPYMRVG-EQLMEVlmlhkgmsKAEAFEEsvrmldAVKMPEARKRMKMYPHEF--------- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 263 llSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLI-IAHRLSTIKN-ANFVAVLDHGKI 339
Cdd:PRK09473  163 --SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIImITHDLGVVAGiCDKVLVMYAGRT 240

                         250
                  ....*....|....*..
gi 1907190441 340 CEHGTHEELLLKPNGLY 356
Cdd:PRK09473  241 MEYGNARDVFYQPSHPY 257
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
122-361 1.19e-13

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 70.20  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARP------EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHD-------- 187
Cdd:PRK15112    5 LEVRNLSKTFRYRTgwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlhfgdysy 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 188 ----IR--------QLNPvwlRSKIGTVSQEPVLFSCSVAENIAYGADNLssvTAQQVERAAEVANaaefirSFPQgfdt 255
Cdd:PRK15112   85 rsqrIRmifqdpstSLNP---RQRISQILDFPLRLNTDLEPEQREKQIIE---TLRQVGLLPDHAS------YYPH---- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 256 vvgekgiLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVA 332
Cdd:PRK15112  149 -------MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkqGISYIYVTQHLGMMKHiSDQVL 221

                         250       260       270
                  ....*....|....*....|....*....|
gi 1907190441 333 VLDHGKICEHGTHEELLLKP-NGLYRKLMN 361
Cdd:PRK15112  222 VMHQGEVVERGSTADVLASPlHELTKRLIA 251
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 142-295 1.32e-13

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 71.96  E-value: 1.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 142 DFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV-WLRSKIGTVSQEP----VLFSCSVAE 216
Cdd:PRK10762  270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISEDRkrdgLVLGMSVKE 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 217 NIAYGADNLSSVTAQQVERAAEVANAAEFIRSF----PqGFDTVVGekgiLLSGGQKQRIAIARALLKNPKILLLDEATS 292
Cdd:PRK10762  350 NMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFniktP-SMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTR 424


                  ...
gi 1907190441 293 ALD 295
Cdd:PRK10762  425 GVD 427
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 137-351 1.72e-13

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 71.76  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 137 VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLL--LRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTvsqepvlfSCSV 214
Cdd:TIGR03269  13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHVALCEKCGYVERPSKVGE--------PCPV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 215 AENIAYGADNLSSVTAQQVERAAEVANAAEFIRSFP-QGFDTVV-------------GEKGIL----------------- 263
Cdd:TIGR03269  85 CGGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFAlYGDDTVLdnvlealeeigyeGKEAVGravdliemvqlshrith 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 264 ----LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM--EGRTVLIIAHRLSTIKNANFVAV-LDH 336
Cdd:TIGR03269 165 iardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIEDLSDKAIwLEN 244

                         250
                  ....*....|....*
gi 1907190441 337 GKICEHGTHEELLLK 351
Cdd:TIGR03269 245 GEIKEEGTPDEVVAV 259
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
119-325 1.73e-13

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 69.91  E-value: 1.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 119 QGALEFRNVHFTYpaRPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlnpVWLRS 198
Cdd:PRK15056    4 QAGIVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 199 KIGTVSQ-EPVLFSCSV-AENIA----YGADNL----SSVTAQQVERAAEVANAAEFIRSfpqgfdtVVGEkgilLSGGQ 268
Cdd:PRK15056   79 LVAYVPQsEEVDWSFPVlVEDVVmmgrYGHMGWlrraKKRDRQIVTAALARVDMVEFRHR-------QIGE----LSGGQ 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441 269 KQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTI 325
Cdd:PRK15056  148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 143-353 1.84e-13

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 69.58  E-value: 1.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 143 FSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYdPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQE-PVLFSCSVAENIA-Y 220
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLTlH 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 221 GADNL-SSVTAQQVERAAEVANAAEFI-RSFPQgfdtvvgekgilLSGGQKQRIAIARALLK-----NP--KILLLDEAT 291
Cdd:PRK03695   94 QPDKTrTEAVASALNEVAEALGLDDKLgRSVNQ------------LSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPM 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441 292 SALDAENehlvQEALDRLME-----GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELLLKPN 353
Cdd:PRK03695  162 NSLDVAQ----QAALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 122-324 4.06e-13

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


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 67.27  E-value: 4.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYP-ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN--SGTVSLDGhdiRQLNPVWLRS 198
Cdd:cd03232     4 LTWKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILING---RPLDKNFQRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 199 kIGTVSQEPVLFSCS-VAENIAYGADNlssvtaqqveRAaevanaaefirsfpqgfdtvvgekgilLSGGQKQRIAIARA 277
Cdd:cd03232    81 -TGYVEQQDVHSPNLtVREALRFSALL----------RG---------------------------LSVEQRKRLTIGVE 122

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907190441 278 LLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLST 324
Cdd:cd03232   123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSA 170
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
 2-92 4.32e-13

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: 69.11  E-value: 4.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   2 TEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSF 81
Cdd:cd18572   196 REARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDV 275

                          90
                  ....*....|.
gi 1907190441  82 YSELMKGLGAG 92
Cdd:cd18572   276 FSSLMQAVGAA 286
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 139-338 4.80e-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: 70.35  E-value: 4.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 139 VFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLRLydpnsgtvsLDGHDIRQLNPVWLRS--KIGTVSQEPVL-FSCSVA 215
Cdd:TIGR03719  20 ILKDISLSFFPGAKIGVLGLNGAGKST----LLRI---------MAGVDKDFNGEARPQPgiKVGYLPQEPQLdPTKTVR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 216 ENIAYGA-------DNLSSVTAQ----------------------------QVERAAEVAnaAEFIRsFPQGfDTVVGEk 260
Cdd:TIGR03719  87 ENVEEGVaeikdalDRFNEISAKyaepdadfdklaaeqaelqeiidaadawDLDSQLEIA--MDALR-CPPW-DADVTK- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 261 gilLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN----EHLVQEaldrlMEGrTVLIIAHRLSTIKN-ANFVAVLD 335
Cdd:TIGR03719 162 ---LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE-----YPG-TVVAVTHDRYFLDNvAGWILELD 232


                  ...
gi 1907190441 336 HGK 338
Cdd:TIGR03719 233 RGR 235
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 139-373 7.29e-13

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 67.83  E-value: 7.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 139 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdirqlnpvwlRSKIGTVSQ----EPVL-FSCS 213
Cdd:PRK09544   19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYVPQklylDTTLpLTVN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 214 VAENIAYGadnlssVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALLKNPKILLLDEATSA 293
Cdd:PRK09544   88 RFLRLRPG------TKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 294 LDAENEHLVQEALDRLME--GRTVLIIAHRLSTI-KNANFVAVLDHgKICEHGTHEELLLKPNGLyrklmnkqSFLSYNG 370
Cdd:PRK09544  151 VDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVLCLNH-HICCSGTPEVVSLHPEFI--------SMFGPRG 221


                  ...
gi 1907190441 371 AEQ 373
Cdd:PRK09544  222 AEQ 224
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 122-330 1.43e-12

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 66.13  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI--------RQLNP 193
Cdd:PRK13540    2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdlctyqKQLCF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 194 VWLRSKIgtvsqEPVLfscSVAENIAYgaDNLSSVTAQQVERAAEVANAAEFIrSFPQGfdtvvgekgiLLSGGQKQRIA 273
Cdd:PRK13540   79 VGHRSGI-----NPYL---TLRENCLY--DIHFSPGAVGITELCRLFSLEHLI-DYPCG----------LLSSGQKRQVA 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441 274 IARALLKNPKILLLDEATSALDAEN-EHLVQEALDRLMEGRTVLIIAHRLSTIKNANF 330
Cdd:PRK13540  138 LLRLWMSKAKLWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKADY 195
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
 2-95 2.07e-12

