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Conserved domains on  [gi|767912304|ref|XP_011542438|]
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ATP-binding cassette sub-family B member 10, mitochondrial isoform X3 [Homo sapiens]

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];
12-438 9.44e-177

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


:

Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 506.62  E-value: 9.44e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:COG1132  157 FVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRA 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWE 171
Cdd:COG1132  237 NLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 172 LLEREPKLPFNEGVIlNEKSFQGALEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA 251
Cdd:COG1132  317 LLDEPPEIPDPPGAV-PLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 252 SGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVV 331
Cdd:COG1132  394 SGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD---ATDEEVEEAAKAAQAHEFIEALPDGYDTVV 470

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 332 GEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQG 411
Cdd:COG1132  471 GERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDG 550

                        410       420
                 ....*....|....*....|....*..
gi 767912304 412 KITEYGKHEELLSKpNGIYRKLMNKQS 438
Cdd:COG1132  551 RIVEQGTHEELLAR-GGLYARLYRLQF 576
 
Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
12-438 9.44e-177

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 506.62  E-value: 9.44e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:COG1132  157 FVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRA 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWE 171
Cdd:COG1132  237 NLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 172 LLEREPKLPFNEGVIlNEKSFQGALEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA 251
Cdd:COG1132  317 LLDEPPEIPDPPGAV-PLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 252 SGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVV 331
Cdd:COG1132  394 SGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD---ATDEEVEEAAKAAQAHEFIEALPDGYDTVV 470

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 332 GEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQG 411
Cdd:COG1132  471 GERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDG 550

                        410       420
                 ....*....|....*....|....*..
gi 767912304 412 KITEYGKHEELLSKpNGIYRKLMNKQS 438
Cdd:COG1132  551 RIVEQGTHEELLAR-GGLYARLYRLQF 576
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 12-433 5.91e-151

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 445.32  E-value: 5.91e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:TIGR00958 297 LWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQL 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWE 171
Cdd:TIGR00958 377 NKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFE 456

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  172 LLEREPKLPFNegVILNEKSFQGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA 251
Cdd:TIGR00958 457 YLDRKPNIPLT--GTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT 534

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  252 SGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVV 331
Cdd:TIGR00958 535 GGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD---TPDEEIMAAAKAANAHDFIMEFPNGYDTEV 611

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  332 GEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEalDRLMDGRTVLVIAHRLSTIKNANMVAVLDQG 411
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKG 689

                         410       420
                  ....*....|....*....|..
gi 767912304  412 KITEYGKHEELLSKPnGIYRKL 433
Cdd:TIGR00958 690 SVVEMGTHKQLMEDQ-GCYKHL 710
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 197-437 1.21e-145

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: 414.63  E-value: 1.21e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 197 EFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGT 276
Cdd:cd03249    2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 277 VSQEPILFSCSIAENIAYGADDPssvTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNP 356
Cdd:cd03249   82 VSQEPVLFDGTIAENIRYGKPDA---TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 357 KILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMNK 436
Cdd:cd03249  159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ-KGVYAKLVKA 237


                 .
gi 767912304 437 Q 437
Cdd:cd03249  238 Q 238
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
8-437 8.79e-106

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 325.05  E-value: 8.79e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   8 CKLQFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDH 87
Cdd:PRK11176 157 FIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNR 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  88 VMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGG 167
Cdd:PRK11176 237 MRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 168 RLWELLEREPKLpfNEGVILNEKSfQGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRL 247
Cdd:PRK11176 317 TLFAILDLEQEK--DEGKRVIERA-KGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRF 392

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 248 YDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDPSSvtAEEIQRVAEVANAVAFIRNFPQGF 327
Cdd:PRK11176 393 YDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYS--REQIEEAARMAYAMDFINKMDNGL 470

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 328 NTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAV 407
Cdd:PRK11176 471 DTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILV 550

                        410       420       430
                 ....*....|....*....|....*....|
gi 767912304 408 LDQGKITEYGKHEELLSKpNGIYRKLMNKQ 437
Cdd:PRK11176 551 VEDGEIVERGTHAELLAQ-NGVYAQLHKMQ 579
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 214-366 2.86e-45

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: 154.34  E-value: 2.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  214 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFS-CSIAENI 292
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912304  293 AYGADDPSSVTAEEIQRVAEVANAVAfIRNFPqgfNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATS 366
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLG-LGDLA---DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
204-408 8.61e-25

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 100.77  E-value: 8.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 204 AYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHdirqlnpvwlrSKIGTVSQ---E 280
Cdd:NF040873   1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQrseV 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 281 PILFSCSIAENIAYG------------ADDPSSVTaEEIQRV--AEVANAVafirnfpqgfntvVGEkgvlLSGGQKQRI 346
Cdd:NF040873  67 PDSLPLTVRDLVAMGrwarrglwrrltRDDRAAVD-DALERVglADLAGRQ-------------LGE----LSGGQRQRA 128

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912304 347 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKNANMVAVL 408
Cdd:NF040873 129 LLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 223-409 2.66e-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: 2.66e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   223 SGSVTALVGPSGSGKSTVLSLLLRLYDPASGT-ISLDGHDIRQLNPVWLRskigtvsqepilfscsiaeniaygaddpss 301
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------ 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   302 vtaeeiqrvaevanavafirnfpqgfNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALD 381
Cdd:smart00382  51 --------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 767912304   382 RLMD-------GRTVLVIAHRLSTIKNANMVAVLD 409
Cdd:smart00382 105 LRLLlllksekNLTVILTTNDEKDLGPALLRRRFD 139
GguA NF040905
sugar ABC transporter ATP-binding protein;
209-415 7.68e-14

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 73.29  E-value: 7.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 209 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYdPA---SGTISLDG-----HDIRQLNpvwlRSKIGTVSQE 280
Cdd:NF040905  12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfKDIRDSE----ALGIVIIHQE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 281 ----PILfscSIAENI-------AYGADDPSSVTAEEIQRVAEVAnavafIRNFPQgfnTVVGEKGVllsgGQKQRIAIA 349
Cdd:NF040905  87 laliPYL---SIAENIflgneraKRGVIDWNETNRRARELLAKVG-----LDESPD---TLVTDIGV----GKQQLVEIA 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912304 350 RALLKNPKILLLDEATSAL-DAENEYLvqeaLDRLMD----GRTVLVIAHRLSTI-KNANMVAVLDQGKITE 415
Cdd:NF040905 152 KALSKDVKLLILDEPTAALnEEDSAAL----LDLLLElkaqGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
216-369 2.03e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 53.59  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 216 DFSLSIPSGSVTALVGPSGSGKSTVLSLLlrlydpA------SGTISLDGHDI------RQLNPvwlrsKIGTVSQ---- 279
Cdd:NF033858  19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLI------AgarkiqQGRVEVLGGDMadarhrRAVCP-----RIAYMPQglgk 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 280 --EPILfscSIAENIA-----YGADdpssvTAEEIQRVAEVANAV---AFiRNFPQGfntvvgeKgvlLSGGQKQRIAIA 349
Cdd:NF033858  88 nlYPTL---SVFENLDffgrlFGQD-----AAERRRRIDELLRATglaPF-ADRPAG-------K---LSGGMKQKLGLC 148

                        170       180
                 ....*....|....*....|
gi 767912304 350 RALLKNPKILLLDEATSALD 369
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVD 168
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
332-428 3.19e-07

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 52.04  E-value: 3.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 332 GEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLV-QEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLD 409
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVID 218

                         90
                 ....*....|....*....
gi 767912304 410 QGKITEYGKHEELLSKPNG 428
Cdd:NF000106 219 RGRVIADGKVDELKTKVGG 237
GguA NF040905
sugar ABC transporter ATP-binding protein;
195-392 8.50e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 44.78  E-value: 8.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKN--VHfaYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKsTVL--SLLLRLYDP-ASGTISLDGHDIRqlnpvw 269
Cdd:NF040905 257 VFEVKNwtVY--HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGR-TELamSVFGRSYGRnISGTVFKDGKEVD------ 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 270 lrskIGTVSQepilfscSIAENIAYGADD------------PSSVTAEEIQRVAE--VANAVAFIR---NFPQGFNT--- 329
Cdd:NF040905 328 ----VSTVSD-------AIDAGLAYVTEDrkgyglnliddiKRNITLANLGKVSRrgVIDENEEIKvaeEYRKKMNIktp 396

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912304 330 VVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVI 392
Cdd:NF040905 397 SVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAeGKGVIVI 460
 
Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
12-438 9.44e-177

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 506.62  E-value: 9.44e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:COG1132  157 FVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRA 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWE 171
Cdd:COG1132  237 NLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 172 LLEREPKLPFNEGVIlNEKSFQGALEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA 251
Cdd:COG1132  317 LLDEPPEIPDPPGAV-PLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 252 SGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVV 331
Cdd:COG1132  394 SGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD---ATDEEVEEAAKAAQAHEFIEALPDGYDTVV 470

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 332 GEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQG 411
Cdd:COG1132  471 GERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDG 550

                        410       420
                 ....*....|....*....|....*..
gi 767912304 412 KITEYGKHEELLSKpNGIYRKLMNKQS 438
Cdd:COG1132  551 RIVEQGTHEELLAR-GGLYARLYRLQF 576
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 12-433 5.91e-151

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 445.32  E-value: 5.91e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:TIGR00958 297 LWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQL 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWE 171
Cdd:TIGR00958 377 NKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFE 456

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  172 LLEREPKLPFNegVILNEKSFQGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA 251
Cdd:TIGR00958 457 YLDRKPNIPLT--GTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT 534

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  252 SGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVV 331
Cdd:TIGR00958 535 GGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD---TPDEEIMAAAKAANAHDFIMEFPNGYDTEV 611

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  332 GEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEalDRLMDGRTVLVIAHRLSTIKNANMVAVLDQG 411
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKG 689

                         410       420
                  ....*....|....*....|..
gi 767912304  412 KITEYGKHEELLSKPnGIYRKL 433
Cdd:TIGR00958 690 SVVEMGTHKQLMEDQ-GCYKHL 710
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 197-437 1.21e-145

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: 414.63  E-value: 1.21e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 197 EFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGT 276
Cdd:cd03249    2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 277 VSQEPILFSCSIAENIAYGADDPssvTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNP 356
Cdd:cd03249   82 VSQEPVLFDGTIAENIRYGKPDA---TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 357 KILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMNK 436
Cdd:cd03249  159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ-KGVYAKLVKA 237


                 .
gi 767912304 437 Q 437
Cdd:cd03249  238 Q 238
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
 12-437 2.46e-145

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: 426.42  E-value: 2.46e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:TIGR02204 154 FITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEA 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   92 ARKEAFARAGffgatgLSGNLIVLS------VLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGA 165
Cdd:TIGR02204 234 ARQRIRTRAL------LTAIVIVLVfgaivgVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGA 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  166 GGRLWELLEREPKLPFNEGVILNEKSFQGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLL 245
Cdd:TIGR02204 308 AERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLL 387

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  246 RLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQ 325
Cdd:TIGR02204 388 RFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPD---ATDEEVEAAARAAHAHEFISALPE 464

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  326 GFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMV 405
Cdd:TIGR02204 465 GYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRI 544

                         410       420       430
                  ....*....|....*....|....*....|..
gi 767912304  406 AVLDQGKITEYGKHEELLSKpNGIYRKLMNKQ 437
Cdd:TIGR02204 545 VVMDQGRIVAQGTHAELIAK-GGLYARLARLQ 575
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 12-437 9.77e-136

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 406.14  E-value: 9.77e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:COG2274  291 FFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNA 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWE 171
Cdd:COG2274  371 RFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDD 450

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 172 LLEREPKLPFNEGVILNEKsFQGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA 251
Cdd:COG2274  451 ILDLPPEREEGRSKLSLPR-LKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT 528

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 252 SGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVV 331
Cdd:COG2274  529 SGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD---ATDEEIIEAARLAGLHDFIEALPMGYDTVV 605

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 332 GEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQG 411
Cdd:COG2274  606 GEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKG 685

                        410       420
                 ....*....|....*....|....*.
gi 767912304 412 KITEYGKHEELLSKpNGIYRKLMNKQ 437
Cdd:COG2274  686 RIVEDGTHEELLAR-KGLYAELVQQQ 710
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 12-437 4.43e-122

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: 366.73  E-value: 4.43e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:TIGR02203 150 LYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRL 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWE 171
Cdd:TIGR02203 230 AMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFT 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  172 LLEREPKLpfNEGVILNEKSfQGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA 251
Cdd:TIGR02203 310 LLDSPPEK--DTGTRAIERA-RGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  252 SGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGAddPSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVV 331
Cdd:TIGR02203 386 SGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR--TEQADRAEIERALAAAYAQDFVDKLPLGLDTPI 463

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  332 GEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQG 411
Cdd:TIGR02203 464 GENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDG 543

                         410       420
                  ....*....|....*....|....*.
gi 767912304  412 KITEYGKHEELLSKpNGIYRKLMNKQ 437
Cdd:TIGR02203 544 RIVERGTHNELLAR-NGLYAQLHNMQ 568
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 196-433 1.74e-118

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: 345.37  E-value: 1.74e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 275
Cdd:cd03251    1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKN 355
Cdd:cd03251   80 LVSQDVFLFNDTVAENIAYGRPG---ATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304 356 PKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKL 433
Cdd:cd03251  157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKL 233
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 64-438 4.17e-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: 337.18  E-value: 4.17e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  64 NVRTVRAFGKEMTEIEKYASkvdhvmQLARKEAFARAGFfgaTGLSGNLIVLSVLYKGGL--LMGSA-------HMTVGE 134
Cdd:COG5265  227 NYETVKYFGNEAREARRYDE------ALARYERAAVKSQ---TSLALLNFGQALIIALGLtaMMLMAaqgvvagTMTVGD 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 135 L---SSFLMYAFwvgISIGGLSSFYSELMKGLGAGGRLWELLEREPK---------LPFNegvilneksfQGALEFKNVH 202
Cdd:COG5265  298 FvlvNAYLIQLY---IPLNFLGFVYREIRQALADMERMFDLLDQPPEvadapdappLVVG----------GGEVRFENVS 364

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 203 FAYpaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPI 282
Cdd:COG5265  365 FGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTV 442

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 283 LFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLD 362
Cdd:COG5265  443 LFNDTIAYNIAYGRPD---ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFD 519

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 363 EATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMNKQS 438
Cdd:COG5265  520 EATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ-GGLYAQMWARQQ 594
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 196-437 4.95e-110

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: 323.80  E-value: 4.95e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 275
Cdd:cd03253    1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKN 355
Cdd:cd03253   79 VVPQDTVLFNDTIGYNIRYGRPD---ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 356 PKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMN 435
Cdd:cd03253  156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK-GGLYAEMWK 234


                 ..
gi 767912304 436 KQ 437
Cdd:cd03253  235 AQ 236
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
8-437 8.79e-106

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 325.05  E-value: 8.79e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   8 CKLQFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDH 87
Cdd:PRK11176 157 FIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNR 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  88 VMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGG 167
Cdd:PRK11176 237 MRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 168 RLWELLEREPKLpfNEGVILNEKSfQGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRL 247
Cdd:PRK11176 317 TLFAILDLEQEK--DEGKRVIERA-KGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRF 392

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 248 YDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDPSSvtAEEIQRVAEVANAVAFIRNFPQGF 327
Cdd:PRK11176 393 YDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYS--REQIEEAARMAYAMDFINKMDNGL 470

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 328 NTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAV 407
Cdd:PRK11176 471 DTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILV 550

                        410       420       430
                 ....*....|....*....|....*....|
gi 767912304 408 LDQGKITEYGKHEELLSKpNGIYRKLMNKQ 437
Cdd:PRK11176 551 VEDGEIVERGTHAELLAQ-NGVYAQLHKMQ 579
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 194-425 4.64e-103

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: 306.07  E-value: 4.64e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 194 GALEFKNVHFAYpaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSK 273
Cdd:cd03254    1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGTVSQEPILFSCSIAENIAYGADDPssvTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALL 353
Cdd:cd03254   79 IGVVLQDTFLFSGTIMENIRLGRPNA---TDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAML 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912304 354 KNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSK 425
Cdd:cd03254  156 RDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 152-425 7.32e-102

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: 314.39  E-value: 7.32e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 152 LSSFYSELMKGLGAGGRLWELLEREPKLPFNEGVILNEKSfQGALEFKNVHFAYPARPevPIFQDFSLSIPSGSVTALVG 231
Cdd:COG4988  294 LGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVG 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 232 PSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVA 311
Cdd:COG4988  371 PSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPD---ASDEELEAAL 447

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 312 EVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLV 391
Cdd:COG4988  448 EAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVIL 527

                        250       260       270
                 ....*....|....*....|....*....|....
gi 767912304 392 IAHRLSTIKNANMVAVLDQGKITEYGKHEELLSK 425
Cdd:COG4988  528 ITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 13-435 1.68e-96

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: 300.91  E-value: 1.68e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  13 FVSPNLA-----TFVLSVVppvsIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDH 87
Cdd:COG4987  152 FFSPALAlvlalGLLLAGL----LLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEAR 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  88 VMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGG 167
Cdd:COG4987  228 LAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAAR 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 168 RLWELLEREPKLPFNEGVILNEKsfQGALEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRL 247
Cdd:COG4987  308 RLNELLDAPPAVTEPAEPAPAPG--GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF 384

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 248 YDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGF 327
Cdd:COG4987  385 LDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD---ATDEELWAALERVGLGDWLAALPDGL 461

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 328 NTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAV 407
Cdd:COG4987  462 DTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILV 541

                        410       420
                 ....*....|....*....|....*...
gi 767912304 408 LDQGKITEYGKHEELLSKpNGIYRKLMN 435
Cdd:COG4987  542 LEDGRIVEQGTHEELLAQ-NGRYRQLYQ 568
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 1-438 9.00e-95

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: 299.74  E-value: 9.00e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304    1 MPFVSTSCKLQFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEK 80
Cdd:TIGR01846 263 LLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNR 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   81 YASKVdhVMQLARKEAFARAGFFG--ATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSE 158
Cdd:TIGR01846 343 WDRQL--AAYVAASFRVTNLGNIAgqAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQD 420

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  159 LMKGLGAGGRLWELLErEPKLPFNEGVILNEKsFQGALEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGK 237
Cdd:TIGR01846 421 FQQTGIALERLGDILN-SPTEPRSAGLAALPE-LRGAITFENIRFRY--APDSPeVLSNLNLDIKPGEFIGIVGPSGSGK 496

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  238 STVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGadDPSsVTAEEIQRVAEVANAV 317
Cdd:TIGR01846 497 STLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALC--NPG-APFEHVIHAAKLAGAH 573

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  318 AFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLS 397
Cdd:TIGR01846 574 DFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLS 653

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 767912304  398 TIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMNKQS 438
Cdd:TIGR01846 654 TVRACDRIIVLEKGQIAESGRHEELLAL-QGLYARLWQQQS 693
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 196-412 1.77e-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: 274.26  E-value: 1.77e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 275
Cdd:cd03228    1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILFSCSIAENIaygaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIARALLKN 355
Cdd:cd03228   80 YVPQDPFLFSGTIRENI---------------------------------------------LSGGQRQRIAIARALLRD 114

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304 356 PKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGK 412
Cdd:cd03228  115 PPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 187-413 2.72e-89

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: 270.88  E-value: 2.72e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 187 LNEKSFQGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLN 266
Cdd:cd03248    3 LAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 267 PVWLRSKIGTVSQEPILFSCSIAENIAYGAddpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRI 346
Cdd:cd03248   83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGL---QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304 347 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKI 413
Cdd:cd03248  160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 196-437 3.89e-89

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: 270.90  E-value: 3.89e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKI 274
Cdd:cd03252    1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQEPILFSCSIAENIAYGADDPSsvtAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLK 354
Cdd:cd03252   79 GVVLQENVLFNRSIRDNIALADPGMS---MERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIH 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 355 NPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLM 434
Cdd:cd03252  156 NPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLY 234


                 ...
gi 767912304 435 NKQ 437
Cdd:cd03252  235 QLQ 237
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
10-440 1.16e-88

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 281.08  E-value: 1.16e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  10 LQFFvSPNLATFV-LSVVPPVSI------------IAVIY---GRYLRKLTKVTQDSL-AQATQLAE---ERIGNVRTVR 69
Cdd:PRK13657 131 LEFM-REHLATLVaLVVLLPLALfmnwrlslvlvvLGIVYtliTTLVMRKTKDGQAAVeEHYHDLFAhvsDAIGNVSVVQ 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  70 AFGKEMTEIEKYASKVDHVM--QLARKEAFARAGffGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAfwvGI 147
Cdd:PRK13657 210 SYNRIEAETQALRDIADNLLaaQMPVLSWWALAS--VLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFA---TL 284

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 148 SIGGL---SSFYSELMKglgAGGRLWELLEREPKLPFNE---GVIlNEKSFQGALEFKNVHFAYPARPevPIFQDFSLSI 221
Cdd:PRK13657 285 LIGRLdqvVAFINQVFM---AAPKLEEFFEVEDAVPDVRdppGAI-DLGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEA 358

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 222 PSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpss 301
Cdd:PRK13657 359 KPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD--- 435

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 302 VTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALD 381
Cdd:PRK13657 436 ATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALD 515

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767912304 382 RLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMNKQSFI 440
Cdd:PRK13657 516 ELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR-GGRFAALLRAQGML 573
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
 12-169 1.11e-83

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: 258.60  E-value: 1.11e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18573  137 LYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDL 216

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 169
Cdd:cd18573  217 AKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 194-413 1.03e-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: 238.26  E-value: 1.03e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 194 GALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSK 273
Cdd:cd03245    1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGTVSQEPILFSCSIAENIAYGAddpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALL 353
Cdd:cd03245   80 IGYVPQDVTLFYGTLRDNITLGA---PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 354 KNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKI 413
Cdd:cd03245  157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
28-437 7.84e-76

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 246.93  E-value: 7.84e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  28 PVSIIAVI---YGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHV----MQLARKEAFARA 100
Cdd:PRK10789 146 PMPVMAIMikrYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTgkknMRVARIDARFDP 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 101 GFFGATGLSgNLIVLSvlykGGLLM---GSahMTVGELSSFLMYafwVGISIG---GLSSFYSELMKGLGAGGRLWELLE 174
Cdd:PRK10789 226 TIYIAIGMA-NLLAIG----GGSWMvvnGS--LTLGQLTSFVMY---LGLMIWpmlALAWMFNIVERGSAAYSRIRAMLA 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 175 REPKLPFNEGVILNEKsfqGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGT 254
Cdd:PRK10789 296 EAPVVKDGSEPVPEGR---GELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD 371

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 255 ISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEK 334
Cdd:PRK10789 372 IRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPD---ATQQEIEHVARLASVHDDILRLPQGYDTEVGER 448

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 335 GVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKIT 414
Cdd:PRK10789 449 GVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIA 528

                        410       420
                 ....*....|....*....|...
gi 767912304 415 EYGKHEELLSKPnGIYRKLMNKQ 437
Cdd:PRK10789 529 QRGNHDQLAQQS-GWYRDMYRYQ 550
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 152-408 1.35e-71

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: 234.87  E-value: 1.35e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  152 LSSFYSELMKGLGAGGRLWELLEREPkLPFNEGVILNEKSFQgALEFKNVHFAYPARPEVPifQDFSLSIPSGSVTALVG 231
Cdd:TIGR02857 280 LGAQYHARADGVAAAEALFAVLDAAP-RPLAGKAPVTAAPAS-SLEFSGVSVAYPGRRPAL--RPVSFTVPPGERVALVG 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  232 PSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVA 311
Cdd:TIGR02857 356 PSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPD---ASDAEIREAL 432

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  312 EVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLV 391
Cdd:TIGR02857 433 ERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLL 512

                         250
                  ....*....|....*..
gi 767912304  392 IAHRLSTIKNANMVAVL 408
Cdd:TIGR02857 513 VTHRLALAALADRIVVL 529
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 117-433 5.32e-70

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


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 234.84  E-value: 5.32e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  117 VLYKGGLLMGSAHMTVGELSSFLmyafwvgiSIggLSSFYSELMKGLGAGGRLWEL---LER---------EPKLPFNEG 184
Cdd:TIGR03796 394 ILVVGGLRVMEGQLTIGMLVAFQ--------SL--MSSFLEPVNNLVGFGGTLQELegdLNRlddvlrnpvDPLLEEPEG 463

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  185 VILNEKS---FQGALEFKNVHFAYpARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHD 261
Cdd:TIGR03796 464 SAATSEPprrLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIP 542

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  262 IRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGadDPSsVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGG 341
Cdd:TIGR03796 543 REEIPREVLANSVAMVDQDIFLFEGTVRDNLTLW--DPT-IPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGG 619

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  342 QKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRlmDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEE 421
Cdd:TIGR03796 620 QRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEE 697

                         330
                  ....*....|..
gi 767912304  422 LLSKPnGIYRKL 433
Cdd:TIGR03796 698 LWAVG-GAYARL 708
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 194-417 2.60e-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: 219.29  E-value: 2.60e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 194 GALEFKNVHFAYpaRPE-VPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS 272
Cdd:cd03244    1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 273 KIGTVSQEPILFSCSIAENIaygadDP-SSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARA 351
Cdd:cd03244   79 RISIIPQDPVLFSGTIRSNL-----DPfGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 352 LLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYG 417
Cdd:cd03244  154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 31-425 1.38e-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: 227.71  E-value: 1.38e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  31 IIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGkeMTE--IEKYASKVDHVMQLARKeAFARAGFFGATGL 108
Cdd:COG4618  170 ALALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVIEAMG--MLPalRRRWQRANARALALQAR-ASDRAGGFSALSK 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 109 SGNLIVLS-VLYKGGLLMGSAHMTVGEL--SSFLMyafwvG-------ISIGGLSSFyselMKGLGAGGRLWELLEREPK 178
Cdd:COG4618  247 FLRLLLQSaVLGLGAYLVIQGEITPGAMiaASILM-----GralapieQAIGGWKQF----VSARQAYRRLNELLAAVPA 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 179 LPfnEGVILNEksFQGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLD 258
Cdd:COG4618  318 EP--ERMPLPR--PKGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD 392

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 259 GHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIA-YGADDPssvtaEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVL 337
Cdd:COG4618  393 GADLSQWDREELGRHIGYLPQDVELFDGTIAENIArFGDADP-----EKVVAAAKLAGVHEMILRLPDGYDTRIGEGGAR 467

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 338 LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTIKNANMVAVLDQGKITEY 416
Cdd:COG4618  468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547


                 ....*....
gi 767912304 417 GKHEELLSK 425
Cdd:COG4618  548 GPRDEVLAR 556
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
 10-437 1.93e-68

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: 230.23  E-value: 1.93e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   10 LQFFVSPNLATF-VLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAE--ERIGNVRT----VRAFGKEMteiEKYA 82
Cdd:TIGR03797 269 LMFYYSWKLALVaVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQliNGISKLRVagaeNRAFARWA---KLFS 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   83 SKVDHVMqlarkeAFARAGFFGATGLSGNLIVLSVL--YKGGLLMGSAHMTVGELSSFlMYAFwvGISIGGLSSFYSELM 160
Cdd:TIGR03797 346 RQRKLEL------SAQRIENLLTVFNAVLPVLTSAAlfAAAISLLGGAGLSLGSFLAF-NTAF--GSFSGAVTQLSNTLI 416

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  161 KGLGAGgRLWE----LLEREPKlpfNEGVILNEKSFQGALEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGS 235
Cdd:TIGR03797 417 SILAVI-PLWErakpILEALPE---VDEAKTDPGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGS 490

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  236 GKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGAddpsSVTAEEIQRVAEVAN 315
Cdd:TIGR03797 491 GKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA----PLTLDEAWEAARMAG 566

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  316 AVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLmdGRTVLVIAHR 395
Cdd:TIGR03797 567 LAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHR 644

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 767912304  396 LSTIKNANMVAVLDQGKITEYGKHEELLSKPnGIYRKLMNKQ 437
Cdd:TIGR03797 645 LSTIRNADRIYVLDAGRVVQQGTYDELMARE-GLFAQLARRQ 685
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
 114-434 5.29e-66

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: 221.69  E-value: 5.29e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  114 VLSVLYKGGLLMGSAHMTVGELSSFLMYAfwvGISIGGLSSFYSELMKGLGAGGRLWELLEREPKL-----PFNEGVILN 188
Cdd:TIGR01192 254 MMCILVIGTVLVIKGELSVGEVIAFIGFA---NLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVfqreePADAPELPN 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  189 EKsfqGALEFKNVHFAYPARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV 268
Cdd:TIGR01192 331 VK---GAVEFRHITFEFANSSQG--VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRE 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  269 WLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAI 348
Cdd:TIGR01192 406 SLRKSIATVFQDAGLFNRSIRENIRLGREG---ATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAI 482

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  349 ARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNG 428
Cdd:TIGR01192 483 ARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK-DG 561


                  ....*.
gi 767912304  429 IYRKLM 434
Cdd:TIGR01192 562 RFYKLL 567
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
18-425 3.64e-65

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 219.59  E-value: 3.64e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  18 LATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNV------RTVRAFGKEMTEiekyASKvDHVMql 91
Cdd:PRK10790 167 MALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMsviqqfRQQARFGERMGE----ASR-SHYM-- 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  92 ARKEAFARAGFFgatgLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFwvgISIGG--------LSSFYSELMKGL 163
Cdd:PRK10790 240 ARMQTLRLDGFL----LRPLLSLFSALILCGLLMLFGFSASGTIEVGVLYAF---ISYLGrlneplieLTTQQSMLQQAV 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 164 GAGGRLWELLERePKLPFNEGVILNEksfQGALEFKNVHFAYpaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSL 243
Cdd:PRK10790 313 VAGERVFELMDG-PRQQYGNDDRPLQ---SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASL 386

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 244 LLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADdpssVTAEEIQRVAEVANAVAFIRNF 323
Cdd:PRK10790 387 LMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD----ISEEQVWQALETVQLAELARSL 462

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 324 PQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNAN 403
Cdd:PRK10790 463 PDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEAD 542

                        410       420
                 ....*....|....*....|..
gi 767912304 404 MVAVLDQGKITEYGKHEELLSK 425
Cdd:PRK10790 543 TILVLHRGQAVEQGTHQQLLAA 564
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 12-435 5.74e-63

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: 215.76  E-value: 5.74e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   12 FFVSPNLATFVLSVVP-PVSIIAVIYgrYLRKLTKVTQDSLAQATQLAE---ERIGNVRTVRAFGKEMTEIEKYASKVDH 87
Cdd:TIGR01193 289 FLVRQNMLLFLLSLLSiPVYAVIIIL--FKRTFNKLNHDAMQANAVLNSsiiEDLNGIETIKSLTSEAERYSKIDSEFGD 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   88 VMQLARKEAFARAGFfGATGLSGNLIV-LSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAG 166
Cdd:TIGR01193 367 YLNKSFKYQKADQGQ-QAIKAVTKLILnVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVAN 445

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  167 GRLWE--LLEREpklpFNEGVILNEKS-FQGALEFKNVHFAYPARPevPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSL 243
Cdd:TIGR01193 446 NRLNEvyLVDSE----FINKKKRTELNnLNGDIVINDVSYSYGYGS--NILSDISLTIKMNSKTTIVGMSGSGKSTLAKL 519

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  244 LLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpsSVTAEEIQRVAEVANAVAFIRNF 323
Cdd:TIGR01193 520 LVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKE--NVSQDEIWAACEIAEIKDDIENM 597

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  324 PQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDgRTVLVIAHRLSTIKNAN 403
Cdd:TIGR01193 598 PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSD 676

                         410       420       430
                  ....*....|....*....|....*....|..
gi 767912304  404 MVAVLDQGKITEYGKHEELLsKPNGIYRKLMN 435
Cdd:TIGR01193 677 KIIVLDHGKIIEQGSHDELL-DRNGFYASLIH 707
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 168-437 6.75e-63

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 213.15  E-value: 6.75e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 168 RLWELLEREPKLPFNEGVilNEKSFQGALEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRL 247
Cdd:PRK11160 313 RINEITEQKPEVTFPTTS--TAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRA 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 248 YDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDPSSvtaeeiQRVAEVANAV--AFIRNFPQ 325
Cdd:PRK11160 390 WDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASD------EALIEVLQQVglEKLLEDDK 463

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 326 GFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMV 405
Cdd:PRK11160 464 GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRI 543

                        250       260       270
                 ....*....|....*....|....*....|..
gi 767912304 406 AVLDQGKITEYGKHEELLSKpNGIYRKLMNKQ 437
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLAQ-QGRYYQLKQRL 574
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 57-432 4.32e-62

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 217.97  E-value: 4.32e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   57 LAEERIGNVRTVRAFGKE---MTEIEKyasKVDHVMQLARKEAFARAGFFGATGlSGNLIVLSVLYK-GGLLMGSAHMTV 132
Cdd:PTZ00265 1024 LIQEAFYNMNTVIIYGLEdyfCNLIEK---AIDYSNKGQKRKTLVNSMLWGFSQ-SAQLFINSFAYWfGSFLIRRGTILV 1099

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  133 GELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLPF--NEGV-ILNEKSFQGALEFKNVHFAYPARP 209
Cdd:PTZ00265 1100 DDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVrdNGGIrIKNKNDIKGKIEIMDVNFRYISRP 1179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  210 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD---------------------------------------- 249
Cdd:PTZ00265 1180 NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefs 1259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  250 --------------PASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVAN 315
Cdd:PTZ00265 1260 ltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED---ATREDVKRACKFAA 1336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  316 AVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIA 393
Cdd:PTZ00265 1337 IDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIA 1416

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 767912304  394 HRLSTIKNANMVAVLDQGK-----ITEYGKHEELLSKPNGIYRK 432
Cdd:PTZ00265 1417 HRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVYKK 1460
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 22-425 9.17e-62