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


Pssm-ID: 350057 [Multi-domain]  Cd Length: 289  Bit Score: 66.95  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   2 TEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSF 81
Cdd:cd18784   196 GEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSV 275

                          90
                  ....*....|....
gi 1907190441  82 YSELMKGLGAGGRL 95
Cdd:cd18784   276 YTGLMQAVGAAEKV 289
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
122-356 3.22e-12

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 66.75  E-value: 3.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRN--VHFTYPARPeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN----SGTVSLDGHDIRQLNPVW 195
Cdd:PRK15093    4 LDIRNltIEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLSPRE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 196 LRSKIG-TVS---QEPVlfSC-SVAENIayGADNLSSVTA--------QQV----ERAAE------VANAAEFIRSFPQG 252
Cdd:PRK15093   83 RRKLVGhNVSmifQEPQ--SClDPSERV--GRQLMQNIPGwtykgrwwQRFgwrkRRAIEllhrvgIKDHKDAMRSFPYE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 253 fdtvvgekgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTI-KNAN 329
Cdd:PRK15093  159 -----------LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWAD 227

                         250       260
                  ....*....|....*....|....*..
gi 1907190441 330 FVAVLDHGKICEHGTHEELLLKPNGLY 356
Cdd:PRK15093  228 KINVLYCGQTVETAPSKELVTTPHHPY 254
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 135-325 3.72e-12

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 67.34  E-value: 3.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 135 PEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPvwlRSK----IGTVSQE---- 206
Cdd:PRK10762   15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGP---KSSqeagIGIIHQElnli 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 207 PVLfscSVAENIAYGADNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEkgilLSGGQKQRIAIARALLKNPKILL 286
Cdd:PRK10762   92 PQL---TIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVII 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907190441 287 LDEATSAL-DAENEHLVQEALDRLMEGRTVLIIAHRLSTI 325
Cdd:PRK10762  165 MDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEI 204
PLN03211 PLN03211
ABC transporter G-25; Provisional
 150-338 3.94e-12

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 67.60  E-value: 3.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 150 GSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRskIGTVSQEPVLFS-CSVAENIAYGA--DNLS 226
Cdd:PLN03211   94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKR--TGFVTQDDILYPhLTVRETLVFCSllRLPK 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 227 SVTAQQVERAAEvANAAEFirSFPQGFDTVVGEKGIL-LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEH-LVQE 304
Cdd:PLN03211  172 SLTKQEKILVAE-SVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYrLVLT 248

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907190441 305 ALDRLMEGRTVLIIAHRLSTIKNANF--VAVLDHGK 338
Cdd:PLN03211  249 LGSLAQKGKTIVTSMHQPSSRVYQMFdsVLVLSEGR 284
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 111-320 4.39e-12

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 67.28  E-value: 4.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 111 MVLDEKTFQGAL--EFRNVHFTYPARPEVSvfqDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVsldghdi 188
Cdd:PRK11147  307 MQVEEASRSGKIvfEMENVNYQIDGKQLVK---DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------- 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 189 rqlnpvwlrsKIGTvSQEPVLFSC---------SVAENIAYGAdnlSSVTAQQVERaaevanaaeFIRSFPQGF------ 253
Cdd:PRK11147  377 ----------HCGT-KLEVAYFDQhraeldpekTVMDNLAEGK---QEVMVNGRPR---------HVLGYLQDFlfhpkr 433

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441 254 -DTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRlMEGrTVLIIAH 320
Cdd:PRK11147  434 aMTPVKA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDS-YQG-TVLLVSH 495
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 144-349 4.96e-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: 67.13  E-value: 4.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 144 SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSL----DGHDIRQLNPVwLRSK----IGTVSQEPVLFSCSVA 215
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD-GRGRakryIGILHQEYDLYPHRTV 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 216 eniaygADNLSSvtAQQVERAAEVANAAEFIRSFPQGFDTVVGEKgIL------LSGGQKQRIAIARALLKNPKILLLDE 289
Cdd:TIGR03269 383 ------LDNLTE--AIGLELPDELARMKAVITLKMVGFDEEKAEE-ILdkypdeLSEGERHRVALAQVLIKEPRIVILDE 453

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907190441 290 ATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 349
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 124-296 6.52e-12

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


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 64.21  E-value: 6.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 124 FRNVHFTYP-ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN---SGTVSLDGHDIRQLNPVWlRSK 199
Cdd:cd03233     6 WRNISFTTGkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKY-PGE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQEPVLFScsvaeniaygadnlsSVTAQQVERAAEVANAAEFIRsfpqgfdtvvgekGIllSGGQKQRIAIARALL 279
Cdd:cd03233    85 IIYVSEEDVHFP---------------TLTVRETLDFALRCKGNEFVR-------------GI--SGGERKRVSIAEALV 134

                         170
                  ....*....|....*..
gi 1907190441 280 KNPKILLLDEATSALDA 296
Cdd:cd03233   135 SRASVLCWDNSTRGLDS 151
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 122-341 7.76e-12

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 66.53  E-value: 7.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPArpevsvfQDFS-----LSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL 196
Cdd:PRK10522  323 LELRNVTFAYQD-------NGFSvgpinLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 197 RSKIGTVSQEPVLFscsvaeniaygaDNLSSVTAQQVERAAeVANAAEFIRSfpQGFDTVVGEK--GILLSGGQKQRIAI 274
Cdd:PRK10522  396 RKLFSAVFTDFHLF------------DQLLGPEGKPANPAL-VEKWLERLKM--AHKLELEDGRisNLKLSKGQKKRLAL 460

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 275 ARALLKNPKILLLDEATSALDAE-NEHLVQEALDRLME-GRTVLIIAHRLSTIKNANFVAVLDHGKICE 341
Cdd:PRK10522  461 LLALAEERDILLLDEWAADQDPHfRREFYQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
142-325 1.59e-11

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 65.60  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 142 DFSLSIPSGS-----VTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDghdIR-QLNPVWLRSKI-GTVSQepVLFSCsv 214
Cdd:PRK13409  352 DFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKiSYKPQYIKPDYdGTVED--LLRSI-- 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 215 aeniaygADNLSSVTAQQveraaevanaaEFIRSF--PQGFDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATS 292
Cdd:PRK13409  425 -------TDDLGSSYYKS-----------EIIKPLqlERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSA 482

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907190441 293 ALDAENEHLVQEALDRLMEGR--TVLIIAHRLSTI 325
Cdd:PRK13409  483 HLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI 517
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 140-325 1.92e-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: 1.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 140 FQDFSLSIPSGS-----VTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDghdirqLN----PVWLRSKI-GTVSQepVL 209
Cdd:COG1245   351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------LKisykPQYISPDYdGTVEE--FL 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 210 FSCSvaeniaygADNLSSVTAQqveraaevanaAEFIRsfPQG----FDTVVGEkgilLSGGQKQRIAIARALLKNPKIL 285
Cdd:COG1245   423 RSAN--------TDDFGSSYYK-----------TEIIK--PLGleklLDKNVKD----LSGGELQRVAIAACLSRDADLY 477

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907190441 286 LLDEATSALDAENEHLVQEALDRLMEGR--TVLIIAHRLSTI 325
Cdd:COG1245   478 LLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI 519
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
134-359 2.64e-11