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: 209.51  E-value: 9.17e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   22 VLSVVPPVSIiAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFG-------KEMTEIEKYASkvdhvmqlARK 94
Cdd:TIGR01842 148 LGGAVVLVGL-ALLNNRATKKPLKEATEASIRANNLADSALRNAEVIEAMGmmgnltkRWGRFHSKYLS--------AQS 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   95 EAFARAGFFGATGLSGNLIVLS-VLYKGGLLMGSAHMTVGEL--SSFLMYAFWVGI--SIGGLSSFyselMKGLGAGGRL 169
Cdd:TIGR01842 219 AASDRAGMLSNLSKYFRIVLQSlVLGLGAYLAIDGEITPGMMiaGSILVGRALAPIdgAIGGWKQF----SGARQAYKRL 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  170 WELLEREP------KLPFNEGVILNEksfqgalefkNVHFAyPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSL 243
Cdd:TIGR01842 295 NELLANYPsrdpamPLPEPEGHLSVE----------NVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARL 363

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  244 LLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNF 323
Cdd:TIGR01842 364 IVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGEN---ADPEKIIEAAKLAGVHELILRL 440

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  324 PQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTIKNA 402
Cdd:TIGR01842 441 PDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCV 520

                         410       420
                  ....*....|....*....|...
gi 767912304  403 NMVAVLDQGKITEYGKHEELLSK 425
Cdd:TIGR01842 521 DKILVLQDGRIARFGERDEVLAK 543
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 12-441 3.58e-61

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 215.28  E-value: 3.58e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLrKLTKVTQDSLAQAT-QLAEERIGNVRTVRAFGKEMTEIEKYaskvdHVMQ 90
Cdd:PTZ00265  193 LFKNARLTLCITCVFPLIYICGVICNKKV-KINKKTSLLYNNNTmSIIEEALVGIRTVVSYCGEKTILKKF-----NLSE 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   91 LARKEAFARAGFFGA--TGLSGNLIVLSvlYKGGLLMGSaHMTVGELSSF-----LMYAFWVGISIGGLSSFY------- 156
Cdd:PTZ00265  267 KLYSKYILKANFMESlhIGMINGFILAS--YAFGFWYGT-RIIISDLSNQqpnndFHGGSVISILLGVLISMFmltiilp 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  157 --SELMKGLGAGGRLWELLEREPKLPFN-EGVILNEKSfqgALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPS 233
Cdd:PTZ00265  344 niTEYMKSLEATNSLYEIINRKPLVENNdDGKKLKDIK---KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGES 420

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  234 GSGKSTVLSLLLRLYDPASGTISL-DGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAY------------------ 294
Cdd:PTZ00265  421 GCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyyned 500

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  295 ------GADDPSSVTAE---------------------------EIQRVAEVANAVA---FIRNFPQGFNTVVGEKGVLL 338
Cdd:PTZ00265  501 gndsqeNKNKRNSCRAKcagdlndmsnttdsneliemrknyqtiKDSEVVDVSKKVLihdFVSALPDKYETLVGSNASKL 580

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  339 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTIKNANMVAVL-------- 408
Cdd:PTZ00265  581 SGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrergst 660

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912304  409 ----------------------DQGK-----------------ITEYGKHEELLSKPNGIYRKLMNKQSFIS 441
Cdd:PTZ00265  661 vdvdiigedptkdnkennnknnKDDNnnnnnnnnnkinnagsyIIEQGTHDALMKNKNGIYYTMINNQKVSS 732
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
 12-169 2.77e-59

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: 195.47  E-value: 2.77e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18557  132 FILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRL 211

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 169
Cdd:cd18557  212 ARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 196-413 7.20e-57

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: 185.11  E-value: 7.20e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 275
Cdd:cd03246    1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILFSCSIAENIaygaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIARALLKN 355
Cdd:cd03246   80 YLPQDDELFSGSIAENI---------------------------------------------LSGGQRQRLGLARALYGN 114

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767912304 356 PKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTIKNANMVAVLDQGKI 413
Cdd:cd03246  115 PRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 196-432 2.64e-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: 193.97  E-value: 2.64e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARP--EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV---WL 270
Cdd:COG1123  261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrEL 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 271 RSKIGTVSQEPilFSC-----SIAENIAYGADDPSSVTAEEI-QRVAEVANAV----AFIRNFPQGFntvvgekgvllSG 340
Cdd:COG1123  341 RRRVQMVFQDP--YSSlnprmTVGDIIAEPLRLHGLLSRAERrERVAELLERVglppDLADRYPHEL-----------SG 407

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 341 GQKQRIAIARALLKNPKILLLDEATSALDaeneYLVQEA-LDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 413
Cdd:COG1123  408 GQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQiLNLLRDlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRI 483

                        250
                 ....*....|....*....
gi 767912304 414 TEYGKHEELLSKPNGIYRK 432
Cdd:COG1123  484 VEDGPTEEVFANPQHPYTR 502
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 196-426 1.64e-54

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: 180.99  E-value: 1.64e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 275
Cdd:COG1122    1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPI--LFSCSIAENIAYGaddP--SSVTAEEI-QRVAEVANAV---AFIRNFPQgfntvvgekgvLLSGGQKQRIA 347
Cdd:COG1122   79 LVFQNPDdqLFAPTVEEDVAFG---PenLGLPREEIrERVEEALELVgleHLADRPPH-----------ELSGGQKQRVA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 348 IARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSK 425
Cdd:COG1122  145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSD 224


                 .
gi 767912304 426 P 426
Cdd:COG1122  225 Y 225
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
196-394 1.93e-54

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: 1.93e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 275
Cdd:COG4619    1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILFSCSIAENIAYgaddPSSVTAEEIQRvaevANAVAFIRNFpqGFNTVVGEKGV-LLSGGQKQRIAIARALLK 354
Cdd:COG4619   78 YVPQEPALWGGTVRDNLPF----PFQLRERKFDR----ERALELLERL--GLPPDILDKPVeRLSGGERQRLALIRALLL 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767912304 355 NPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAH 394
Cdd:COG4619  148 QPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSH 189
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
 12-168 4.26e-54

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: 182.06  E-value: 4.26e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18780  138 FTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLL 217

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGR 168
Cdd:cd18780  218 GKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVR 294
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 218-437 2.78e-53

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 187.36  E-value: 2.78e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 218 SLSIPSGSVTALVGPSGSGKSTVLSLLLRlYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGAd 297
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN- 447

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 298 dpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQ 377
Cdd:PRK11174 448 --PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 378 EALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYRKLMNKQ 437
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQ 585
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 196-422 2.54e-51

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: 172.75  E-value: 2.54e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD-----PASGTISLDGHDIRQL--NPV 268
Cdd:cd03260    1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLdvDVL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 269 WLRSKIGTVSQEPILFSCSIAENIAYGADDPSSVTAEEI-QRVAEVANAVAFIRNfpqgfntvVGEK--GVLLSGGQKQR 345
Cdd:cd03260   78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELdERVEEALRKAALWDE--------VKDRlhALGLSGGQQQR 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304 346 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEEL 422
Cdd:cd03260  150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 25-396 4.33e-51

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: 180.63  E-value: 4.33e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   25 VVPPVSIIAV-IYGRYLRKL-TKVTQDSLAQATQLAEERI-----GNVRTVRAFGKEMTEIEKYASKVDHVMQlarkeaf 97
Cdd:TIGR02868 169 VAPLVSLRAArAAEQALARLrGELAAQLTDALDGAAELVAsgalpAALAQVEEADRELTRAERRAAAATALGA------- 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   98 aragffGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLE--- 174
Cdd:TIGR02868 242 ------ALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDaag 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  175 --REPKLPFNEGVILNEKSfqgaLEFKNVHFAYPARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPAS 252
Cdd:TIGR02868 316 pvAEGSAPAAGAVGLGKPT----LELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  253 GTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVG 332
Cdd:TIGR02868 390 GEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPD---ATDEELWAALERVGLADWLRALPDGLDTVLG 466

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912304  333 EKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRL 396
Cdd:TIGR02868 467 EGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 196-426 1.31e-50

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: 171.22  E-value: 1.31e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---R 271
Cdd:cd03258    2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 272 SKIGTVSQEPILFSC-SIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIA 347
Cdd:cd03258   82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELVgleDKADAYPAQ-----------LSGGQKQRVG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 348 IARALLKNPKILLLDEATSALDAENeylVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEE 421
Cdd:cd03258  151 IARALANNPKVLLCDEATSALDPET---TQSILALLRDinrelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227


                 ....*
gi 767912304 422 LLSKP 426
Cdd:cd03258  228 VFANP 232
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
196-426 4.35e-50

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 172.95  E-value: 4.35e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---R 271
Cdd:COG1135    2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 272 SKIGTVSQEPILF-SCSIAENIAYgaddP---SSVTAEEI-QRVAEVANAV---AFIRNFP-QgfntvvgekgvlLSGGQ 342
Cdd:COG1135   82 RKIGMIFQHFNLLsSRTVAENVAL----PleiAGVPKAEIrKRVAELLELVglsDKADAYPsQ------------LSGGQ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 343 KQRIAIARALLKNPKILLLDEATSALDAENeylVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEY 416
Cdd:COG1135  146 KQRVGIARALANNPKVLLCDEATSALDPET---TRSILDLLKDinrelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQ 222

                        250
                 ....*....|
gi 767912304 417 GKHEELLSKP 426
Cdd:COG1135  223 GPVLDVFANP 232
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 196-417 4.63e-50

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: 169.61  E-value: 4.63e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---R 271
Cdd:cd03257    2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 272 SKIGTVSQEPilFSC-----SIAENIA--YGADDPSSVTAEEIQRVAEVANAV----AFIRNFPQGfntvvgekgvlLSG 340
Cdd:cd03257   82 KEIQMVFQDP--MSSlnprmTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVglpeEVLNRYPHE-----------LSG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 341 GQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYG 417
Cdd:cd03257  149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 195-427 1.62e-49

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: 168.68  E-value: 1.62e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKI 274
Cdd:COG1120    1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQEPIL-FSCSIAENIAYG----ADDPSSVTAEEIQRVAEV---ANAVAFI-RNFPQgfntvvgekgvlLSGGQKQR 345
Cdd:COG1120   78 AYVPQEPPApFGLTVRELVALGryphLGLFGRPSAEDREAVEEAlerTGLEHLAdRPVDE------------LSGGERQR 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 346 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEEL 422
Cdd:COG1120  146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225


                 ....*
gi 767912304 423 LSKPN 427
Cdd:COG1120  226 LTPEL 230
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 196-412 1.94e-49

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: 166.88  E-value: 1.94e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPEV--PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlnpvwlrsK 273
Cdd:cd03250    1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGTVSQEPILFSCSIAENIAYGADdpssvtaEEIQRVAEVANAVAF---IRNFPQGFNTVVGEKGVLLSGGQKQRIAIAR 350
Cdd:cd03250   68 IAYVSQEPWIQNGTIRENILFGKP-------FDEERYEKVIKACALepdLEILPDGDLTEIGEKGINLSGGQKQRISLAR 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912304 351 ALLKNPKILLLDEATSALDAE-NEYLVQEAL-DRLMDGRTVLVIAHRLSTIKNANMVAVLDQGK 412
Cdd:cd03250  141 AVYSDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 197-412 2.83e-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: 159.72  E-value: 2.83e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 197 EFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGT 276
Cdd:cd00267    1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 277 VSQepilfscsiaeniaygaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIARALLKNP 356
Cdd:cd00267   78 VPQ----------------------------------------------------------LSGGQRQRVALARALLLNP 99

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304 357 KILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNA-NMVAVLDQGK 412
Cdd:cd00267  100 DLLLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
196-425 4.01e-47

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 162.16  E-value: 4.01e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 275
Cdd:COG1131    1 IEVRGLTKRYGDKTAL---DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILF-SCSIAENIAYGAD---DPSSVTAEEIQRVAEVANAVAFIrnfpqgfNTVVGEkgvlLSGGQKQRIAIARA 351
Cdd:COG1131   77 YVPQEPALYpDLTVRENLRFFARlygLPRKEARERIDELLELFGLTDAA-------DRKVGT----LSGGMKQRLGLALA 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 352 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSK 425
Cdd:COG1131  146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 195-435 4.47e-47

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: 162.28  E-value: 4.47e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARPE-VPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSK 273
Cdd:COG1124    1 MLEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGTVSQEPilfscsiaeniaYGADDPSSvTAEEI--------------QRVAEVANAV----AFIRNFP-Qgfntvvgek 334
Cdd:COG1124   81 VQMVFQDP------------YASLHPRH-TVDRIlaeplrihglpdreERIAELLEQVglppSFLDRYPhQ--------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 335 gvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneyLVQ-EALDRLMD-----GRTVLVIAHRLSTIknANM---V 405
Cdd:COG1124  139 ---LSGGQRQRVAIARALILEPELLLLDEPTSALDV----SVQaEILNLLKDlreerGLTYLFVSHDLAVV--AHLcdrV 209

                        250       260       270
                 ....*....|....*....|....*....|.
gi 767912304 406 AVLDQGKITEYGKHEELLSKPNGIY-RKLMN 435
Cdd:COG1124  210 AVMQNGRIVEELTVADLLAGPKHPYtRELLA 240
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 196-417 1.41e-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: 158.63  E-value: 1.41e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSKIG 275
Cdd:cd03247    1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILFSCSIAENIaygaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekGVLLSGGQKQRIAIARALLKN 355
Cdd:cd03247   79 VLNQRPYLFDTTLRNNL------------------------------------------GRRFSGGERQRLALARILLQD 116

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912304 356 PKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYG 417
Cdd:cd03247  117 APIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 195-426 1.91e-46

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 167.77  E-value: 1.91e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA---SGTISLDGHDIRQLNPVWLR 271
Cdd:COG1123    4 LLEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 272 SKIGTVSQEPI--LFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQgfntvvgekgvLLSGGQKQRI 346
Cdd:COG1123   83 RRIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVgleRRLDRYPH-----------QLSGGQRQRV 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 347 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELL 423
Cdd:COG1123  152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEIL 231


                 ...
gi 767912304 424 SKP 426
Cdd:COG1123  232 AAP 234
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
195-415 2.45e-46

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 159.44  E-value: 2.45e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPA-RPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP----VW 269
Cdd:COG1136    4 LLELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErelaRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 270 LRSKIGTVSQEPILFSC-SIAENIAYGADdPSSVTAEEI-QRVAEVANAV---AFIRNFPqgfntvvGEkgvlLSGGQKQ 344
Cdd:COG1136   84 RRRHIGFVFQFFNLLPElTALENVALPLL-LAGVSRKERrERARELLERVglgDRLDHRP-------SQ----LSGGQQQ 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912304 345 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKITE 415
Cdd:COG1136  152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 195-426 2.81e-46

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 160.59  E-value: 2.81e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD--P---ASGTISLDGHDI--RQLNP 267
Cdd:COG1117   11 KIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 268 VWLRSKIGTVSQEPILFSCSIAENIAYGA---DDPSSVTAEEI-----QRVA---EVANavafirnfpqgfntVVGEKGV 336
Cdd:COG1117   88 VELRRRVGMVFQKPNPFPKSIYDNVAYGLrlhGIKSKSELDEIveeslRKAAlwdEVKD--------------RLKKSAL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 337 LLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAH------RLStiknaNMVAVLDQ 410
Cdd:COG1117  154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYL 228

                        250
                 ....*....|....*.
gi 767912304 411 GKITEYGKHEELLSKP 426
Cdd:COG1117  229 GELVEFGPTEQIFTNP 244
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 194-417 4.42e-46

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: 158.34  E-value: 4.42e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 194 GALEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS 272
Cdd:cd03369    5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 273 KIGTVSQEPILFSCSIAENIaygadDP-SSVTAEEIQRVAEVAnavafirnfpqgfntvvgEKGVLLSGGQKQRIAIARA 351
Cdd:cd03369   83 SLTIIPQDPTLFSGTIRSNL-----DPfDEYSDEEIYGALRVS------------------EGGLNLSQGQRQLLCLARA 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 352 LLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYG 417
Cdd:cd03369  140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 197-412 4.71e-46

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


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 158.40  E-value: 4.71e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 197 EFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGT 276
Cdd:cd03225    1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 277 VSQEP--ILFSCSIAENIAYGAdDPSSVTAEEI-QRVAEVANAvafirnfpqgfntvVGEKGVL------LSGGQKQRIA 347
Cdd:cd03225   80 VFQNPddQFFGPTVEEEVAFGL-ENLGLPEEEIeERVEEALEL--------------VGLEGLRdrspftLSGGQKQRVA 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304 348 IARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGK 412
Cdd:cd03225  145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 196-426 6.31e-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: 159.00  E-value: 6.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPevPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 275
Cdd:cd03295    1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILFS-CSIAENIAYgadDPSSVTAEEIQRVAEVANAVAFIRNFPQGF-NTVVGEkgvlLSGGQKQRIAIARALL 353
Cdd:cd03295   79 YVIQQIGLFPhMTVEENIAL---VPKLLKWPKEKIRERADELLALVGLDPAEFaDRYPHE----LSGGQQQRVGVARALA 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 354 KNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRL-STIKNANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:cd03295  152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 196-426 7.03e-46