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 62.51  E-value: 2.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 134 RPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRS--KIGTVSQ-EPVLf 210
Cdd:PRK13538   11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllYLGHQPGiKTEL- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 211 scSVAENIAYGADNLSSVTAQQVERAAEVANAAefirsfpqGF-DTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDE 289
Cdd:PRK13538   90 --TALENLRFYQRLHGPGDDEALWEALAQVGLA--------GFeDVPVRQ----LSAGQQRRVALARLWLTRAPLWILDE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 290 ATSALDAenehlvqEALDRLmegrTVLIIAHrlstiknanfvavldhgkiCEHG------THEELLLKPNGlYRKL 359
Cdd:PRK13538  156 PFTAIDK-------QGVARL----EALLAQH-------------------AEQGgmviltTHQDLPVASDK-VRKL 200
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 122-324 3.47e-11

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: 64.57  E-value: 3.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLdGHDIrqlnpvwlrsKIG 201
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQ--EPVLFSCSVAENIAYGADNLSSVTAQQVERAaevanaaeFIRSFpqGFDTVVGEKGI-LLSGGQKQRIAIARAL 278
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGGLDIIKLGKREIPSRA--------YVGRF--NFKGSDQQKKVgQLSGGERNRVHLAKTL 458

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907190441 279 LKNPKILLLDEATSALDAENEHLVQEALDRLmeGRTVLIIAH------RLST 324
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 122-345 3.51e-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: 64.46  E-value: 3.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYdPN---SGTVSLDGHDIRQLNPVWLRS 198
Cdd:TIGR02633   2 LEMKGIVKTFGG---VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTER 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 199 K-IGTVSQEPVLF-SCSVAENIAYGadNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTV---VGEKGillsGGQKQRIA 273
Cdd:TIGR02633  78 AgIVIIHQELTLVpELSVAENIFLG--NEITLPGGRMAYNAMYLRAKNLLRELQLDADNVtrpVGDYG----GGQQQLVE 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907190441 274 IARALLKNPKILLLDEATSAL-DAENEHLVQEALDRLMEGRTVLIIAHRLSTIKnanfvAVLDHGKICEHGTH 345
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVK-----AVCDTICVIRDGQH 219
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
140-335 3.58e-11

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 64.44  E-value: 3.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 140 FQDFSLSIPS-GSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVsldghdirQLNPVW---LRSKIGTVSQEpvLFSCSVA 215
Cdd:PRK13409   88 FKLYGLPIPKeGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--------EEEPSWdevLKRFRGTELQN--YFKKLYN 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 216 ENIAygadnlSSVTAQQVERAAEV--ANAAEFIRSFPQG--FDTVVGEKGIL---------LSGGQKQRIAIARALLKNP 282
Cdd:PRK13409  158 GEIK------VVHKPQYVDLIPKVfkGKVRELLKKVDERgkLDEVVERLGLEnildrdiseLSGGELQRVAIAAALLRDA 231

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907190441 283 KILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLstiknanfvAVLD 335
Cdd:PRK13409  232 DFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL---------AVLD 275
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 122-340 4.68e-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: 64.08  E-value: 4.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN-SGTVSLDGHDIRQLNPV-WLRSK 199
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAqAIRAG 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 200 IGTVSQE-------PVLfscSVAENIAYGADNlSSVTAQQVERAAEVANAAEFIR------SFPqgfDTVVGEkgilLSG 266
Cdd:TIGR02633 338 IAMVPEDrkrhgivPIL---GVGKNITLSVLK-SFCFKMRIDAAAELQIIGSAIQrlkvktASP---FLPIGR----LSG 406

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441 267 GQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHGKIC 340
Cdd:TIGR02633 407 GNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAEVLGlSDRVLVIGEGKLK 482
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 135-325 5.10e-11

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 63.98  E-value: 5.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 135 PEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIR-QLNPVWLRSKIGTVSQE-PVLFSC 212
Cdd:PRK10982    9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 213 SVAENIAYGADNLSSVTAQQVERAAEVANAAEFIrsfpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATS 292
Cdd:PRK10982   89 SVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDEL-----DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907190441 293 AL-DAENEHLVQeALDRLME-GRTVLIIAHRLSTI 325
Cdd:PRK10982  164 SLtEKEVNHLFT-IIRKLKErGCGIVYISHKMEEI 197
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 74-326 6.59e-11

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: 64.00  E-value: 6.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  74 SIGGLSSFYSELMKGLGAGGRLWEL---LERQPRLPFNEGMVLD--------------------EKTFQGaLEFRNVHFT 130
Cdd:TIGR00954 382 ALGRLMLAGRDMTRLAGFTARVDTLlqvLDDVKSGNFKRPRVEEiesgreggrnsnlvpgrgivEYQDNG-IKFENIPLV 460

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 131 YPARpEVsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdirqlnpvwlRSKIGTVSQEPVLF 210
Cdd:TIGR00954 461 TPNG-DV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMT 527

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 211 SCSVAENIAY--GADNL--SSVTAQQVERAAEVANAaEFIRSFPQGFDTVVGEKGiLLSGGQKQRIAIARALLKNPKILL 286
Cdd:TIGR00954 528 LGTLRDQIIYpdSSEDMkrRGLSDKDLEQILDNVQL-THILEREGGWSAVQDWMD-VLSGGEKQRIAMARLFYHKPQFAI 605

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1907190441 287 LDEATSALDAENEHLVQEALDRLmeGRTVLIIAHRLSTIK 326
Cdd:TIGR00954 606 LDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWK 643
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
 3-95 1.23e-10

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: 61.68  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFY 82
Cdd:cd18551   197 ETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFF 276

                          90
                  ....*....|...
gi 1907190441  83 SELMKGLGAGGRL 95
Cdd:cd18551   277 TQLQKALGALERI 289
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 93-295 1.33e-10

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 62.64  E-value: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  93 GRlwELLERQPRLPFNEGMVLdektfqgaLEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLR 172
Cdd:PRK13549  241 GR--ELTALYPREPHTIGEVI--------LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 173 LYdP--NSGTVSLDGHDIRQLNPV-WLRSKIGTVSQE-------PVLfscSVAENIAYGAdnLSSVT-AQQVERAAEVAN 241
Cdd:PRK13549  311 AY-PgrWEGEIFIDGKPVKIRNPQqAIAQGIAMVPEDrkrdgivPVM---GVGKNITLAA--LDRFTgGSRIDDAAELKT 384

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 242 AAEFIR------SFPqgfDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATSALD 295
Cdd:PRK13549  385 ILESIQrlkvktASP---ELAIAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 140-335 2.05e-10

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 62.11  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 140 FQDFSLSIP-SGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDghdirqlnPVW---LRSKIGTVSQEpvLFScSVA 215
Cdd:COG1245    88 FRLYGLPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEE--------PSWdevLKRFRGTELQD--YFK-KLA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 216 ENiaygadNLS-SVTAQQVERAAEV--ANAAEFIRSfpqgfdtvVGEKGIL-------------------LSGGQKQRIA 273
Cdd:COG1245   157 NG------EIKvAHKPQYVDLIPKVfkGTVRELLEK--------VDERGKLdelaeklglenildrdiseLSGGELQRVA 222

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 274 IARALLKNPKILLLDEATSALD-------AEnehLVQEALDrlmEGRTVLIIAHRLstiknanfvAVLD 335
Cdd:COG1245   223 IAAALLRDADFYFFDEPSSYLDiyqrlnvAR---LIRELAE---EGKYVLVVEHDL---------AILD 276
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 139-320 2.45e-10