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 158.62  E-value: 7.03e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI----RQLNPvwLR 271
Cdd:COG1126    2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdskKDINK--LR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 272 SKIGTVSQEPILFS-CSIAENIAYGaddPSSV------TAEEI-----QRV--AEVANAvafirnFP-Qgfntvvgekgv 336
Cdd:COG1126   77 RKVGMVFQQFNLFPhLTVLENVTLA---PIKVkkmskaEAEERamellERVglADKADA------YPaQ----------- 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 337 lLSGGQKQRIAIARALLKNPKILLLDEATSALDAEneyLVQEALDrLM-----DGRTVLVIAHRLSTIKN-ANMVAVLDQ 410
Cdd:COG1126  137 -LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLD-VMrdlakEGMTMVVVTHEMGFAREvADRVVFMDG 211

                        250
                 ....*....|....*.
gi 767912304 411 GKITEYGKHEELLSKP 426
Cdd:COG1126  212 GRIVEEGPPEEFFENP 227
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 196-425 1.66e-45

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: 158.10  E-value: 1.66e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 275
Cdd:COG4555    2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILFS-CSIAENIAYGA---DDPSSVTAEEIQRVAEVANAVAFIrnfpqgfNTVVGEkgvlLSGGQKQRIAIARA 351
Cdd:COG4555   78 VLPDERGLYDrLTVRENIRYFAelyGLFDEELKKRIEELIELLGLEEFL-------DRRVGE----LSTGMKKKVALARA 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 352 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSK 425
Cdd:COG4555  147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREE 222
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 195-427 2.37e-45

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: 157.45  E-value: 2.37e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP---VWLR 271
Cdd:COG1127    5 MIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 272 SKIGTVSQEPILF-SCSIAENIAYGADDPSSVTAEEI-QRVAEVANAV---AFIRNFPqgfntvvGEkgvlLSGGQKQRI 346
Cdd:COG1127   82 RRIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIrELVLEKLELVglpGAADKMP-------SE----LSGGMRKRV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 347 AIARALLKNPKILLLDEATSALD----AENEYLVQEALDRLmdGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEE 421
Cdd:COG1127  151 ALARALALDPEILLYDEPTAGLDpitsAVIDELIRELRDEL--GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228


                 ....*.
gi 767912304 422 LLSKPN 427
Cdd:COG1127  229 LLASDD 234
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 214-366 2.86e-45

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: 154.34  E-value: 2.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  214 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFS-CSIAENI 292
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912304  293 AYGADDPSSVTAEEIQRVAEVANAVAfIRNFPqgfNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATS 366
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLG-LGDLA---DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 18-430 4.22e-45

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 168.59  E-value: 4.22e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304    18 LATFVLSVV-PPVSIIAVIYGRYL----RKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLA 92
Cdd:TIGR00957 1102 LATPIAAVIiPPLGLLYFFVQRFYvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAY 1181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304    93 RKEAFARAGFFGATGLSGNLIVL-SVLYKgglLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWE 171
Cdd:TIGR00957 1182 YPSIVANRWLAVRLECVGNCIVLfAALFA---VISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKE 1258

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   172 LLEREPKLPF--NEGVILNEKSFQGALEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLY 248
Cdd:TIGR00957 1259 YSETEKEAPWqiQETAPPSGWPPRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRIN 1336

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   249 DPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIaygadDP-SSVTAEEIQRVAEVANAVAFIRNFPQGF 327
Cdd:TIGR00957 1337 ESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL-----DPfSQYSDEEVWWALELAHLKTFVSALPDKL 1411

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   328 NTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAV 407
Cdd:TIGR00957 1412 DHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIV 1491

                          410       420
                   ....*....|....*....|...
gi 767912304   408 LDQGKITEYGKHEELLSKpNGIY 430
Cdd:TIGR00957 1492 LDKGEVAEFGAPSNLLQQ-RGIF 1513
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 196-394 4.82e-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: 4.82e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYP-ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwlrsKI 274
Cdd:cd03293    1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIAIAR 350
Cdd:cd03293   76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEELLELVglsGFENAYPHQ-----------LSGGMRQRVALAR 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767912304 351 ALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAH 394
Cdd:cd03293  145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWreTGKTVLLVTH 190
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 196-412 1.01e-44

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: 153.88  E-value: 1.01e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLN--PVWLRSK 273
Cdd:cd03229    1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGTVSQEPILFS-CSIAENIAYGaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIARAL 352
Cdd:cd03229   78 IGMVFQDFALFPhLTVLENIALG------------------------------------------LSGGQQQRVALARAL 115

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912304 353 LKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGK 412
Cdd:cd03229  116 AMDPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 196-417 2.45e-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: 153.83  E-value: 2.45e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRsKIG 275
Cdd:cd03259    1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV-PPERR-NIG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILF-SCSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIAIARA 351
Cdd:cd03259   76 MVFQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLELVgleGLLNRYPHE-----------LSGGQQQRVALARA 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912304 352 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYG 417
Cdd:cd03259  145 LAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 195-394 3.95e-44

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 154.86  E-value: 3.95e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwlrsK 273
Cdd:COG1116    7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-----D 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFP-QgfntvvgekgvlLSGGQKQRIAI 348
Cdd:COG1116   82 RGVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELLELVglaGFEDAYPhQ------------LSGGMRQRVAI 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767912304 349 ARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAH 394
Cdd:COG1116  150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTH 197
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 195-427 4.23e-44

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 154.48  E-value: 4.23e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnpvwlRSKI 274
Cdd:COG1121    6 AIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQepilfscsiaeNIAYGADDPSSV------------------TAEEIQRVAEVANAV---AFIrnfpqgfNTVVGE 333
Cdd:COG1121   78 GYVPQ-----------RAEVDWDFPITVrdvvlmgrygrrglfrrpSRADREAVDEALERVgleDLA-------DRPIGE 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 334 kgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTI-KNANMVAVLDQG 411
Cdd:COG1121  140 ----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVrEYFDRVLLLNRG 215

                        250
                 ....*....|....*.
gi 767912304 412 KITeYGKHEELLSKPN 427
Cdd:COG1121  216 LVA-HGPPEEVLTPEN 230
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 12-169 1.40e-43

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: 154.18  E-value: 1.40e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18576  132 FFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKL 211

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 169
Cdd:cd18576  212 ALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 196-427 1.61e-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: 152.66  E-value: 1.61e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---RS 272
Cdd:cd03261    1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 273 KIGTVSQEPILF-SCSIAENIAYGADDPSSVTAEEI-QRVAEVANAV---AFIRNFPqgfntvvGEkgvlLSGGQKQRIA 347
Cdd:cd03261   78 RMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIrEIVLEKLEAVglrGAEDLYP-------AE----LSGGMKKRVA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 348 IARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLS 424
Cdd:cd03261  147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226


                 ...
gi 767912304 425 KPN 427
Cdd:cd03261  227 SDD 229
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 196-425 2.12e-43

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: 153.35  E-value: 2.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  196 LEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVW-LRSKI 274
Cdd:TIGR04520   1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  275 GTVSQEP-ILFSCSIAEN-IAYGaddPSS--VTAEEI-QRVAEVANAV---AFIRNFPQgfntvvgekgvLLSGGQKQRI 346
Cdd:TIGR04520  80 GMVFQNPdNQFVGATVEDdVAFG---LENlgVPREEMrKRVDEALKLVgmeDFRDREPH-----------LLSGGQKQRV 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  347 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLS 424
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225


                  .
gi 767912304  425 K 425
Cdd:TIGR04520 226 Q 226
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
196-427 8.15e-43

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 150.68  E-value: 8.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPevpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIG 275
Cdd:COG3840    2 LRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPqgfntvvGEkgvlLSGGQKQRIAIARA 351
Cdd:COG3840   75 MLFQENNLFPhLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVglaGLLDRLP-------GQ----LSGGQRQRVALARC 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 352 LLKNPKILLLDEATSALD----AENEYLVQEALDRLmdGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:COG3840  144 LVRKRPILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221


                 .
gi 767912304 427 N 427
Cdd:COG3840  222 P 222
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 195-427 9.87e-43

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 153.72  E-value: 9.87e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRsKI 274
Cdd:COG3842    5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL-PPEKR-NV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQEPILFS-CSIAENIAYGADDpSSVTAEEI-QRVAEVANAV---AFIRNFPQgfntvvgekgvLLSGGQKQRIAIA 349
Cdd:COG3842   80 GMVFQDYALFPhLTVAENVAFGLRM-RGVPKAEIrARVAELLELVgleGLADRYPH-----------QLSGGQQQRVALA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 350 RALLKNPKILLLDEATSALDAEneyL---VQEALDRLMD--GRTVLVIAHRLS---TIknANMVAVLDQGKITEYGKHEE 421
Cdd:COG3842  148 RALAPEPRVLLLDEPLSALDAK---LreeMREELRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEE 222


                 ....*.
gi 767912304 422 LLSKPN 427
Cdd:COG3842  223 IYERPA 228
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 197-417 1.70e-42

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: 147.97  E-value: 1.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 197 EFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGT 276
Cdd:cd03214    1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 277 VSQepilfscsiaeniaygaddpssvtaeeiqrVAEVANAVAFIRnfpQGFNTvvgekgvlLSGGQKQRIAIARALLKNP 356
Cdd:cd03214   78 VPQ------------------------------ALELLGLAHLAD---RPFNE--------LSGGERQRVLLARALAQEP 116

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912304 357 KILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYG 417
Cdd:cd03214  117 PILLLDEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
196-415 3.14e-42

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 148.66  E-value: 3.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP---VWLRS 272
Cdd:COG2884    2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreiPYLRR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 273 KIGTVSQE-PILFSCSIAENIAY-----GADDpssvtaEEIQ-RVAEVANAV---AFIRNFPQgfntvvgEkgvlLSGGQ 342
Cdd:COG2884   80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSR------KEIRrRVREVLDLVglsDKAKALPH-------E----LSGGE 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912304 343 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTIKNANM-VAVLDQGKITE 415
Cdd:COG2884  143 QQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 196-413 3.66e-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: 148.41  E-value: 3.66e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPE-VPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---- 270
Cdd:cd03255    1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 271 RSKIGTVSQE----PILfscSIAENIAYGADDPSSVTAEEIQRVAEVANAVafirNFPQGFNTVVGEkgvlLSGGQKQRI 346
Cdd:cd03255   81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEELLERV----GLGDRLNHYPSE----LSGGQQQRV 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912304 347 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLSTIKNANMVAVLDQGKI 413
Cdd:cd03255  150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
PLN03130 PLN03130
ABC transporter C family member; Provisional
 194-433 2.39e-41

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 157.21  E-value: 2.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  194 GALEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS 272
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  273 KIGTVSQEPILFSCSIAENIaygadDPSSVTAE-EIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARA 351
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNL-----DPFNEHNDaDLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARA 1388

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  352 LLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYR 431
Cdd:PLN03130 1389 LLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468


                  ..
gi 767912304  432 KL 433
Cdd:PLN03130 1469 KM 1470
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 196-413 1.04e-40

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: 142.92  E-value: 1.04e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 275
Cdd:cd03230    1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILFScsiaeniaygaddpsSVTAEEIqrvaevanavafirnfpqgfntvvgekgVLLSGGQKQRIAIARALLKN 355
Cdd:cd03230   77 YLPEEPSLYE---------------NLTVREN----------------------------LKLSGGMKQRLALAQALLHD 113

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 356 PKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 413
Cdd:cd03230  114 PELLILDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 193-423 1.68e-40

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 145.52  E-value: 1.68e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 193 QGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS 272
Cdd:PRK13632   5 SVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 273 KIGTVSQEP--ILFSCSIAENIAYGADD---PSSVTAEEIQRVAEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIA 347
Cdd:PRK13632  84 KIGIIFQNPdnQFIGATVEDDIAFGLENkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVA 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304 348 IARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELL 423
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
 12-166 8.79e-40

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: 144.22  E-value: 8.79e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18572  132 FSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKL 211

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAG 166
Cdd:cd18572  212 SVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAA 286
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 196-422 1.17e-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: 142.32  E-value: 1.17e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPArpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---RS 272
Cdd:cd03256    1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 273 KIGTVSQEPILFS-CSIAENIAYGADD--------PSSVTAEEIQRVAEVANAV-----AFIRnfpqgfntvVGEkgvlL 338
Cdd:cd03256   79 QIGMIFQQFNLIErLSVLENVLSGRLGrrstwrslFGLFPKEEKQRALAALERVglldkAYQR---------ADQ----L 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 339 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLSTIK-NANMVAVLDQGKITE 415
Cdd:cd03256  146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIVF 225


                 ....*..
gi 767912304 416 YGKHEEL 422
Cdd:cd03256  226 DGPPAEL 232
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 216-427 2.29e-39

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: 141.70  E-value: 2.29e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 216 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIGTVSQEPILF-SCSIAENIAY 294
Cdd:cd03299   17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNIAY 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 295 GADDPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEY 374
Cdd:cd03299   95 GLKKRKVDKKEIERKVLEIAEML--------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 375 LVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPN 427
Cdd:cd03299  167 KLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPK 222
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 195-413 3.93e-39

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 141.35  E-value: 3.93e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---R 271
Cdd:COG3638    2 MLELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 272 SKIGTVSQEPILFS-CSIAENIAYG--ADDP------SSVTAEEIQRVAEVANAV-----AFIRnfpqgfntvVGEkgvl 337
Cdd:COG3638   80 RRIGMIFQQFNLVPrLSVLTNVLAGrlGRTStwrsllGLFPPEDRERALEALERVgladkAYQR---------ADQ---- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 338 LSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-----EYLVQEALDrlmDGRTVLVIAHRLSTIKN-ANMVAVLDQG 411
Cdd:COG3638  147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTarqvmDLLRRIARE---DGITVVVNLHQVDLARRyADRIIGLRDG 223


                 ..
gi 767912304 412 KI 413
Cdd:COG3638  224 RV 225
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 196-426 1.20e-38

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: 142.11  E-value: 1.20e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDP---ASGTISLDGHDIRQLNPVWLR 271
Cdd:COG0444    2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 272 S----KIGTVSQEPilFSC---------SIAENIAYGADdpssVTAEEI-QRVAEVANAV------AFIRNFP-Qgfntv 330
Cdd:COG0444   82 KirgrEIQMIFQDP--MTSlnpvmtvgdQIAEPLRIHGG----LSKAEArERAIELLERVglpdpeRRLDRYPhE----- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 331 vgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneyLVQ-EALDRLMD-----GRTVLVIAHRLSTIKN-AN 403
Cdd:COG0444  151 -------LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNLLKDlqrelGLAILFITHDLGVVAEiAD 219

                        250       260
                 ....*....|....*....|...
gi 767912304 404 MVAVLDQGKITEYGKHEELLSKP 426
Cdd:COG0444  220 RVAVMYAGRIVEEGPVEELFENP 242
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 197-413 1.51e-38

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: 138.44  E-value: 1.51e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 197 EFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnpvwlRSKIGT 276
Cdd:cd03235    1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 277 VSQEPIL---FSCSIAENIAYGADDPSS----VTAEEIQRVAEVANAV---AFI-RNFpqgfntvvGEkgvlLSGGQKQR 345
Cdd:cd03235   73 VPQRRSIdrdFPISVRDVVLMGLYGHKGlfrrLSKADKAKVDEALERVglsELAdRQI--------GE----LSGGQQQR 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 346 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTI-KNANMVAVLDQGKI 413
Cdd:cd03235  141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 197-426 8.88e-38

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 140.32  E-value: 8.88e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 197 EFKNVHFAYP-ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS--- 272
Cdd:PRK11153   3 ELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarr 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 273 KIGTVSQE-PILFSCSIAENIAYgaddP---SSVTAEEI-QRVAEVANAV---AFIRNFP-QgfntvvgekgvlLSGGQK 343
Cdd:PRK11153  83 QIGMIFQHfNLLSSRTVFDNVAL----PlelAGTPKAEIkARVTELLELVglsDKADRYPaQ------------LSGGQK 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 344 QRIAIARALLKNPKILLLDEATSALDAENeylVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYG 417
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPAT---TRSILELLKDinrelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223


                 ....*....
gi 767912304 418 KHEELLSKP 426
Cdd:PRK11153 224 TVSEVFSHP 232
PLN03232 PLN03232
ABC transporter C family member; Provisional
 194-435 1.09e-37

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 146.66  E-value: 1.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  194 GALEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS 272
Cdd:PLN03232 1233 GSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR 1310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  273 KIGTVSQEPILFSCSIAENIaygadDP-SSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARA 351
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFNI-----DPfSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARA 1385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  352 LLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYR 431
Cdd:PLN03232 1386 LLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFF 1465


                  ....
gi 767912304  432 KLMN 435
Cdd:PLN03232 1466 RMVH 1469
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 196-413 1.61e-37

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: 135.74  E-value: 1.61e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI----RQLNPvwLR 271
Cdd:cd03262    1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkKNINE--LR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 272 SKIGTVSQEPILFS-CSIAENIAYGaddPSSV----------TAEEI-QRV--AEVANAvafirnFPQGfntvvgekgvl 337
Cdd:cd03262   76 QKVGMVFQQFNLFPhLTVLENITLA---PIKVkgmskaeaeeRALELlEKVglADKADA------YPAQ----------- 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 338 LSGGQKQRIAIARALLKNPKILLLDEATSALDAEneyLVQEALDRLMD----GRTVLVIAHRLSTIKN-ANMVAVLDQGK 412
Cdd:cd03262  136 LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLDVMKDlaeeGMTMVVVTHEMGFAREvADRVIFMDDGR 212


                 .
gi 767912304 413 I 413
Cdd:cd03262  213 I 213
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 212-434 1.16e-36

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: 1.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 212 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAEN 291
Cdd:cd03288   35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 292 IaygaDDPSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 371
Cdd:cd03288  115 L----DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912304 372 NEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYRKLM 434
Cdd:cd03288  191 TENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 218-426 2.05e-36

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 136.40  E-value: 2.05e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 218 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP---VWLRSKIGTVSQEPilFSC-----SIA 289
Cdd:COG4608   38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGrelRPLRRRMQMVFQDP--YASlnprmTVG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 290 ENIAYGADDPSSVTAEEIQ-RVAEVANAV----AFIRNFPQGFntvvgekgvllSGGQKQRIAIARALLKNPKILLLDEA 364
Cdd:COG4608  116 DIIAEPLRIHGLASKAERReRVAELLELVglrpEHADRYPHEF-----------SGGQRQRIGIARALALNPKLIVCDEP 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912304 365 TSALDAEneylVQ-EALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:COG4608  185 VSALDVS----IQaQVLNLLEDlqdelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYARP 249
cbiO PRK13640
energy-coupling factor transporter ATPase;
195-426 2.33e-36

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 134.93  E-value: 2.33e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL--LRLYDPASGT-ISLDGHDIRQLNpVW-L 270
Cdd:PRK13640   5 IVEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLIngLLLPDDNPNSkITVDGITLTAKT-VWdI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 271 RSKIGTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVA---FIRNFPQGfntvvgekgvlLSGGQKQR 345
Cdd:PRK13640  83 REKVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGmldYIDSEPAN-----------LSGGQKQR 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 346 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELL 423
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF 231


                 ...
gi 767912304 424 SKP 426
Cdd:PRK13640 232 SKV 234
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 199-414 4.16e-36

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: 132.00  E-value: 4.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 199 KNVHFAYPARPEvpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdiRQLNPVWLRSKIGTVS 278
Cdd:cd03226    3 ENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVM 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 279 QEP--ILFSCSIAENIAYGADDPSSVtAEEIQRVAEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNP 356
Cdd:cd03226   78 QDVdyQLFTDSVREELLLGLKELDAG-NEQAETVLKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLSGK 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 357 KILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQGKIT 414
Cdd:cd03226  146 DLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 215-426 5.67e-36

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: 133.54  E-value: 5.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 215 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL----RSKIGTVSQEPILF-SCSIA 289
Cdd:cd03294   41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 290 ENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPqgfntvvGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATS 366
Cdd:cd03294  121 ENVAFGLEVQGVPRAEREERAAEALELVgleGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEAFS 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912304 367 ALDAENEYLVQEALDRLMD--GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:cd03294  190 ALDPLIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 196-426 7.06e-36

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 135.27  E-value: 7.06e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIrqlnPVWL---RS 272
Cdd:COG1118    3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL----FTNLpprER 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 273 KIGTVSQEPILF-SCSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFP-QgfntvvgekgvlLSGGQKQRIA 347
Cdd:COG1118   76 RVGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARVEELLELVqleGLADRYPsQ------------LSGGQRQRVA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 348 IARALLKNPKILLLDEATSALDA----ENEYLVQEALDRLmdGRTVLVIAH------RLstiknANMVAVLDQGKITEYG 417
Cdd:COG1118  144 LARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDEL--GGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVG 216


                 ....*....
gi 767912304 418 KHEELLSKP 426
Cdd:COG1118  217 TPDEVYDRP 225
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 196-417 6.74e-35

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: 128.85  E-value: 6.74e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPevpIFQDFSLSIPSGsVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 275
Cdd:cd03264    1 LQLENLTKRYGKKR---ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILF-SCSIAENIAYGA---DDPSSvtaEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARA 351
Cdd:cd03264   76 YLPQEFGVYpNFTVREFLDYIAwlkGIPSK---EVKARVDEVLELV--------NLGDRAKKKIGSLSGGMRRRVGIAQA 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304 352 LLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYG 417
Cdd:cd03264  145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
 12-168 7.44e-35

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: 131.13  E-value: 7.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18574  138 YLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKL 217

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGR 168
Cdd:cd18574  218 NEKLGLGIGIFQGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGAR 294
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 194-427 8.02e-35

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 132.50  E-value: 8.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 194 GALEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSK 273
Cdd:COG3839    2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGTVSQEPILF-SCSIAENIAYG---ADdpssVTAEEI-QRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQR 345
Cdd:COG3839   77 IAMVFQSYALYpHMTVYENIAFPlklRK----VPKAEIdRRVREAAELLgleDLLDRKPKQ-----------LSGGQRQR 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 346 IAIARALLKNPKILLLDEATSALDAEneyLVQEA---LDRLMDGR---TVLV---------IAHRlstiknanmVAVLDQ 410
Cdd:COG3839  142 VALGRALVREPKVFLLDEPLSNLDAK---LRVEMraeIKRLHRRLgttTIYVthdqveamtLADR---------IAVMND 209

                        250
                 ....*....|....*..
gi 767912304 411 GKITEYGKHEELLSKPN 427
Cdd:COG3839  210 GRIQQVGTPEELYDRPA 226
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
196-424 1.54e-34

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 129.75  E-value: 1.54e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdiRQLNP--VW-LRS 272
Cdd:PRK13635   6 IRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEetVWdVRR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 273 KIGTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIA 347
Cdd:PRK13635  82 QVGMVFQNPdnQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVgmeDFLNREPHR-----------LSGGQKQRVA 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912304 348 IARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLS 424
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 196-427 3.55e-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: 127.35  E-value: 3.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIG 275
Cdd:cd03300    1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIAIARA 351
Cdd:cd03300   76 TVFQNYALFPhLTVFENIAFGLRLKKLPKAEIKERVAEALDLVqleGYANRKPSQ-----------LSGGQQQRVAIARA 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912304 352 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKPN 427
Cdd:cd03300  145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
 7-169 9.24e-34

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: 128.20  E-value: 9.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   7 SCKLQFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVD 86
Cdd:cd18784  127 VIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLK 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  87 HVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAG 166
Cdd:cd18784  207 DTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAA 286


                 ...
gi 767912304 167 GRL 169
Cdd:cd18784  287 EKV 289
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 196-413 1.42e-33

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


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 125.21  E-value: 1.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLN----PvWLR 271
Cdd:cd03292    1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraiP-YLR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 272 SKIGTVSQE-PILFSCSIAENIAYgADDPSSVTAEEIQ-RVAEVANAVAF---IRNFPQGfntvvgekgvlLSGGQKQRI 346
Cdd:cd03292   78 RKIGVVFQDfRLLPDRNVYENVAF-ALEVTGVPPREIRkRVPAALELVGLshkHRALPAE-----------LSGGEQQRV 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912304 347 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 413
Cdd:cd03292  146 AIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTtRHRVIALERGKL 214
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 196-434 1.43e-33

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: 132.12  E-value: 1.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPAR--------PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLyDPASGTISLDGHDI----- 262
Cdd:COG4172  276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLdglsr 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 263 RQLNPvwLRSKIGTVSQEPilFSC-----SIAENIAYG--ADDPSSVTAEEIQRVAEVANAV----AFIRNFPQGFntvv 331
Cdd:COG4172  355 RALRP--LRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrVHGPGLSAAERRARVAEALEEVgldpAARHRYPHEF---- 426

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 332 gekgvllSGGQKQRIAIARALLKNPKILLLDEATSALDAeneyLVQ-EALDRLMD-----GRTVLVIAHRLSTIKN-ANM 404
Cdd:COG4172  427 -------SGGQRQRIAIARALILEPKLLVLDEPTSALDV----SVQaQILDLLRDlqrehGLAYLFISHDLAVVRAlAHR 495

                        250       260       270
                 ....*....|....*....|....*....|.
gi 767912304 405 VAVLDQGKITEYGKHEELLSKPNGIY-RKLM 434
Cdd:COG4172  496 VMVMKDGKVVEQGPTEQVFDAPQHPYtRALL 526
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 195-427 1.64e-33

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 125.91  E-value: 1.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwLRSKI 274
Cdd:cd03296    2 SIEVRNVSKRFGDFVAL---DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV--QERNV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQEPILFS-CSIAENIAYG------ADDPSSvtAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQ 344
Cdd:cd03296   77 GFVFQHYALFRhMTVFDNVAFGlrvkprSERPPE--AEIRAKVHELLKLVqldWLADRYPAQ-----------LSGGQRQ 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 345 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDG---RTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEE 421
Cdd:cd03296  144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223


                 ....*.
gi 767912304 422 LLSKPN 427
Cdd:cd03296  224 VYDHPA 229
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 195-427 3.43e-33

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: 125.20  E-value: 3.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASG-TISLDGHDIRQLNPVWLRSK 273
Cdd:COG1119    3 LLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGTVS---QEPILFSCSIAENIAYGADD----PSSVTAEEIQRVAEVANAVAFI----RNFPQgfntvvgekgvlLSGGQ 342
Cdd:COG1119   80 IGLVSpalQLRFPRDETVLDVVLSGFFDsiglYREPTDEQRERARELLELLGLAhladRPFGT------------LSQGE 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 343 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNA-NMVAVLDQGKITEYGKH 419
Cdd:COG1119  148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPK 227


                 ....*...
gi 767912304 420 EELLSKPN 427
Cdd:COG1119  228 EEVLTSEN 235
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
196-426 9.68e-33

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 124.05  E-value: 9.68e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNV--HFAyparpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIR--QLNPVWLR 271
Cdd:PRK09493   2 IEFKNVskHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 272 SKIGTVSQEPILFSCSIA-ENIAYGaddP------SSVTAEEIQR-------VAEVANavafirNFPqgfntvvGEkgvl 337
Cdd:PRK09493  77 QEAGMVFQQFYLFPHLTAlENVMFG---PlrvrgaSKEEAEKQARellakvgLAERAH------HYP-------SE---- 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 338 LSGGQKQRIAIARALLKNPKILLLDEATSALDAEneyLVQEALdRLM-----DGRTVLVIAHRLS-TIKNANMVAVLDQG 411
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE---LRHEVL-KVMqdlaeEGMTMVIVTHEIGfAEKVASRLIFIDKG 212

                        250
                 ....*....|....*
gi 767912304 412 KITEYGKHEELLSKP 426
Cdd:PRK09493 213 RIAEDGDPQVLIKNP 227
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 216-426 1.59e-32

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: 126.37  E-value: 1.59e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 216 DFSLSIPSGSVTALVGPSGSGKSTVLSL---LLRlydPASGTISLDGH-----DIRQLNPVWLRSkIGTVSQEPILFS-C 286
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqdsARGIFLPPHRRR-IGYVFQEARLFPhL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 287 SIAENIAYGADD-PSSVTAEEIQRVAEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEAT 365
Cdd:COG4148   93 SVRGNLLYGRKRaPRAERRISFDEVVELLGIGHLLDRRPAT-----------LSGGERQRVAIGRALLSSPRLLLMDEPL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912304 366 SALDAENEYLVQEALDRLMD--GRTVLVIAH------RLstiknANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:COG4148  162 AALDLARKAEILPYLERLRDelDIPILYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSRP 225
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 196-424 1.63e-32

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


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 122.54  E-value: 1.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP-VWLRSKI 274
Cdd:cd03224    1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQEPILF-SCSIAENIAYGADD-PSSVTAEEIQRVAEVanavafirnFPqgfntVVGE----KGVLLSGGQKQRIAI 348
Cdd:cd03224   78 GYVPEGRRIFpELTVEENLLLGAYArRRAKRKARLERVYEL---------FP-----RLKErrkqLAGTLSGGEQQMLAI 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 349 ARALLKNPKILLLDEATSALdAENeyLVQEALDRLMD----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELL 423
Cdd:cd03224  144 ARALMSRPKLLLLDEPSEGL-APK--IVEEIFEAIRElrdeGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220


                 .
gi 767912304 424 S 424
Cdd:cd03224  221 A 221
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 12-169 4.32e-32

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: 123.36  E-value: 4.32e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18575  132 FITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAA 211

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 169
Cdd:cd18575  212 ALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
189-430 7.67e-32

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 124.95  E-value: 7.67e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 189 EKSFQGALEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPv 268
Cdd:PRK11607  13 RKALTPLLEIRNLTKSFDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 269 wLRSKIGTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFirnfpQGFntvVGEKGVLLSGGQKQRIA 347
Cdd:PRK11607  89 -YQRPINMMFQSYALFPhMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM-----QEF---AKRKPHQLSGGQRQRVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 348 IARALLKNPKILLLDEATSALDAE----NEYLVQEALDRLmdGRTVLVIAH-RLSTIKNANMVAVLDQGKITEYGKHEEL 422
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237


                 ....*...
gi 767912304 423 LSKPNGIY 430
Cdd:PRK11607 238 YEHPTTRY 245
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 196-394 8.53e-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: 120.28  E-value: 8.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAypaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 275
Cdd:COG4133    3 LEAENLSCR---RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILF-SCSIAENIAYGAD-DPSSVTAEEIQRVAEVANAVAFIRNFPQgfntvvgekgvLLSGGQKQRIAIARALL 353
Cdd:COG4133   79 YLGHADGLKpELTVRENLRFWAAlYGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLL 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767912304 354 KNPKILLLDEATSALDAENEYLVQEALDR-LMDGRTVLVIAH 394
Cdd:COG4133  148 SPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 216-417 9.72e-32

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: 120.29  E-value: 9.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 216 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIGTVSQEPILFS-CSIAENIAY 294
Cdd:cd03298   16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 295 GADDPSSVTAEEIQRVAEVANAVAFirnfpQGFNTVVGEKgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAEney 374
Cdd:cd03298   94 GLSPGLKLTAEDRQAIEVALARVGL-----AGLEKRLPGE---LSGGERQRVALARVLVRDKPVLLLDEPFAALDPA--- 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767912304 375 LVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYG 417
Cdd:cd03298  163 LRAEMLDLVLDlhaetKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 196-426 2.17e-31

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: 120.09  E-value: 2.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRSK-- 273
Cdd:COG0410    4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL-PPHRIARlg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGTVSQEPILF-SCSIAENI---AYGADDPSSVtAEEIQRVAEVanavafirnFPqgfntVVGE----KGVLLSGGQKQR 345
Cdd:COG0410   80 IGYVPEGRRIFpSLTVEENLllgAYARRDRAEV-RADLERVYEL---------FP-----RLKErrrqRAGTLSGGEQQM 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 346 IAIARALLKNPKILLLDEATSALdAENeyLVQE---ALDRLMD-GRTVLV----------IAHRlstiknanmVAVLDQG 411
Cdd:COG0410  145 LAIGRALMSRPKLLLLDEPSLGL-APL--IVEEifeIIRRLNReGVTILLveqnarfaleIADR---------AYVLERG 212

                        250
                 ....*....|....*
gi 767912304 412 KITEYGKHEELLSKP 426
Cdd:COG0410  213 RIVLEGTAAELLADP 227
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 216-427 3.71e-31

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: 122.53  E-value: 3.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  216 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDG---HDIRQ---LNPVwlRSKIGTVSQEPILFS-CSI 288
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgifLPPE--KRRIGYVFQEARLFPhLSV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  289 AENIAYG---ADDPSSVTAEEiqRVAEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEAT 365
Cdd:TIGR02142  93 RGNLRYGmkrARPSERRISFE--RVIELLGIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912304  366 SALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPN 427
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPD 224
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 195-427 5.97e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 119.84  E-value: 5.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKI 274
Cdd:PRK13647   4 IIEVEDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIAIA 349
Cdd:PRK13647  82 GLVFQDPddQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVrmwDFRDKPPYH-----------LSYGQKKRVAIA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 350 RALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKhEELLSKPN 427
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLTDED 229
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 195-427 7.15e-31

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 119.49  E-value: 7.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvWLRSKI 274
Cdd:PRK13548   2 MLEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP-AELARR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 -GTVSQEPIL-FSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFI----RNFPQgfntvvgekgvlLSGGQKQRIAI 348
Cdd:PRK13548  78 rAVLPQHSSLsFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAhlagRDYPQ------------LSGGEQQRVQL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 349 ARALL------KNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLstikN-----ANMVAVLDQGKITE 415
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHerGLAVIVVLHDL----NlaaryADRIVLLHQGRLVA 221

                        250
                 ....*....|..
gi 767912304 416 YGKHEELLSKPN 427
Cdd:PRK13548 222 DGTPAEVLTPET 233
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 195-425 1.26e-30