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 62.06  E-value: 2.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 139 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSL-DGHdirqlnpvwlrsKIGTVSQEPVL-FSCSVAE 216
Cdd:PRK11819   22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGI------------KVGYLPQEPQLdPEKTVRE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 217 NIAYG--------------ADNLSSVTAQQVERAAEVAN-------------------AAEFIRSfPQGfDTVVGEkgil 263
Cdd:PRK11819   90 NVEEGvaevkaaldrfneiYAAYAEPDADFDALAAEQGElqeiidaadawdldsqleiAMDALRC-PPW-DAKVTK---- 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907190441 264 LSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-----EHLVQealdrlMEGrTVLIIAH 320
Cdd:PRK11819  164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawleQFLHD------YPG-TVVAVTH 218
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 3-95 2.91e-10

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: 60.58  E-value: 2.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFY 82
Cdd:cd18575   197 ERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVW 276

                          90
                  ....*....|...
gi 1907190441  83 SELMKGLGAGGRL 95
Cdd:cd18575   277 GDLQRAAGAAERL 289
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 122-345 3.48e-10

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 59.80  E-value: 3.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLL--RLYDPNSGTVSLDGHDIRQLNP------ 193
Cdd:PRK09580    2 LSIKDLHVSVEDKA---ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPedrage 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 194 -VWLR----SKIGTVSQEPVLFSCSVAENIAYGADNLSSVTAQQ-VERAAEVANAAE--FIRSFPQGFdtvvgekgillS 265
Cdd:PRK09580   79 gIFMAfqypVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDlMEEKIALLKMPEdlLTRSVNVGF-----------S 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 266 GGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEG-RTVLIIAH--RLSTIKNANFVAVLDHGKICEH 342
Cdd:PRK09580  148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKS 227


                  ...
gi 1907190441 343 GTH 345
Cdd:PRK09580  228 GDF 230
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 141-348 6.34e-10

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: 60.80  E-value: 6.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 141 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLL------RLYdpNSGTVSLDGHDIRQLNPVwlrSKIGTVSQEPV------ 208
Cdd:TIGR00630 625 KNITVSIPLGLFTCITGVSGSGKSTLINDTLypalanRLN--GAKTVPGRYTSIEGLEHL---DKVIHIDQSPIgrtprs 699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 209 --------------LFS----------------------------------------------CSVAE---------NIA 219
Cdd:TIGR00630 700 npatytgvfdeireLFAetpeakvrgytpgrfsfnvkggrceacqgdgvikiemhflpdvyvpCEVCKgkrynretlEVK 779

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 220 YGADNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTV------VGEKGILLSGGQKQRIAIARALLK---NPKILLLDEA 290
Cdd:TIGR00630 780 YKGKNIADVLDMTVEEAYEFFEAVPSISRKLQTLCDVglgyirLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEP 859

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907190441 291 TSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKNANFVAVL-----DH-GKICEHGTHEEL 348
Cdd:TIGR00630 860 TTGLHFDDIKKLLEVLQRLVDkGNTVVVIEHNLDVIKTADYIIDLgpeggDGgGTVVASGTPEEV 924
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
141-322 1.11e-09

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 59.92  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 141 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHdirqlnPVWLRSKIGTVSQEPVLfsC-------- 212
Cdd:PRK11288  270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK------PIDIRSPRDAIRAGIML--Cpedrkaeg 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 213 -----SVAENIAYGADNLSSVTAQQVERAAEVANAAEFIRSFpqGFDTVVGEKGIL-LSGGQKQRIAIARALLKNPKILL 286
Cdd:PRK11288  342 iipvhSVADNINISARRHHLRAGCLINNRWEAENADRFIRSL--NIKTPSREQLIMnLSGGNQQKAILGRWLSEDMKVIL 419

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907190441 287 LDEATSALD--AENE--HLVQEALDRlmeGRTVLIIAHRL 322
Cdd:PRK11288  420 LDEPTRGIDvgAKHEiyNVIYELAAQ---GVAVLFVSSDL 456
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 108-330 1.23e-09

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 60.12  E-value: 1.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  108 NEGMVLDEKTFQGALEFRNVHFTYPARPEVSVFQD-FSLSIPSGSVTALVGPSGSGKSTvvsLLLRLYDPNSGTVSLDGH 186
Cdd:TIGR00956  746 NDEKDMEKESGEDIFHWRNLTYEVKIKKEKRVILNnVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGD 822

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  187 DI---RQLNPVWLRSkIGTVSQEPV-LFSCSVAENIAYGA--DNLSSVT-AQQVERAAEVANAAEfIRSFPqgfDTVVGE 259
Cdd:TIGR00956  823 RLvngRPLDSSFQRS-IGYVQQQDLhLPTSTVRESLRFSAylRQPKSVSkSEKMEYVEEVIKLLE-MESYA---DAVVGV 897

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907190441  260 KGILLSGGQKQRIAIARALLKNPKILL-LDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKNANF 330
Cdd:TIGR00956  898 PGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSAILFEEF 970
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
 3-94 1.28e-09

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


Pssm-ID: 350018 [Multi-domain]  Cd Length: 295  Bit Score: 58.71  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFY 82
Cdd:cd18574   203 ELELYEEEVEKAAKLNEKLGLGIGIFQGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLF 282

                          90
                  ....*....|..
gi 1907190441  83 SELMKGLGAGGR 94
Cdd:cd18574   283 GQYVKGKSAGAR 294
PLN03073 PLN03073
ABC transporter F family; Provisional
 122-347 1.34e-09

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 59.87  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARPevSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVsldghdirqlnpvwLRS--- 198
Cdd:PLN03073  509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--------------FRSakv 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 199 KIGTVSQEPVLFSCSVAENIAYGADNLSSVTAQQVeRAaevanaaeFIRSFpqgfdtvvGEKGIL-------LSGGQKQR 271
Cdd:PLN03073  573 RMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKL-RA--------HLGSF--------GVTGNLalqpmytLSGGQKSR 635

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 272 IAIARALLKNPKILLLDEATSALDAEN-EHLVQEALdrLMEGrTVLIIAHRLSTIKNA-NFVAVLDHGKICE-HGTHEE 347
Cdd:PLN03073  636 VAFAKITFKKPHILLLDEPSNHLDLDAvEALIQGLV--LFQG-GVLMVSHDEHLISGSvDELWVVSEGKVTPfHGTFHD 711
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 123-327 1.40e-09

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 59.26  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 123 EFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLL-----------LRLYDPNSGTvsldGHDIrql 191
Cdd:PRK10938  262 VLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndLTLFGRRRGS----GETI--- 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 192 npvW-LRSKIGTVSQEPVL---FSCSVAENIAYG-----------ADNLSSVTAQQVER---AAEVANAAefIRSfpqgf 253
Cdd:PRK10938  332 ---WdIKKHIGYVSSSLHLdyrVSTSVRNVILSGffdsigiyqavSDRQQKLAQQWLDIlgiDKRTADAP--FHS----- 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 254 dtvvgekgilLSGGQkQRIA-IARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLI------------IA 319
Cdd:PRK10938  402 ----------LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsEGETQLLfvshhaedapacIT 470


                  ....*...
gi 1907190441 320 HRLSTIKN 327
Cdd:PRK10938  471 HRLEFVPD 478
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 127-356 3.53e-09

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 57.44  E-value: 3.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 127 VHFTYPARPEVSVfQDFSLSIPSGSVTALVGPSGSGKStVVSL-LLRLYDpNSGTVS-----LDGHDIRQLNPVWLRSKI 200
Cdd:PRK11022   11 VHFGDESAPFRAV-DRISYSVKQGEVVGIVGESGSGKS-VSSLaIMGLID-YPGRVMaekleFNGQDLQRISEKERRNLV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 201 GT----VSQEPVlfscsVAENIAY--GADNLSSVTAQQ-------VERAAE------VANAAEFIRSFPQGfdtvvgekg 261
Cdd:PRK11022   88 GAevamIFQDPM-----TSLNPCYtvGFQIMEAIKVHQggnkktrRQRAIDllnqvgIPDPASRLDVYPHQ--------- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 262 ilLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM--EGRTVLIIAHRLSTI-KNANFVAVLDHGK 338
Cdd:PRK11022  154 --LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVaEAAHKIIVMYAGQ 231