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: 125.44  E-value: 1.26e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   195 ALEFKNVHFAYpARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDpasgtiSLDGHdirqlnpVWLRSKI 274
Cdd:TIGR00957  636 SITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD------KVEGH-------VHMKGSV 701

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   275 GTVSQEPILFSCSIAENIAYGaddpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLK 354
Cdd:TIGR00957  702 AYVPQQAWIQNDSLRENILFG----KALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYS 777

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912304   355 NPKILLLDEATSALDAE-NEYLVQEAL--DRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSK 425
Cdd:TIGR00957  778 NADIYLFDDPLSAVDAHvGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 196-429 1.73e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 118.70  E-value: 1.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPArPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 275
Cdd:PRK13648   8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPI-LFSCSIAE-NIAYGADDpSSVTAEEIQR-VAEVANAVAFI--RNF-PQGfntvvgekgvlLSGGQKQRIAIA 349
Cdd:PRK13648  87 IVFQNPDnQFVGSIVKyDVAFGLEN-HAVPYDEMHRrVSEALKQVDMLerADYePNA-----------LSGGQKQRVAIA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 350 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPN 427
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234


                 ..
gi 767912304 428 GI 429
Cdd:PRK13648 235 EL 236
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 218-426 2.01e-30

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 117.95  E-value: 2.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 218 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD-----PASGTISLDGHDI--RQLNPVWLRSKIGTVSQEPILFSCSIAE 290
Cdd:PRK14239  25 SLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPMSIYE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 291 NIAYGADDPSSVTAEEIQRVAEVANAVAFIrnfpqgFNTV---VGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSA 367
Cdd:PRK14239 105 NVVYGLRLKGIKDKQVLDEAVEKSLKGASI------WDEVkdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912304 368 LDAENEYLVQEALDRLMDGRTVLVIAHRL---STIknANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNDTKQMFMNP 238
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 213-426 2.18e-30

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 118.23  E-value: 2.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 213 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH------DIRQLNPVWLRSKIGTVSQEPILFS- 285
Cdd:PRK14246  25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 286 CSIAENIAYGADDPSSVTAEEIQRVAEVA-NAVAFIRNFPQGFNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEA 364
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEEClRKVGLWKEVYDRLNSPASQ----LSGGQQQRLTIARALALKPKVLLMDEP 180

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912304 365 TSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTSP 243
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 196-408 2.80e-30

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 116.74  E-value: 2.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 275
Cdd:PRK10247   8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILFSCSIAENIAYgaddPSSVTAEEIQRVAEVANAVAFirNFPQgfNTVvgEKGV-LLSGGQKQRIAIARALLK 354
Cdd:PRK10247  85 YCAQTPTLFGDTVYDNLIF----PWQIRNQQPDPAIFLDDLERF--ALPD--TIL--TKNIaELSGGEKQRISLIRNLQF 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 355 NPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTIKNANMVAVL 408
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVITL 210
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 207-371 3.11e-30

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 116.04  E-value: 3.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 207 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDP---ASGTISLDGHDIRQLNPvwLRSKIGTVSQEPIL 283
Cdd:COG4136   10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA--EQRRIGILFQDDLL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 284 FS-CSIAENIAYGAddPSSVTAEeiQRVAEVANAVA------FIRNFPqgfNTvvgekgvlLSGGQKQRIAIARALLKNP 356
Cdd:COG4136   88 FPhLSVGENLAFAL--PPTIGRA--QRRARVEQALEeaglagFADRDP---AT--------LSGGQRARVALLRALLAEP 152

                        170
                 ....*....|....*
gi 767912304 357 KILLLDEATSALDAE 371
Cdd:COG4136  153 RALLLDEPFSKLDAA 167
cbiO PRK13650
energy-coupling factor transporter ATPase;
196-427 3.67e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 117.91  E-value: 3.67e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNpVW-LRSKI 274
Cdd:PRK13650   5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN-VWdIRHKI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFirnfpQGFNTvvgEKGVLLSGGQKQRIAIARAL 352
Cdd:PRK13650  84 GMVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGM-----QDFKE---REPARLSGGQKQRVAIAGAV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304 353 LKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPN 427
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 210-426 4.80e-30

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 116.94  E-value: 4.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 210 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRL---YDPA--SGTISLDGHDIRQLNPVWLRSKIGTVSQEP-IL 283
Cdd:PRK14247  15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielYPEArvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 284 FSCSIAENIAYGADDPSSVT--AEEIQRVAEVANAVAFIRNFPQGFNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLL 361
Cdd:PRK14247  95 PNLSIFENVALGLKLNRLVKskKELQERVRWALEKAQLWDEVKDRLDAPAGK----LSGGQQQRLCIARALAFQPEVLLA 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912304 362 DEATSALDAENEYLVQEALDRLMDGRTVLVIAH------RLStiknaNMVAVLDQGKITEYGKHEELLSKP 426
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGPTREVFTNP 236
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 215-426 9.84e-30

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 116.42  E-value: 9.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 215 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD-----PASGTISLDGHDI--RQLNPVWLRSKIGTVSQEPILFSCS 287
Cdd:PRK14243  27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 288 IAENIAYGAD------DPSSVTAEEIQRVA---EVANAVAfirnfpqgfntvvgEKGVLLSGGQKQRIAIARALLKNPKI 358
Cdd:PRK14243 107 IYDNIAYGARingykgDMDELVERSLRQAAlwdEVKDKLK--------------QSGLSLSGGQQQRLCIARAIAVQPEV 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304 359 LLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRL-STIKNANMVAVLD---------QGKITEYGKHEELLSKP 426
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMqQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSP 250
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 215-413 1.38e-29

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: 115.23  E-value: 1.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 215 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSKIGTVS--QEPILF-SCSIAEN 291
Cdd:cd03219   17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELTVLEN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 292 IAYGA-------DDPSSVTAEEIQRVAEVANAVAFIRNFPQGfNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEA 364
Cdd:cd03219   96 VMVAAqartgsgLLLARARREEREARERAEELLERVGLADLA-DRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767912304 365 TSALDAEneyLVQEALDRLMD----GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 413
Cdd:cd03219  171 AAGLNPE---ETEELAELIRElrerGITVLLVEHDMDVVMSlADRVTVLDQGRV 221
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
216-430 2.51e-29

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 117.51  E-value: 2.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 216 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlnpvwlRS----KIGTVSQEPILFS-CSIAE 290
Cdd:PRK11432  24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSiqqrDICMVFQSYALFPhMSLGE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 291 NIAYGAdDPSSVTAEEI-QRVAEVANAVAFIrnfpqGFntvvGEKGV-LLSGGQKQRIAIARALLKNPKILLLDEATSAL 368
Cdd:PRK11432  98 NVGYGL-KMLGVPKEERkQRVKEALELVDLA-----GF----EDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNL 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912304 369 DAENEYLVQEALDRLMD--GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKPNGIY 430
Cdd:PRK11432 168 DANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 216-417 2.61e-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: 113.93  E-value: 2.61e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 216 DFSLSIP---SGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDG---HDIRQ---LNPVwlRSKIGTVSQEPILFS- 285
Cdd:cd03297   12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKkinLPPQ--QRKIGLVFQQYALFPh 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 286 CSIAENIAYGADDPSSvtAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEAT 365
Cdd:cd03297   90 LNVRENLAFGLKRKRN--REDRISVDELLDLL--------GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767912304 366 SALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYG 417
Cdd:cd03297  160 SALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 196-417 2.96e-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: 2.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIG 275
Cdd:cd03301    1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILF-SCSIAENIAYG---ADDPSSVTAEEIQRVAEVAnavafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARA 351
Cdd:cd03301   76 MVFQNYALYpHMTVYDNIAFGlklRKVPKDEIDERVREVAELL-----------QIEHLLDRKPKQLSGGQRQRVALGRA 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912304 352 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAH-RLSTIKNANMVAVLDQGKITEYG 417
Cdd:cd03301  145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 168-395 4.28e-29

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 119.53  E-value: 4.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 168 RLWEL---LEREPKLPFNEGVIlnEKSFQGALEFKNVHFAYPArpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTvlslL 244
Cdd:COG4178  334 RLAGFeeaLEAADALPEAASRI--ETSEDGALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSGSGKST----L 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 245 LR----LYDPASGTISL-DGHDIrqlnpVWLrskigtvSQEPILFSCSIAENIAYgADDPSSVTAEEIQRV------AEV 313
Cdd:COG4178  406 LRaiagLWPYGSGRIARpAGARV-----LFL-------PQRPYLPLGTLREALLY-PATAEAFSDAELREAleavglGHL 472

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 314 ANAVAFIRNFPQgfntvvgekgvLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIA 393
Cdd:COG4178  473 AERLDEEADWDQ-----------VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVG 541


                 ..
gi 767912304 394 HR 395
Cdd:COG4178  542 HR 543
PLN03232 PLN03232
ABC transporter C family member; Provisional
 11-434 4.94e-29

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 120.85  E-value: 4.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   11 QFFVSPNLATFVLSVVPPVSIIAViygRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQ 90
Cdd:PLN03232  438 QLGVASLFGSLILFLLIPLQTLIV---RKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELS 514

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   91 LARKEAFARAgfFGATGLSGNLIVLSVLYKGG-LLMGSAHMTVGELSSFLMYAFwVGISIGGLSSFYSELMKGLGAGGRL 169
Cdd:PLN03232  515 WFRKAQLLSA--FNSFILNSIPVVVTLVSFGVfVLLGGDLTPARAFTSLSLFAV-LRSPLNMLPNLLSQVVNANVSLQRI 591

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  170 WELLEREPKL-----PFNEGVilneksfqGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL 244
Cdd:PLN03232  592 EELLLSEERIlaqnpPLQPGA--------PAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM 663

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  245 LRLYDPASGTisldghdirqlnPVWLRSKIGTVSQEPILFSCSIAENIAYGADDPSSvtaeeiqRVAEVANAVAFIRN-- 322
Cdd:PLN03232  664 LGELSHAETS------------SVVIRGSVAYVPQVSWIFNATVRENILFGSDFESE-------RYWRAIDVTALQHDld 724

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  323 -FPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLV-QEALDRLMDGRTVLVIAHRLSTIK 400
Cdd:PLN03232  725 lLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLP 804

                         410       420       430
                  ....*....|....*....|....*....|....
gi 767912304  401 NANMVAVLDQGKITEYGKHEElLSKPNGIYRKLM 434
Cdd:PLN03232  805 LMDRIILVSEGMIKEEGTFAE-LSKSGSLFKKLM 837
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
196-424 9.99e-29

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 113.57  E-value: 9.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 275
Cdd:PRK11231   3 LRTENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQ-----EPIlfscSIAENIAYG------------ADDPSSVT-AEEIQRVAEVAnavafirnfpqgfntvvgEKGVL 337
Cdd:PRK11231  80 LLPQhhltpEGI----TVRELVAYGrspwlslwgrlsAEDNARVNqAMEQTRINHLA------------------DRRLT 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 338 -LSGGQKQRIAIARALLKNPKILLLDEATSALDAENeylvQEALDRLM-----DGRTVLVIAHRLS-TIKNANMVAVLDQ 410
Cdd:PRK11231 138 dLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH----QVELMRLMrelntQGKTVVTVLHDLNqASRYCDHLVVLAN 213

                        250
                 ....*....|....
gi 767912304 411 GKITEYGKHEELLS 424
Cdd:PRK11231 214 GHVMAQGTPEEVMT 227
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
196-369 1.02e-28

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 116.20  E-value: 1.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIG 275
Cdd:PRK09452  15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILFS-CSIAENIAYGADdPSSVTAEEIQ-RVAEvanAVAFIR--NFPQgfntvvgEKGVLLSGGQKQRIAIARA 351
Cdd:PRK09452  90 TVFQSYALFPhMTVFENVAFGLR-MQKTPAAEITpRVME---ALRMVQleEFAQ-------RKPHQLSGGQQQRVAIARA 158

                        170
                 ....*....|....*...
gi 767912304 352 LLKNPKILLLDEATSALD 369
Cdd:PRK09452 159 VVNKPKVLLLDESLSALD 176
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 209-411 1.64e-28

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: 111.65  E-value: 1.64e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 209 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTI----SLDGHDIRQLNPVWLRSKIGTVSQEPILF 284
Cdd:cd03290   12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 285 SCSIAENIAYGaddpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEA 364
Cdd:cd03290   92 NATVEENITFG----SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767912304 365 TSALDAE-NEYLVQEALDRLM--DGRTVLVIAHRLSTIKNANMVAVLDQG 411
Cdd:cd03290  168 FSALDIHlSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 215-413 2.11e-28

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: 112.44  E-value: 2.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 215 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvWLRSKIGtVS---QEPILF-SCSIAE 290
Cdd:COG0411   21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLG-IArtfQNPRLFpELTVLE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 291 NIAYGAD------------DPSSVTAEEIQRVAEVANAVAFIrnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKI 358
Cdd:COG0411   99 NVLVAAHarlgrgllaallRLPRARREEREARERAEELLERV-----GLADRADEPAGNLSYGQQRRLEIARALATEPKL 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912304 359 LLLDEATSALDAEneyLVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 413
Cdd:COG0411  174 LLLDEPAAGLNPE---ETEELAELIRRlrderGITILLIEHDMDLVMGlADRIVVLDFGRV 231
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 196-417 3.43e-28

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: 109.95  E-value: 3.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARP---EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL--LRLYDPASGTISLDGHDIRqlnPVWL 270
Cdd:cd03213    4 LSFRNLTVTVKSSPsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 271 RSKIGTVSQEPILFSC-SIAENIAYGAddpssvtaeEIQRvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIA 349
Cdd:cd03213   81 RKIIGYVPQDDILHPTlTVRETLMFAA---------KLRG----------------------------LSGGERKRVSIA 123

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912304 350 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLST--IKNANMVAVLDQGKITEYG 417
Cdd:cd03213  124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 215-413 3.87e-28

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: 110.38  E-value: 3.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 215 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWlrSKIGTVSQEPILF-SCSIAENIA 293
Cdd:cd03268   17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYpNLTARENLR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 294 YGADDPsSVTAEEIQRVAEVAnavafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENE 373
Cdd:cd03268   95 LLARLL-GIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767912304 374 YLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGKI 413
Cdd:cd03268  163 KELRELILSLRDqGITVLISSHLLSEIqKVADRIGIINKGKL 204
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 196-413 4.24e-28

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 111.72  E-value: 4.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVH--FaYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRS 272
Cdd:COG1101    2 LELKNLSktF-NPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 273 K-IGTVSQEPILFSC---SIAEN--IAYGADDP----SSVTAEEIQRVAEvanavaFIRNFPQGF----NTVVGekgvLL 338
Cdd:COG1101   80 KyIGRVFQDPMMGTApsmTIEENlaLAYRRGKRrglrRGLTKKRRELFRE------LLATLGLGLenrlDTKVG----LL 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304 339 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGKI 413
Cdd:COG1101  150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
195-394 4.76e-28

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 111.88  E-value: 4.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPA-RPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlnPVWLRsk 273
Cdd:COG4525    3 MLTVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADR-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 iGTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFirnfpQGFntvvGEKGVL-LSGGQKQRIAIARA 351
Cdd:COG4525   79 -GVVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEELLALVGL-----ADF----ARRRIWqLSGGMRQRVGIARA 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767912304 352 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAH 394
Cdd:COG4525  149 LAADPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITH 193
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 196-414 6.49e-28

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: 108.28  E-value: 6.49e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLRSKI 274
Cdd:cd03216    1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQepilfscsiaeniaygaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIARALLK 354
Cdd:cd03216   78 AMVYQ----------------------------------------------------------LSVGERQMVEIARALAR 99

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912304 355 NPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKIT 414
Cdd:cd03216  100 NARLLILDEPTAALTPAEVERLFKVIRRLRAqGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 207-435 8.43e-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: 8.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  207 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVW---LRSKIGTVSQEpil 283
Cdd:TIGR02769  20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQD--- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  284 fscsiaeniAYGADDPSSvTAEEI-----------------QRVAEVANAVAF----IRNFPQGFntvvgekgvllSGGQ 342
Cdd:TIGR02769  97 ---------SPSAVNPRM-TVRQIigeplrhltsldeseqkARIAELLDMVGLrsedADKLPRQL-----------SGGQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  343 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKH 419
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDV 235

                         250
                  ....*....|....*.
gi 767912304  420 EELLSKPNGIYRKLMN 435
Cdd:TIGR02769 236 AQLLSFKHPAGRNLQS 251
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 195-415 1.13e-27

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: 109.83  E-value: 1.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYP-ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLN----PVW 269
Cdd:COG4181    8 IIELRGLTKTVGtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 270 LRSKIGTVSQ-EPILFSCSIAENIAY-----GADDPSSVTAEEIQRV--AEVANAvafirnFPQGfntvvgekgvlLSGG 341
Cdd:COG4181   88 RARHVGFVFQsFQLLPTLTALENVMLplelaGRRDARARARALLERVglGHRLDH------YPAQ-----------LSGG 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 342 QKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKITE 415
Cdd:COG4181  151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRerGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
213-426 3.76e-27