                         250
                  ....*....|....*...
gi 1907190441 339 ICEHGTHEELLLKPNGLY 356
Cdd:PRK11022  232 VVETGKAHDIFRAPRHPY 249
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 101-349 4.28e-09

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 57.98  E-value: 4.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 101 RQ-PRLPFNEgmvlDEKTFQGALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSG 179
Cdd:PRK15064  302 RQnPFIRFEQ----DKKLHRNALEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 180 TVSldghdirqlnpvWlrskigtvsqepvlfscsvAENIAYGadnlssVTAQqvERAAEVAN---AAEFIRSF--PQGFD 254
Cdd:PRK15064  375 TVK------------W-------------------SENANIG------YYAQ--DHAYDFENdltLFDWMSQWrqEGDDE 415

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 255 TVVgeKGIL----------------LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDrLMEGrTVLII 318
Cdd:PRK15064  416 QAV--RGTLgrllfsqddikksvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE-KYEG-TLIFV 491

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907190441 319 AHrlstikNANFVAVL--------DHGKICEHGTHEELL 349
Cdd:PRK15064  492 SH------DREFVSSLatriieitPDGVVDFSGTYEEYL 524
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 144-376 6.81e-09

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 57.21  E-value: 6.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 144 SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVsqepvlfscsvaENIAYGAD 223
Cdd:PRK13545   44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI------------ENIELKGL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 224 NLSSVTAQQVERAAEVANAAEFIRSFPQGFDTvvgekgilLSGGQKQRIAIARALLKNPKILLLDEATSALDaenEHLVQ 303
Cdd:PRK13545  112 MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKT--------YSSGMKSRLGFAISVHINPDILVIDEALSVGD---QTFTK 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441 304 EALDRLME----GRTVLIIAHRLSTIKNANFVAV-LDHGKICEHGTHEELLLKpnglYRKLMNKQSFLSYNGAEQFLE 376
Cdd:PRK13545  181 KCLDKMNEfkeqGKTIFFISHSLSQVKSFCTKALwLHYGQVKEYGDIKEVVDH----YDEFLKKYNQMSVEERKDFRE 254
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 135-296 7.61e-09

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 57.81  E-value: 7.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  135 PEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVV-SLLLRLYD---PNSGTVSLDGHDIRQLNPvWLRSKIGTVSQEPVLF 210
Cdd:TIGR00956   72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTDGfhiGVEGVITYDGITPEEIKK-HYRGDVVYNAETDVHF 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  211 -SCSVAENIAYGA---------DNLSsvtaqQVERAAEVANAAEFIRSFPQGFDTVVGE---KGIllSGGQKQRIAIARA 277
Cdd:TIGR00956  151 pHLTVGETLDFAArcktpqnrpDGVS-----REEYAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEA 223

                          170
                   ....*....|....*....
gi 1907190441  278 LLKNPKILLLDEATSALDA 296
Cdd:TIGR00956  224 SLGGAKIQCWDNATRGLDS 242
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
133-306 9.99e-09

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 54.85  E-value: 9.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 133 ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNpvwlRSK-IGTVSQEPVLFS 211
Cdd:PRK13543   20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRfMAYLGHLPGLKA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 212 -CSVAENIAYgadnlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEA 290
Cdd:PRK13543   96 dLSTLENLHF-------LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEP 164

                         170
                  ....*....|....*.
gi 1907190441 291 TSALDAENEHLVQEAL 306
Cdd:PRK13543  165 YANLDLEGITLVNRMI 180
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 140-323 1.18e-08

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


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 55.45  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 140 FQDFSLSIP-SGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTvsldghdiRQLNPVW---LRSKIGTVSQEpvLFSCSVA 215
Cdd:cd03236    15 FKLHRLPVPrEGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--------FDDPPDWdeiLDEFRGSELQN--YFTKLLE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 216 ENIAygadnlSSVTAQQVERAAEVA--NAAEFIRSFPQ--GFDTVV---GEKGIL------LSGGQKQRIAIARALLKNP 282
Cdd:cd03236    85 GDVK------VIVKPQYVDLIPKAVkgKVGELLKKKDErgKLDELVdqlELRHVLdrnidqLSGGELQRVAIAAALARDA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907190441 283 KILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLS 323
Cdd:cd03236   159 DFYFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLA 200
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 141-337 1.32e-08

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: 53.87  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 141 QDFSLSIPSGSVTALVGPSGSGKSTVVslllrlydpnsgtvsLDGhdIRQLNPVWLRSKIGTVSQEPVLFscsvaeniay 220
Cdd:cd03238    12 QNLDVSIPLNVLVVVTGVSGSGKSTLV---------------NEG--LYASGKARLISFLPKFSRNKLIF---------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 221 gADNLSSVtaqqveraaeVANAAEFIRsfpqgfdtvVGEKGILLSGGQKQRIAIARALLKNPK--ILLLDEATSALDAEN 298
Cdd:cd03238    65 -IDQLQFL----------IDVGLGYLT---------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907190441 299 EHLVQEALDRLM-EGRTVLIIAHRLSTIKNANFVAVLDHG 337
Cdd:cd03238   125 INQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFGPG 164
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
 3-91 1.53e-08

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


Pssm-ID: 350033 [Multi-domain]  Cd Length: 289  Bit Score: 55.56  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFY 82
Cdd:cd18589   197 EAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYY 276


                  ....*....
gi 1907190441  83 SELMKGLGA 91
Cdd:cd18589   277 PSVMKAVGS 285
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 144-329 1.62e-08

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: 53.52  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 144 SLSIPSGSVTALVGPSGSGKSTVvslllrlydpnsgtvsldghdirqlnpvwlrskigtvsqepvLFSCSVAENIAYGAD 223
Cdd:cd03227    15 DVTFGEGSLTIITGPNGSGKSTI------------------------------------------LDAIGLALGGAQSAT 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 224 NLSSVTAQQVERAAEvanAAEFIRSFPQgfdtvvgekgilLSGGQKQRIAIARAL---LKNPKIL-LLDEATSALDAENE 299
Cdd:cd03227    53 RRRSGVKAGCIVAAV---SAELIFTRLQ------------LSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDG 117

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907190441 300 HLVQEAL-DRLMEGRTVLIIAHRLSTIKNAN 329
Cdd:cd03227   118 QALAEAIlEHLVKGAQVIVITHLPELAELAD 148
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 147-325 2.18e-08

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 53.34  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 147 IPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHdirqlnpvwlrskigTVSQEPvlfscsvaeniaygadnls 226
Cdd:cd03222    22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI---------------TPVYKP------------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 227 svtaqqveraaevanaaefirsfpqgfdtvvgeKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEAL 306
Cdd:cd03222    68 ---------------------------------QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114

                         170       180
                  ....*....|....*....|.
gi 1907190441 307 DRLME--GRTVLIIAHRLSTI 325
Cdd:cd03222   115 RRLSEegKKTALVVEHDLAVL 135
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 152-336 3.49e-08

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


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 53.38  E-value: 3.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 152 VTALVGPSGSGKSTVVSLLLrlydpnsgtVSLDGHDIRQLNPVWLRSKIgtvsqepvlfsCSVAENIAYGADNLSSVTAQ 231
Cdd:cd03240    24 LTLIVGQNGAGKTTIIEALK---------YALTGELPPNSKGGAHDPKL-----------IREGEVRAQVKLAFENANGK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 232 Q--VERAAEVANAAEFIRsfpQG-FDTVVGEKGILLSGGQKQ------RIAIARALLKNPKILLLDEATSALDAENehlV 302
Cdd:cd03240    84 KytITRSLAILENVIFCH---QGeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---I 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907190441 303 QEALDRLME------GRTVLIIAHrlstikNANFVAVLDH 336
Cdd:cd03240   158 EESLAEIIEerksqkNFQLIVITH------DEELVDAADH 191
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 140-295 6.60e-08

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 54.29  E-value: 6.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 140 FQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwLRSKIGTV-----SQEPVLF-SCS 213
Cdd:PRK15439  279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYlDAP 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 214 VAENI-AYGADNLSSVTAQQVERAA-EVANAAEFIRsFPQGFDTVVGekgilLSGGQKQRIAIARALLKNPKILLLDEAT 291
Cdd:PRK15439  358 LAWNVcALTHNRRGFWIKPARENAVlERYRRALNIK-FNHAEQAART-----LSGGNQQKVLIAKCLEASPQLLIVDEPT 431


                  ....
gi 1907190441 292 SALD 295
Cdd:PRK15439  432 RGVD 435
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
 2-95 7.97e-08

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: 53.32  E-value: 7.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   2 TEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSF 81
Cdd:cd07346   199 REIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANL 278

                          90
                  ....*....|....
gi 1907190441  82 YSELMKGLGAGGRL 95
Cdd:cd07346   279 YNQLQQALASLERI 292
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 143-328 2.78e-07

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 50.64  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 143 FSLSI---PSgSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLrSKIGtvSQEPVLFSCSVAENIA 219
Cdd:PRK13541   17 FDLSItflPS-AITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC-TYIG--HNLGLKLEMTVFENLK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 220 YGadnlssvtaqqveraAEVANAAEFIRSFPQGF--DTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 297
Cdd:PRK13541   93 FW---------------SEIYNSAETLYAAIHYFklHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907190441 298 NEHLVQEALD-RLMEGRTVLIIAHRLSTIKNA 328
Cdd:PRK13541  158 NRDLLNNLIVmKANSGGIVLLSSHLESSIKSA 189
PLN03140 PLN03140
ABC transporter G family member; Provisional
 254-323 2.78e-07

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 52.54  E-value: 2.78e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907190441  254 DTVVGEKGIL-LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLS 323
Cdd:PLN03140  1009 DAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPS 1080
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
141-373 6.96e-07

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 50.20  E-value: 6.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 141 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH-DIRQLNpVWLRSKIGTVsqEPVLFSCSVaenIA 219
Cdd:PRK13546   41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAIS-AGLSGQLTGI--ENIEFKMLC---MG 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 220 YGADNLSSVTAQQVEraaeVANAAEFIRSFPQGFdtvvgekgillSGGQKQRIAIARALLKNPKILLLDEATSALDaenE 299
Cdd:PRK13546  115 FKRKEIKAMTPKIIE----FSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD---Q 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441 300 HLVQEALDRLME----GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKpnglYRKLMNkqSFLSYNGAEQ 373
Cdd:PRK13546  177 TFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK----YEAFLN--DFKKKSKAEQ 249
PLN03140 PLN03140
ABC transporter G family member; Provisional
 134-317 9.28e-07

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 51.00  E-value: 9.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  134 RPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN---SGTVSLDGHDIRQLNPvwlRSKIGTVSQEPV-L 209
Cdd:PLN03140   175 KTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVP---RKTSAYISQNDVhV 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  210 FSCSVAENIAYGA---------DNLSSVTAQQVERA----AEV-----ANAAEFIRS------------FPQGFDTVVGE 259
Cdd:PLN03140   252 GVMTVKETLDFSArcqgvgtryDLLSELARREKDAGifpeAEVdlfmkATAMEGVKSslitdytlkilgLDICKDTIVGD 331

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907190441  260 ---KGIllSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALD---RLMEGrTVLI 317
Cdd:PLN03140   332 emiRGI--SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQqivHLTEA-TVLM 392
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 264-339 1.78e-06

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 49.95  E-value: 1.78e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907190441 264 LSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-EHLVQEALDrlMEGrTVLIIAHRLSTIKN-ANFVAVLDHGKI 339
Cdd:PRK11147  157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETiEWLEGFLKT--FQG-SIIFISHDRSFIRNmATRIVDLDRGKL 231
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
119-354 1.92e-06

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 49.35  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 119 QGALEFRNV--HFTyparpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVvSLLLRLYDPNSGTVSLDgHDIRQLNPVWL 196
Cdd:NF000106   11 RNAVEVRGLvkHFG-----EVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWR-F*TWCANRRAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 197 RSKIGTvsQEPVlfSCSVAENIAyGADNLSSVTAQ-QVERAAEVANAAEFIRSFpqGFDTVVGEKGILLSGGQKQRIAIA 275
Cdd:NF000106   84 RRTIG*--HRPV--R*GRRESFS-GRENLYMIGR*lDLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 276 RALLKNPKILLLDEATSALDAENEHLV-QEALDRLMEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPN 353
Cdd:NF000106  157 ASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236


                  .
gi 1907190441 354 G 354
Cdd:NF000106  237 G 237
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
 3-94 2.14e-06

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


Pssm-ID: 350034 [Multi-domain]  Cd Length: 289  Bit Score: 48.87  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFY 82
Cdd:cd18590   197 EACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIY 276

                          90
                  ....*....|..
gi 1907190441  83 SELMKGLGAGGR 94
Cdd:cd18590   277 GDMLSNVGAAAK 288
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 144-349 2.26e-06

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 49.24  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 144 SLSIPSGSVTALVGPSGSGKStvvSLLLRLydpnSGTVSL-DGHDIRQLNPVWLRS-----KIgtVSQEpvlFSCSVAEN 217
Cdd:PRK10938   23 SLTLNAGDSWAFVGANGSGKS---ALARAL----AGELPLlSGERQSQFSHITRLSfeqlqKL--VSDE---WQRNNTDM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 218 IAYGADNLSSVTAQQV-------ERAAEVAnaAEFirsfpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEA 290
Cdd:PRK10938   91 LSPGEDDTGRTTAEIIqdevkdpARCEQLA--QQF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907190441 291 TSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 349
Cdd:PRK10938  163 FDGLDVASRQQLAELLASLHqSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEIL 223
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
264-348 2.44e-06

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 49.64  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 264 LSGGQKQRIAIARALLK--NPKIL-LLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKNAnfvavlDH--- 336
Cdd:COG0178   827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTA------DWiid 900

                          90       100
                  ....*....|....*....|.
gi 1907190441 337 ---------GKICEHGTHEEL 348
Cdd:COG0178   901 lgpeggdggGEIVAEGTPEEV 921
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 150-322 2.83e-06

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 49.63  E-value: 2.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  150 GSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNLSSVT 229
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVP 2043

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  230 AQQVERaaeVANAAefIRSFpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL 309
Cdd:TIGR01257 2044 AEEIEK---VANWS--IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116

                          170
                   ....*....|....
gi 1907190441  310 M-EGRTVLIIAHRL 322
Cdd:TIGR01257 2117 IrEGRAVVLTSHSM 2130
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
142-295 3.37e-06