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 111.33  E-value: 3.76e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 213 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwlRS-KIGTVSQEPILFS-CSIAE 290
Cdd:PRK10851  17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---RDrKVGFVFQHYALFRhMTVFD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 291 NIAYGA------DDPSSvtAEEIQRVAEVANAVAFIR---NFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPKILLL 361
Cdd:PRK10851  94 NIAFGLtvlprrERPNA--AAIKAKVTQLLEMVQLAHladRYPAQ-----------LSGGQKQRVALARALAVEPQILLL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912304 362 DEATSALDAEneylVQEALDRLMdgR---------TVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:PRK10851 161 DEPFGALDAQ----VRKELRRWL--RqlheelkftSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 198-416 4.89e-27

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 113.24  E-value: 4.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 198 FKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhDIRqlnpvwlrskIGTV 277
Cdd:COG0488    1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 278 SQEPILFS-CSIAENIAYGADDPSSVTAE-------------------EIQ-------------RVAEVANAVafirNFP 324
Cdd:COG0488   67 PQEPPLDDdLTVLDTVLDGDAELRALEAEleeleaklaepdedlerlaELQeefealggweaeaRAEEILSGL----GFP 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 325 QG-FNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-----EYLVQEaldrlmDGrTVLVIAH-R-- 395
Cdd:COG0488  143 EEdLDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNY------PG-TVLVVSHdRyf 211

                        250       260
                 ....*....|....*....|.
gi 767912304 396 LSTIknANMVAVLDQGKITEY 416
Cdd:COG0488  212 LDRV--ATRILELDRGKLTLY 230
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
195-422 7.28e-27

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 112.42  E-value: 7.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLRSK 273
Cdd:COG1129    4 LLEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdAQAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGTVSQEPILFSC-SIAENIAYGADDPSSVT---AEEIQRVAEVANAVafirnfpqGFN----TVVGEkgvlLSGGQKQR 345
Cdd:COG1129   81 IAIIHQELNLVPNlSVAENIFLGREPRRGGLidwRAMRRRARELLARL--------GLDidpdTPVGD----LSVAQQQL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 346 IAIARALLKNPKILLLDEATSAL-DAENEYLVqEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEEL 422
Cdd:COG1129  149 VEIARALSRDARVLILDEPTASLtEREVERLF-RIIRRLKAqGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 196-427 7.56e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 108.95  E-value: 7.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYpaRPEVPiFQ-----DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI------RQ 264
Cdd:PRK13634   3 ITFQKVEHRY--QYKTP-FErralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkknKK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 265 LNPvwLRSKIGTVSQ--EPILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVL-LSGG 341
Cdd:PRK13634  80 LKP--LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELV--------GLPEELLARSPFeLSGG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 342 QKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGK 418
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229


                 ....*....
gi 767912304 419 HEELLSKPN 427
Cdd:PRK13634 230 PREIFADPD 238
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
217-424 1.40e-26

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 106.98  E-value: 1.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 217 FSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIGTVSQEPILFS-CSIAENIAYG 295
Cdd:PRK10771  18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 296 ADDPSSVTAEEIQRVAEVANAVaFIRNFpqgFNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDA--ENE 373
Cdd:PRK10771  96 LNPGLKLNAAQREKLHAIARQM-GIEDL---LARLPGQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPalRQE 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767912304 374 YLvqEALDRLMDGR--TVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLS 424
Cdd:PRK10771 168 ML--TLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 215-414 1.60e-26

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 111.66  E-value: 1.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 215 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP-VWLRSKIGTVSQEPILF-SCSIAENI 292
Cdd:COG3845   22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPrDAIALGIGMVHQHFMLVpNLTVAENI 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 293 AYGADDPSSV---TAEEIQRVAEVANAVafirnfpqGF----NTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEAT 365
Cdd:COG3845  102 VLGLEPTKGGrldRKAARARIRELSERY--------GLdvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPT 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304 366 SALDAeneylvQEAlDRLM--------DGRTVLVIAHRLSTIK-NANMVAVLDQGKIT 414
Cdd:COG3845  170 AVLTP------QEA-DELFeilrrlaaEGKSIIFITHKLREVMaIADRVTVLRRGKVV 220
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
195-420 1.70e-26

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 107.02  E-value: 1.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI---RQLNP---V 268
Cdd:COG4161    2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEkaiR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 269 WLRSKIGTVSQE----PILfscSIAENIAygaDDPSSV---TAEEIQRVAEVANAVAFIRNFPQGFNtvvgekgVLLSGG 341
Cdd:COG4161   79 LLRQKVGMVFQQynlwPHL---TVMENLI---EAPCKVlglSKEQAREKAMKLLARLRLTDKADRFP-------LHLSGG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 342 QKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKH 419
Cdd:COG4161  146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFArKVASQVVYMEKGRIIEQGDA 225


                 .
gi 767912304 420 E 420
Cdd:COG4161  226 S 226
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
196-425 1.96e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 107.87  E-value: 1.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPE---VPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVW-LR 271
Cdd:PRK13633   5 IKCKNVSYKYESNEEsteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 272 SKIGTVSQEP--ILFSCSIAENIAYGADDpSSVTAEEIQ-RVAEVANAVA---FIRNFPQgfntvvgekgvLLSGGQKQR 345
Cdd:PRK13633  85 NKAGMVFQNPdnQIVATIVEEDVAFGPEN-LGIPPEEIReRVDESLKKVGmyeYRRHAPH-----------LLSGGQKQR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 346 IAIARALLKNPKILLLDEATSALDAENEylvQEALDRLMD-----GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHE 420
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGR---REVVNTIKElnkkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229


                 ....*
gi 767912304 421 ELLSK 425
Cdd:PRK13633 230 EIFKE 234
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 196-413 2.30e-26

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: 106.05  E-value: 2.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 275
Cdd:cd03263    1 LQIRNLTKTYK-KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILFS-CSIAENIAYGAddpsSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEkgvlLSGGQKQRIAIARALLK 354
Cdd:cd03263   79 YCPQFDALFDeLTVREHLRFYA----RLKGLPKSEIKEEVELLLRVLGLTDKANKRART----LSGGMKRKLSLAIALIG 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 355 NPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKI 413
Cdd:cd03263  151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKL 210
PTZ00243 PTZ00243
ABC transporter; Provisional
 205-433 2.42e-26

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 112.56  E-value: 2.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  205 YPARPEVpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTisldghdirqlnpVWLRSKIGTVSQEPILF 284
Cdd:PTZ00243  668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR-------------VWAERSIAYVPQQAWIM 733

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  285 SCSIAENIAYGADDpssvTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEA 364
Cdd:PTZ00243  734 NATVRGNILFFDEE----DAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  365 TSALDAE-NEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPngIYRKL 433
Cdd:PTZ00243  810 LSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS--LYATL 877
cbiO PRK13649
energy-coupling factor transporter ATPase;
195-418 2.77e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 107.14  E-value: 2.77e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPA-RP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI------RQLN 266
Cdd:PRK13649   2 GINLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsknKDIK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 267 PVwlRSKIGTVSQ--EPILFSCSIAENIAYGADDpSSVTAEEIQRVA-EVANAVAFIRNFpqgFNTVVGEkgvlLSGGQK 343
Cdd:PRK13649  82 QI--RKKVGLVFQfpESQLFEETVLKDVAFGPQN-FGVSQEEAEALArEKLALVGISESL---FEKNPFE----LSGGQM 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304 344 QRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGK 418
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 213-425 3.94e-26

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


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 106.86  E-value: 3.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 213 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDpASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENI 292
Cdd:cd03289   19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 293 aygadDPSSV-TAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 371
Cdd:cd03289   98 -----DPYGKwSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767912304 372 NEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSK 425
Cdd:cd03289  173 TYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 196-413 5.42e-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: 104.76  E-value: 5.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAY-PARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKI 274
Cdd:cd03266    2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALL 353
Cdd:cd03266   81 GFVSDSTGLYDrLTARENLEYFAGLYGLKGDELTARLEELADRL--------GMEELLDRRVGGFSTGMRQKVAIARALV 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912304 354 KNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 413
Cdd:cd03266  153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRV 214
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 219-426 6.72e-26

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 105.60  E-value: 6.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 219 LSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV--------WLRSKIGTVSQEPILFSC-SIA 289
Cdd:PRK11264  24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqqkglirQLRQHVGFVFQNFNLFPHrTVL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 290 ENIAYGaddPSSVTAEEiqRVAEVANAVAFIRNfpqgfntvVGEKGV------LLSGGQKQRIAIARALLKNPKILLLDE 363
Cdd:PRK11264 104 ENIIEG---PVIVKGEP--KEEATARARELLAK--------VGLAGKetsyprRLSGGQQQRVAIARALAMRPEVILFDE 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304 364 ATSALDAEneyLVQEALDRLM----DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:PRK11264 171 PTSALDPE---LVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADP 235
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 213-426 8.15e-26

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 105.95  E-value: 8.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 213 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASG-----TISLDGHDIRQLNPVW-LRSKIGTVSQEPILFSC 286
Cdd:PRK14271  36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLeFRRRVGMLFQRPNPFPM 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 287 SIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATS 366
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWD---AVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912304 367 ALDAENEYLVQEALDRLMDGRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSSP 253
cbiO PRK13642
energy-coupling factor transporter ATPase;
196-424 1.13e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 105.56  E-value: 1.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNpVW-LRSKI 274
Cdd:PRK13642   5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN-VWnLRRKI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIrnfpqGFNTvvgEKGVLLSGGQKQRIAIARAL 352
Cdd:PRK13642  84 GMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML-----DFKT---REPARLSGGQKQRVAVAGII 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912304 353 LKNPKILLLDEATSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLS 424
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
215-430 1.43e-25

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 107.81  E-value: 1.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 215 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS----KIGTVSQEPILFS-CSIA 289
Cdd:PRK10070  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTVL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 290 ENIAYGAdDPSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALD 369
Cdd:PRK10070 125 DNTAFGM-ELAGINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912304 370 AENEYLVQEALDRLM--DGRTVLVIAHRL-STIKNANMVAVLDQGKITEYGKHEELLSKPNGIY 430
Cdd:PRK10070 197 PLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 196-422 1.76e-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: 103.76  E-value: 1.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  196 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL-RSKI 274
Cdd:TIGR03410   1 LEVSNLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  275 GTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVanavafirnFPQGFnTVVGEKGVLLSGGQKQRIAIARALL 353
Cdd:TIGR03410  78 AYVPQGREIFPrLTVEENLLTGLAALPRRSRKIPDEIYEL---------FPVLK-EMLGRRGGDLSGGQQQQLAIARALV 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912304  354 KNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEEL 422
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAegGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
PLN03130 PLN03130
ABC transporter C family member; Provisional
 168-436 2.01e-25

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 109.83  E-value: 2.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  168 RLWELLERE-----PKLPFNEGvilneksfQGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLS 242
Cdd:PLN03130  590 RLEELLLAEervllPNPPLEPG--------LPAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIS 661

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  243 LLLRLYDPASGTIsldghdirqlnpVWLRSKIGTVSQEPILFSCSIAENIAYGADdpssVTAEEIQRVAEVANAVAFIRN 322
Cdd:PLN03130  662 AMLGELPPRSDAS------------VVIRGTVAYVPQVSWIFNATVRDNILFGSP----FDPERYERAIDVTALQHDLDL 725

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  323 FPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneYLVQEALDRL----MDGRTVLVIAHRLST 398
Cdd:PLN03130  726 LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA---HVGRQVFDKCikdeLRGKTRVLVTNQLHF 802

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767912304  399 IKNANMVAVLDQGKITEYGKHEELLSkpNG-IYRKLMNK 436
Cdd:PLN03130  803 LSQVDRIILVHEGMIKEEGTYEELSN--NGpLFQKLMEN 839
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
213-426 2.05e-25

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 104.28  E-value: 2.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 213 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIR-------QLNPV------WLRSKIGTVSQ 279
Cdd:PRK10619  20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVAdknqlrLLRTRLTMVFQ 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 280 EPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNFPQGfntvvgEKGVLLSGGQKQRIAIARALLKNPKI 358
Cdd:PRK10619 100 HFNLWShMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQG------KYPVHLSGGQQQRVSIARALAMEPEV 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912304 359 LLLDEATSALDAEneyLVQEALdRLM-----DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:PRK10619 174 LLFDEPTSALDPE---LVGEVL-RIMqqlaeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNP 243
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 195-420 2.56e-25

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 103.56  E-value: 2.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH-----------DIR 263
Cdd:PRK11124   2 SIQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpsdkAIR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 264 QLnpvwlRSKIGTVSQE----PILfscSIAENI------AYGADDPSSVT-AEEI---QRVAEVANAvafirnFPQGfnt 329
Cdd:PRK11124  79 EL-----RRNVGMVFQQynlwPHL---TVQQNLieapcrVLGLSKDQALArAEKLlerLRLKPYADR------FPLH--- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 330 vvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAV 407
Cdd:PRK11124 142 --------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVArKTASRVVY 213

                        250
                 ....*....|...
gi 767912304 408 LDQGKITEYGKHE 420
Cdd:PRK11124 214 MENGHIVEQGDAS 226
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
 12-169 3.41e-25

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: 104.44  E-value: 3.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18551  132 FLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRA 211

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 169
Cdd:cd18551  212 GLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 196-435 4.38e-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: 107.46  E-value: 4.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKN--VHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKS-TVLSLLlRLYDP----ASGTISLDGHDIRQLNPV 268
Cdd:COG4172    7 LSVEDlsVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDLLGLSER 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 269 WLR----SKIGTVSQEPI-----LFSCS--IAENIA--YGADDpssvtAEEIQRVAEVANAVAfIRN-------FP-Qgf 327
Cdd:COG4172   85 ELRrirgNRIAMIFQEPMtslnpLHTIGkqIAEVLRlhRGLSG-----AAARARALELLERVG-IPDperrldaYPhQ-- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 328 ntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneyLVQ-EALDRLMD-----GRTVLVIAHRLSTIKN 401
Cdd:COG4172  157 ----------LSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaQILDLLKDlqrelGMALLLITHDLGVVRR 222

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 767912304 402 -ANMVAVLDQGKITEYGKHEELLSKPNGIY-RKLMN 435
Cdd:COG4172  223 fADRVAVMRQGEIVEQGPTAELFAAPQHPYtRKLLA 258
cbiO PRK13641
energy-coupling factor transporter ATPase;
195-427 5.16e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 103.76  E-value: 5.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYParPEVPI----FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIR----QLN 266
Cdd:PRK13641   2 SIKFENVDYIYS--PGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 267 PVWLRSKIGTVSQ--EPILFSCSIAENIAYGaddPSSVTAEEiQRVAEvaNAVAFIRNFpqGFNTVVGEKGVL-LSGGQK 343
Cdd:PRK13641  80 LKKLRKKVSLVFQfpEAQLFENTVLKDVEFG---PKNFGFSE-DEAKE--KALKWLKKV--GLSEDLISKSPFeLSGGQM 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 344 QRIAIARALLKNPKILLLDEATSALDAEN-EYLVQEALDRLMDGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEE 421
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKE 231


                 ....*.
gi 767912304 422 LLSKPN 427
Cdd:PRK13641 232 IFSDKE 237
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 196-425 6.28e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 103.77  E-value: 6.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH--DIRQLNPVWLRSK 273
Cdd:PRK13636   6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGTVSQEP--ILFSCSIAENIAYGADDpSSVTAEEIQRVAEVA---NAVAFIRNFPQGFntvvgekgvlLSGGQKQRIAI 348
Cdd:PRK13636  84 VGMVFQDPdnQLFSASVYQDVSFGAVN-LKLPEDEVRKRVDNAlkrTGIEHLKDKPTHC----------LSFGQKKRVAI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 349 ARALLKNPKILLLDEATSALD----AENEYLVQEALDRLmdGRTVLVIAHRLSTIK-NANMVAVLDQGKITEYGKHEELL 423
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230


                 ..
gi 767912304 424 SK 425
Cdd:PRK13636 231 AE 232
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 213-425 7.03e-25

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: 108.07  E-value: 7.03e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   213 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDpASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENI 292
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL 1312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   293 aygadDP-SSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 371
Cdd:TIGR01271 1313 -----DPyEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPV 1387

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767912304   372 NEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSK 425
Cdd:TIGR01271 1388 TLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
204-408 8.61e-25

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 100.77  E-value: 8.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 204 AYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHdirqlnpvwlrSKIGTVSQ---E 280
Cdd:NF040873   1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQrseV 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 281 PILFSCSIAENIAYG------------ADDPSSVTaEEIQRV--AEVANAVafirnfpqgfntvVGEkgvlLSGGQKQRI 346
Cdd:NF040873  67 PDSLPLTVRDLVAMGrwarrglwrrltRDDRAAVD-DALERVglADLAGRQ-------------LGE----LSGGQRQRA 128