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 48.97  E-value: 3.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 142 DFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI------RQLNPvwlrsKIGTVSQ------EPVL 209
Cdd:NF033858   19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadarhrRAVCP-----RIAYMPQglgknlYPTL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 210 fscSVAENIA-----YGADnlssvTAQQVERAAEVANA---AEFiRSFPQGfdtvvgeKgilLSGGQKQRIAIARALLKN 281
Cdd:NF033858   94 ---SVFENLDffgrlFGQD-----AAERRRRIDELLRAtglAPF-ADRPAG-------K---LSGGMKQKLGLCCALIHD 154

                         170
                  ....*....|....
gi 1907190441 282 PKILLLDEATSALD 295
Cdd:NF033858  155 PDLLILDEPTTGVD 168
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 264-331 5.99e-06

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 48.67  E-value: 5.99e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907190441  264 LSGGQKQRIAIARALL---KNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKNANFV 331
Cdd:PRK00635   810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVKVADYV 881
uvrA PRK00349
excinuclease ABC subunit UvrA;
264-377 7.46e-06

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 48.15  E-value: 7.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 264 LSGGQKQRIAIARALLKNP--KIL-LLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKNAnfvavlDH--- 336
Cdd:PRK00349  831 LSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTA------DWiid 904

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907190441 337 ---------GKICEHGTHEELLLKPNglyrklmnkqsflSYNGaeQFLEP 377
Cdd:PRK00349  905 lgpeggdggGEIVATGTPEEVAKVEA-------------SYTG--RYLKP 939
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 155-320 9.49e-06

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 47.58  E-value: 9.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 155 LVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDirqlnpvwlrsKIGTVSQEPVLF-SCSVAENIAYGADNLSSVTAqqv 233
Cdd:PRK15064   32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDPNE-----------RLGKLRQDQFAFeEFTVLDTVIMGHTELWEVKQ--- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 234 ERAAEVAN----------AAEFIRSFPQgFDTVVGEK--GILLSG-----------------GQKQRIAIARALLKNPKI 284
Cdd:PRK15064   98 ERDRIYALpemseedgmkVADLEVKFAE-MDGYTAEAraGELLLGvgipeeqhyglmsevapGWKLRVLLAQALFSNPDI 176

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907190441 285 LLLDEATSALDAENEHLVQEALDRlmEGRTVLIIAH 320
Cdd:PRK15064  177 LLLDEPTNNLDINTIRWLEDVLNE--RNSTMIIISH 210
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
 122-320 1.07e-05

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


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 46.11  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNvhFTYPARPEVSVFQDFSLSipsgSVTALVGPSGSGKSTvvslllrLYDpnSGTVSLDGHDIRQLNPVWLRSKIG 201
Cdd:cd03279     6 LELKN--FGPFREEQVIDFTGLDNN----GLFLICGPTGAGKST-------ILD--AITYALYGKTPRYGRQENLRSVFA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQE-PVLFSCSvAENIAYgadnlssvtaqQVERAAEVaNAAEFIRSF--PQG-FDTVVGEKGILLSGGQKQRIAIARA 277
Cdd:cd03279    71 PGEDTaEVSFTFQ-LGGKKY-----------RVERSRGL-DYDQFTRIVllPQGeFDRFLARPVSTLSGGETFLASLSLA 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907190441 278 L-----LKNPK-----ILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAH 320
Cdd:cd03279   138 LalsevLQNRGgarleALFIDEGFGTLDPEALEAVATALELIrTENRMVGVISH 191
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 122-320 1.08e-05

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 47.42  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 122 LEFRNVHFTYPARpevSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLdGHDIrqlnpvwlrsKIG 201
Cdd:PRK11819  325 IEAENLSKSFGDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLA 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 202 TVSQ-----EPvlfSCSVAENIAYGADNLsSVTAQQVERAAEVAnaaefirSFpqGFdtvvgeKGI-------LLSGGQK 269
Cdd:PRK11819  391 YVDQsrdalDP---NKTVWEEISGGLDII-KVGNREIPSRAYVG-------RF--NF------KGGdqqkkvgVLSGGER 451

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907190441 270 QRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLmeGRTVLIIAH 320
Cdd:PRK11819  452 NRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEF--PGCAVVISH 500
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
140-295 1.43e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 47.04  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 140 FQDF------SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSL-----DGHDIRqlnpvwLRSKIGTVSQEpv 208
Cdd:NF033858  276 FGDFtavdhvSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDIA------TRRRVGYMSQA-- 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 209 lFSC----SVAENIAYGADnLSSVTAQQV-ERAAEVANA---AEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALLK 280
Cdd:NF033858  348 -FSLygelTVRQNLELHAR-LFHLPAAEIaARVAEMLERfdlADVADALPDS-----------LPLGIRQRLSLAVAVIH 414

                         170
                  ....*....|....*
gi 1907190441 281 NPKILLLDEATSALD 295
Cdd:NF033858  415 KPELLILDEPTSGVD 429
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
141-349 7.02e-05

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 44.78  E-value: 7.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 141 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV-WLRSKIGTVSQ---EPVLFS-CSVA 215
Cdd:PRK09700  280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdAVKKGMAYITEsrrDNGFFPnFSIA 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 216 ENIAY----------GADNLSSVTAQQveRAAEVANAAEFIRSfpQGFDTVVGEkgilLSGGQKQRIAIARALLKNPKIL 285
Cdd:PRK09700  360 QNMAIsrslkdggykGAMGLFHEVDEQ--RTAENQRELLALKC--HSVNQNITE----LSGGNQQKVLISKWLCCCPEVI 431

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907190441 286 LLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKNA-NFVAVLDHGKI------CEHGTHEELL 349
Cdd:PRK09700  432 IFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLtqiltnRDDMSEEEIM 503
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 145-306 8.26e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 44.78  E-value: 8.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 145 LSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLdGHDIrqlnpvwlrsKIGTVSQEPVLFscsvaeniaYGAD- 223
Cdd:PRK10636  333 LNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGI----------KLGYFAQHQLEF---------LRADe 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 224 ----NLSSVTAQQVERAaevanaaefIRSFPQGF----DTVVGEKGiLLSGGQKQRIAIARALLKNPKILLLDEATSALD 295
Cdd:PRK10636  393 splqHLARLAPQELEQK---------LRDYLGGFgfqgDKVTEETR-RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462

                         170
                  ....*....|.
gi 1907190441 296 AENEHLVQEAL 306
Cdd:PRK10636  463 LDMRQALTEAL 473
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
 2-68 1.42e-04

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: 43.02  E-value: 1.42e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907190441   2 TEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA 68
Cdd:pfam00664 201 YELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLF 267
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 257-337 1.99e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 43.66  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441  257 VGEKGILLSGGQKQRIAIARALL---KNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKNANFVA 332
Cdd:PRK00635  1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVsLGHSVIYIDHDPALLKQADYLI 1772


                   ....*
gi 1907190441  333 VLDHG 337
Cdd:PRK00635  1773 EMGPG 1777
PLN03073 PLN03073
ABC transporter F family; Provisional
 265-295 2.10e-04

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 43.31  E-value: 2.10e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907190441 265 SGGQKQRIAIARALLKNPKILLLDEATSALD 295
Cdd:PLN03073  346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
GguA NF040905
sugar ABC transporter ATP-binding protein;
121-295 2.25e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 43.24  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 121 ALEFRN--VHftYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKS-TVVSLLLRLYDPN-SGTVSLDGHDIRqlnpvwl 196
Cdd:NF040905  257 VFEVKNwtVY--HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRNiSGTVFKDGKEVD------- 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 197 rskIGTVSQepvlfscSVAENIAY--------------------GADNLSSVTAQQV-ERAAEVANAAEF-----IRSfp 250
Cdd:NF040905  328 ---VSTVSD-------AIDAGLAYvtedrkgyglnliddikrniTLANLGKVSRRGViDENEEIKVAEEYrkkmnIKT-- 395

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907190441 251 QGFDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATSALD 295
Cdd:NF040905  396 PSVFQKVGN----LSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
AAA_29 pfam13555
P-loop containing region of AAA domain;
140-178 2.36e-04

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 38.74  E-value: 2.36e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907190441 140 FQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNS 178
Cdd:pfam13555  12 FDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
149-320 2.82e-04

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 41.53  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 149 SGSVTALVGPSGSGKSTVV-SLLLRLYDPNSGTVSLDGHDIR--------------------------------QLNPVW 195
Cdd:COG0419    22 DDGLNLIVGPNGAGKSTILeAIRYALYGKARSRSKLRSDLINvgseeasvelefehggkryrierrqgefaeflEAKPSE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 196 LRSKIGTvsqepvLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVgekgiLLSGGQKQRIAIA 275
Cdd:COG0419   102 RKEALKR------LLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSGLDPIE-----TLSGGERLRLALA 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907190441 276 RALLknpkiLLLDeaTSALDAENEHLVQEALDRLMegrtvlIIAH 320
Cdd:COG0419   171 DLLS-----LILD--FGSLDEERLERLLDALEELA------IITH 202
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 264-295 2.94e-04

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 42.79  E-value: 2.94e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907190441 264 LSGGQKQRIAIARALLKNPKILLLDEATSALD 295
Cdd:PRK10982  392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
COG4639 COG4639
Predicted kinase [General function prediction only];
150-191 3.11e-04

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 40.58  E-value: 3.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907190441 150 GSVTALVGPSGSGKSTVVSlllRLYDPNSgTVSLDghDIRQL 191
Cdd:COG4639     2 LSLVVLIGLPGSGKSTFAR---RLFAPTE-VVSSD--DIRAL 37
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
 4-104 3.13e-04

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: 42.05  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   4 VEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYS 83
Cdd:cd18578   216 LEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAP 295

                          90       100
                  ....*....|....*....|.
gi 1907190441  84 ELMKGLGAGGRLWELLERQPR 104
Cdd:cd18578   296 DIAKAKAAAARIFRLLDRKPE 316
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 141-331 3.42e-04

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


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 41.47  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 141 QDFSLSIPSGSVTALVGPSGSGKST--------------VVSL-------LLRLYDPN-------SGTVSLDGHDIRQlN 192
Cdd:cd03270    12 KNVDVDIPRNKLVVITGVSGSGKSSlafdtiyaegqrryVESLsayarqfLGQMDKPDvdsieglSPAIAIDQKTTSR-N 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 193 PvwlRSKIGTVSQ----EPVLFS-CSVAENIAY----GADNLSsvtaqqVERAAEVanaaefirsfpqgfdtvvgekgil 263
Cdd:cd03270    91 P---RSTVGTVTEiydyLRLLFArVGIRERLGFlvdvGLGYLT------LSRSAPT------------------------ 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907190441 264 LSGGQKQRIAIARALLKNPK--ILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKNANFV 331
Cdd:cd03270   138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHV 208
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
 3-95 3.63e-04

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: 42.02  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAG------FFGAAGLSGnlivlsVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIG 76
Cdd:cd18552   200 EIKRFRKANERLRRLSMKIARARALssplmeLLGAIAIAL------VLWYGGYQVISGELTPGEFISFITALLLLYQPIK 273

                          90
                  ....*....|....*....
gi 1907190441  77 GLSSFYSELMKGLGAGGRL 95
Cdd:cd18552   274 RLSNVNANLQRGLAAAERI 292
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 3-68 1.53e-03

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: 40.19  E-value: 1.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA 68
Cdd:cd18563   204 EIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYL 269
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 155-181 1.57e-03

Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.


Pssm-ID: 238026  Cd Length: 137  Bit Score: 38.28  E-value: 1.57e-03
                          10        20
                  ....*....|....*....|....*..
gi 1907190441 155 LVGPSGSGKSTVVSLLLRLYDPNSGTV 181
Cdd:cd00071     4 LSGPSGVGKSTLLKRLLEEFDPNFGFS 30
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
 3-71 1.90e-03

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: 39.72  E-value: 1.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907190441   3 EVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWV 71
Cdd:cd18542   200 EIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWML 268
PRK01156 PRK01156
chromosome segregation protein; Provisional
 241-297 2.24e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.27  E-value: 2.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907190441 241 NAAEFIRSFPQGFDTvvgekgilLSGGQKQ------RIAIARALLKNPKILLLDEATSALDAE 297
Cdd:PRK01156  787 NITVSRGGMVEGIDS--------LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDED 841
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 263-329 2.66e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.95  E-value: 2.66e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907190441  263 LLSGGQKQRIAIA--RALLK-NPK-ILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNAN 329
Cdd:pfam02463 1077 LLSGGEKTLVALAliFAIQKyKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKAD 1147
Zeta_toxin pfam06414
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ...
 155-193 2.81e-03

Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.


Pssm-ID: 428926  Cd Length: 192  Bit Score: 38.50  E-value: 2.81e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907190441 155 LVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP 193
Cdd:pfam06414  16 LGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELHP 54
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 263-329 4.28e-03

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 37.83  E-value: 4.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907190441 263 LLSGGQKQRIAIAR--ALLK-NPK-ILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNAN 329
Cdd:cd03278   113 LLSGGEKALTALALlfAIFRvRPSpFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAAD 183
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
 140-187 5.43e-03

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 38.44  E-value: 5.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907190441 140 FQDFSLSIPSGsVTALVGPSGSGKSTVVSLLLRLYDPNSGTvSLDGHD 187
Cdd:COG3593    14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSR-KFDEED 59
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 264-355 6.93e-03

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 38.46  E-value: 6.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 264 LSGGQKQRIAIARAL---LKNpKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKNANFV------AV 333
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsgLTG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDlGNTLIVVEHDEDTIRAADYVidigpgAG 567

                          90       100
                  ....*....|....*....|..
gi 1907190441 334 LDHGKICEHGTHEELLLKPNGL 355
Cdd:TIGR00630 568 EHGGEVVASGTPEEILANPDSL 589
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
 3-67 7.54e-03

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: 37.81  E-value: 7.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907190441   3 EVEKYTgRVDQLLQLAQKEAL-ARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 67
Cdd:cd18549   203 EIEKFD-EGNDRFLESKKKAYkAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLY 267
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 135-193 8.43e-03

adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion protein with sulfate adenylyltransferase. Important residue (active site in E.coli) is residue 100 of the seed alignment. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 129547  Cd Length: 184  Bit Score: 37.06  E-value: 8.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907190441 135 PEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLR-LYDPNSGTVSLDGHDIRQ-LNP 193
Cdd:TIGR00455   3 PAITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKkLESKGYRVYVLDGDNVRHgLNK 63
RloC COG4694
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
137-242 9.79e-03

Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 443729 [Multi-domain]  Cd Length: 692  Bit Score: 38.18  E-value: 9.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907190441 137 VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLrlydpnsgtvSLDGHDIRQLNPVWLRSKIGTVSQEPVLF---SCS 213
Cdd:COG4694    11 VGAFKDFGWLAFFKKLNLIYGENGSGKSTLSRILR----------SLELGDTSSEVIAEFEIEAGGSAPNPSVRvfnRDF 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907190441 214 VAENIAYGADNLSSVT--AQQVERAAEVANA 242
Cdd:COG4694    81 VEENLRSGEEIKGIFTlgEENIELEEEIEEL 111
 
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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