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912304 347 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKNANMVAVL 408
Cdd:NF040873 129 LLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
cbiO PRK13637
energy-coupling factor transporter ATPase;
199-421 9.30e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 103.20  E-value: 9.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 199 KNVHFAY-PARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI--RQLNPVWLRSKI 274
Cdd:PRK13637   6 ENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQEP--ILFSCSIAENIAYGaddPSS--VTAEEIQ-RVAEVANAVAFirnfpqGFNTVVGEKGVLLSGGQKQRIAIA 349
Cdd:PRK13637  86 GLVFQYPeyQLFEETIEKDIAFG---PINlgLSEEEIEnRVKRAMNIVGL------DYEDYKDKSPFELSGGQKRRVAIA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912304 350 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEE 421
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 218-426 9.46e-25

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 103.89  E-value: 9.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 218 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI-----------RQ------------LNPvwlRSKI 274
Cdd:PRK11308  35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpeaqkllRQkiqivfqnpygsLNP---RKKV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQEPILFscsiaeNIAYGAddpssvtAEEIQRVAEVANAVA----FIRNFPQGFntvvgekgvllSGGQKQRIAIAR 350
Cdd:PRK11308 112 GQILEEPLLI------NTSLSA-------AERREKALAMMAKVGlrpeHYDRYPHMF-----------SGGQRQRIAIAR 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 351 ALLKNPKILLLDEATSALDAEneylVQ-EALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELL 423
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVS----VQaQVLNLMMDlqqelGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIF 243


                 ...
gi 767912304 424 SKP 426
Cdd:PRK11308 244 NNP 246
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 212-439 1.68e-24

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: 102.24  E-value: 1.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 212 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlnpvwlrsKIGTVSQEPILFSCSIAEN 291
Cdd:cd03291   51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKEN 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 292 IAYGaddpssVTAEEIqRVAEVANAVAF---IRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSAL 368
Cdd:cd03291  118 IIFG------VSYDEY-RYKSVVKACQLeedITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912304 369 DAENEYLVQEA-LDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYRKLMNKQSF 439
Cdd:cd03291  191 DVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTF 262
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 195-426 2.30e-24

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 101.46  E-value: 2.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYpARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD-----PASGTISLDGHDI--RQLNP 267
Cdd:PRK14267   4 AIETVNLRVYY-GSNHV--IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 268 VWLRSKIGTVSQEPILFS-CSIAENIAYGADDPSSVTA-EEIQRVAEVA-NAVAFIRNFPQGFNTVVGEkgvlLSGGQKQ 344
Cdd:PRK14267  81 IEVRREVGMVFQYPNPFPhLTIYDNVAIGVKLNGLVKSkKELDERVEWAlKKAALWDEVKDRLNDYPSN----LSGGQRQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 345 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHR-LSTIKNANMVAVLDQGKITEYGKHEELL 423
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVF 236


                 ...
gi 767912304 424 SKP 426
Cdd:PRK14267 237 ENP 239
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 210-394 2.69e-24

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: 100.59  E-value: 2.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 210 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH----DIRQLNPVWL----RSKIGTVSQep 281
Cdd:COG4778   23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPREIlalrRRTIGYVSQ-- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 282 ilFSCSIaeniaygaddPSsVTAEEIqrVAE------VANAVAFIR--------NFPQGF-----NTvvgekgvlLSGGQ 342
Cdd:COG4778  101 --FLRVI----------PR-VSALDV--VAEpllergVDREEARARarellarlNLPERLwdlppAT--------FSGGE 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 343 KQRIAIARALLKNPKILLLDEATSALDAENE----YLVQEALDRlmdGRTVLVIAH 394
Cdd:COG4778  158 QQRVNIARGFIADPPLLLLDEPTASLDAANRavvvELIEEAKAR---GTAIIGIFH 210
PTZ00243 PTZ00243
ABC transporter; Provisional
 194-435 2.82e-24

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 106.40  E-value: 2.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  194 GALEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS 272
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  273 KIGTVSQEPILFSCSIAENIaygadDP-SSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARA 351
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNV-----DPfLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARA 1459

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  352 LLK-NPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIY 430
Cdd:PTZ00243 1460 LLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539


                  ....*
gi 767912304  431 RKLMN 435
Cdd:PTZ00243 1540 HSMVE 1544
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 174-416 2.86e-24

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 105.15  E-value: 2.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 174 EREPKLPFNEGVILNEKsfqgALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASG 253
Cdd:COG0488  298 DKTVEIRFPPPERLGKK----VLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 254 TISLdGHDIrqlnpvwlrsKIGTVSQEPILFSC--SIAENIAYGADDpssvtAEEIQrvaevanavafIRNFPQGFN--- 328
Cdd:COG0488  371 TVKL-GETV----------KIGYFDQHQEELDPdkTVLDELRDGAPG-----GTEQE-----------VRGYLGRFLfsg 423

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 329 ----TVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLmDGrTVLVIAH-R--LSTIkn 401
Cdd:COG0488  424 ddafKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHdRyfLDRV-- 495

                        250
                 ....*....|....*
gi 767912304 402 ANMVAVLDQGKITEY 416
Cdd:COG0488  496 ATRILEFEDGGVREY 510
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 210-426 3.56e-24

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 103.77  E-value: 3.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 210 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPIL-FSCSI 288
Cdd:PRK09536  15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 289 AENIAYG---------ADDPSSVTAeeIQRVAEVANAVAFIrnfPQGFNTvvgekgvlLSGGQKQRIAIARALLKNPKIL 359
Cdd:PRK09536  95 RQVVEMGrtphrsrfdTWTETDRAA--VERAMERTGVAQFA---DRPVTS--------LSGGERQRVLLARALAQATPVL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912304 360 LLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDdGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTAD 230
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
207-415 4.31e-24

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 100.92  E-value: 4.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 207 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQL--------------------- 265
Cdd:PRK10419  21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraqrkafrrdiqmvfqdsis 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 266 --NPvwlRSKIGTVSQEPILFSCSIAEniaygaddpssvtAEEIQRVAEVANAV----AFIRNFPQGfntvvgekgvlLS 339
Cdd:PRK10419 101 avNP---RKTVREIIREPLRHLLSLDK-------------AERLARASEMLRAVdlddSVLDKRPPQ-----------LS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 340 GGQKQRIAIARALLKNPKILLLDEATSALDAeneYLVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 413
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDL---VLQAGVIRLLKKlqqqfGTACLFITHDLRLVERfCQRVMVMDNGQI 230


                 ..
gi 767912304 414 TE 415
Cdd:PRK10419 231 VE 232
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 212-439 4.86e-24

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 105.76  E-value: 4.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   212 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlnpvwlrsKIGTVSQEPILFSCSIAEN 291
Cdd:TIGR01271  440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   292 IAYGaddpssVTAEEIqRVAEVANAVAF---IRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSAL 368
Cdd:TIGR01271  507 IIFG------LSYDEY-RYTSVIKACQLeedIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHL 579

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912304   369 DAENEYLVQEA-LDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYRKLMNKQSF 439
Cdd:TIGR01271  580 DVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAF 651
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 196-429 5.70e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 100.54  E-value: 5.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL--RSK 273
Cdd:PRK13639   2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGTVSQEP--ILFSCSIAENIAYGADDpSSVTAEEIQ-RVAEVANAVAFirnfpQGFNTVVGEKgvlLSGGQKQRIAIAR 350
Cdd:PRK13639  80 VGIVFQNPddQLFAPTVEEDVAFGPLN-LGLSKEEVEkRVKEALKAVGM-----EGFENKPPHH---LSGGQKKRVAIAG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 351 ALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSKPNG 428
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIET 230


                 .
gi 767912304 429 I 429
Cdd:PRK13639 231 I 231
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 195-426 6.88e-24

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 100.11  E-value: 6.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPAS-----GTISLDGHDI--RQLNP 267
Cdd:PRK14258   7 AIKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 268 VWLRSKIGTVSQEPILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAfirNFPQGFNTVVGEKGVLLSGGQKQRIA 347
Cdd:PRK14258  84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDA---DLWDEIKHKIHKSALDLSGGQQQRLC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 348 IARALLKNPKILLLDEATSALDA----ENEYLVQEAldRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQ-----GKITEYG 417
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPiasmKVESLIQSL--RLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFG 238


                 ....*....
gi 767912304 418 KHEELLSKP 426
Cdd:PRK14258 239 LTKKIFNSP 247
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 207-394 1.06e-23

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: 98.88  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 207 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL---LRLYDPASGTISLDGhdiRQLNPVWLRSKIGTVSQEPIL 283
Cdd:cd03234   16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDIL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 284 FSC-SIAENIAYGADDPSSVTAEEIQRVAEVA----NAVAfirnfpqgfNTVVGEKGVL-LSGGQKQRIAIARALLKNPK 357
Cdd:cd03234   93 LPGlTVRETLTYTAILRLPRKSSDAIRKKRVEdvllRDLA---------LTRIGGNLVKgISGGERRRVSIAVQLLWDPK 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767912304 358 ILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAH 394
Cdd:cd03234  164 VLILDEPTSGLDSFTALNLVSTLSQLArRNRIVILTIH 201
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 196-417 1.18e-23

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: 97.98  E-value: 1.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAypaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRL--YDPASGTISLDGHDIRQLnPVWLRSK 273
Cdd:cd03217    1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDL-PPEERAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IG-TVS-QEPIlfscsiaeniaygaddpssvtaeeiqRVAEVANAvAFIRNFPQGFntvvgekgvllSGGQKQRIAIARA 351
Cdd:cd03217   77 LGiFLAfQYPP--------------------------EIPGVKNA-DFLRYVNEGF-----------SGGEKKRNEILQL 118

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912304 352 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAH--RLSTIKNANMVAVLDQGKITEYG 417
Cdd:cd03217  119 LLLEPDLAILDEPDSGLDIDALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 216-422 1.66e-23

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 97.83  E-value: 1.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 216 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIGTVSQEPILFSCSIA-ENIAY 294
Cdd:cd03265   18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwENLYI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 295 GADDPSSVTAEEIQRVAEVANAVAF-------IRNFpqgfntvvgekgvllSGGQKQRIAIARALLKNPKILLLDEATSA 367
Cdd:cd03265   97 HARLYGVPGAERRERIDELLDFVGLleaadrlVKTY---------------SGGMRRRLEIARSLVHRPEVLFLDEPTIG 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304 368 LDAENEYLVQEALDRLMD--GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEEL 422
Cdd:cd03265  162 LDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
 12-169 2.81e-23

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: 99.16  E-value: 2.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd07346  135 FYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDA 214

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 169
Cdd:cd07346  215 NLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
 12-142 6.73e-23

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


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 97.71  E-value: 6.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:pfam00664 137 FYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKA 216

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767912304   92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA 142
Cdd:pfam00664 217 GIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLF 267
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 196-434 8.16e-23

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 100.94  E-value: 8.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARP--------EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYdPASGTISLDGHDIRQLNP 267
Cdd:PRK15134 276 LDVEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 268 ---VWLRSKIGTVSQEPilFSC-----SIAENIAYG--ADDPSSVTAEEIQRVAEVANAV----AFIRNFPQGFntvvge 333
Cdd:PRK15134 355 rqlLPVRHRIQVVFQDP--NSSlnprlNVLQIIEEGlrVHQPTLSAAQREQQVIAVMEEVgldpETRHRYPAEF------ 426

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 334 kgvllSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTV--LVIAHRLSTIKN-ANMVAVLDQ 410
Cdd:PRK15134 427 -----SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQ 501

                        250       260
                 ....*....|....*....|....*
gi 767912304 411 GKITEYGKHEELLSKPNGIY-RKLM 434
Cdd:PRK15134 502 GEVVEQGDCERVFAAPQQEYtRQLL 526
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
198-426 8.20e-23

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 99.33  E-value: 8.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 198 FKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIGTV 277
Cdd:PRK11000   6 LRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 278 SQEPILFS-CSIAENIAYGADDPSSVTAEEIQRV---AEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALL 353
Cdd:PRK11000  81 FQSYALYPhLSVAENMSFGLKLAGAKKEEINQRVnqvAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLV 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 354 KNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAH-RLSTIKNANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
cbiO PRK13644
energy-coupling factor transporter ATPase;
196-427 1.74e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 96.59  E-value: 1.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTI---SLDGHDIRQLNPVwlRS 272
Cdd:PRK13644   2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsGIDTGDFSKLQGI--RK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 273 KIGTVSQEP--ILFSCSIAENIAYGaddPSSVTAEEIQRVAEVANAVAFIrnfpqGFNTVVGEKGVLLSGGQKQRIAIAR 350
Cdd:PRK13644  78 LVGIVFQNPetQFVGRTVEEDLAFG---PENLCLPPIEIRKRVDRALAEI-----GLEKYRHRSPKTLSGGQGQCVALAG 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304 351 ALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPN 427
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
219-426 1.85e-22

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 98.02  E-value: 1.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 219 LSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH---DIRQlnPVWL---RSKIGTVSQEPILFS-CSIAEN 291
Cdd:PRK11144  19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEK--GICLppeKRRIGYVFQDARLFPhYKVRGN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 292 IAYGAddpSSVTAEEIQRVAEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 371
Cdd:PRK11144  97 LRYGM---AKSMVAQFDKIVALLGIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 372 NEYLVQEALDRLmdGRTV----LVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:PRK11144 163 RKRELLPYLERL--AREInipiLYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEEVWASS 220
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 170-437 2.90e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 96.84  E-value: 2.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 170 WELLEREPKLPFNEGVILNEKSFQGALEFKNVHfayparpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD 249
Cdd:PRK13631   5 FMKKKLKVPNPLSDDIILRVKNLYCVFDEKQEN-------ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 250 PASGTISLD----GHDIRQLNPVW------------LRSKIGTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVA 311
Cdd:PRK13631  78 SKYGTIQVGdiyiGDKKNNHELITnpyskkiknfkeLRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLAK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 312 EVANAVA----FIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEY-LVQEALDRLMDG 386
Cdd:PRK13631 158 FYLNKMGlddsYLERSPFG-----------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANN 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912304 387 RTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEEL-----------------------LSKPNGIYRKLMNKQ 437
Cdd:PRK13631 227 KTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIftdqhiinstsiqvprviqvindLIKKDPKYKKLYQKQ 301
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
195-394 3.62e-22

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 95.15  E-value: 3.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdIRQLNPVWLRski 274
Cdd:PRK11248   1 MLQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG--KPVEGPGAER--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQ-EPILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFirnfpQGFntvvGEKGVL-LSGGQKQRIAIARAL 352
Cdd:PRK11248  73 GVVFQnEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGL-----EGA----EKRYIWqLSGGQRQRVGIARAL 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767912304 353 LKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAH 394
Cdd:PRK11248 144 AANPQLLLLDEPFGALDAFTREQMQTLLLKLWqeTGKQVLLITH 187
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
 12-169 3.81e-22

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


Pssm-ID: 350021 [Multi-domain]  Cd Length: 300  Bit Score: 96.00  E-value: 3.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18577  143 FIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKA 222

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 169
Cdd:cd18577  223 GIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 197-427 4.98e-22

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 94.76  E-value: 4.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 197 EFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGT 276
Cdd:COG4604    3 EIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 277 VSQEPILfscsiaeniaygaddPSSVTAEEIqrvaevanaVAFIRnFP--QGFNTVVGEKGV--------L--------- 337
Cdd:COG4604   80 LRQENHI---------------NSRLTVREL---------VAFGR-FPysKGRLTAEDREIIdeaiayldLedladryld 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 338 -LSGGQKQRIAIARALLKNPKILLLDEATSALDAenEYLVQ--EALDRLMD--GRTVLVIAHRLstiknaNMVAV----- 407
Cdd:COG4604  135 eLSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM--KHSVQmmKLLRRLADelGKTVVIVLHDI------NFASCyadhi 206

                        250       260
                 ....*....|....*....|..
gi 767912304 408 --LDQGKITEYGKHEELLSKPN 427
Cdd:COG4604  207 vaMKDGRVVAQGTPEEIITPEV 228
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
196-437 5.21e-22

ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 94.90  E-value: 5.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAY------PARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH--------- 260
Cdd:COG4167    5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdyky 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 261 ---DIR--------QLNPvwlRSKIGTVSQEPILFScsiaeniaygaddpSSVTAEE-IQRVAEVANAVAFIRN----FP 324
Cdd:COG4167   85 rckHIRmifqdpntSLNP---RLNIGQILEEPLRLN--------------TDLTAEErEERIFATLRLVGLLPEhanfYP 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 325 QgfntvvgekgvLLSGGQKQRIAIARALLKNPKILLLDEATSALDAE------NEYL-VQEALdrlmdGRTVLVIAHRLS 397
Cdd:COG4167  148 H-----------MLSSGQKQRVALARALILQPKIIIADEALAALDMSvrsqiiNLMLeLQEKL-----GISYIYVSQHLG 211

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 767912304 398 TIKN-ANMVAVLDQGKITEYGKHEELLSKP-NGIYRKLMNKQ 437
Cdd:COG4167  212 IVKHiSDKVLVMHQGEVVEYGKTAEVFANPqHEVTKRLIESH 253
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
 8-168 5.42e-22

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: 95.48  E-value: 5.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   8 CKLQFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDH 87
Cdd:cd18590  128 LGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALER 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  88 VMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGG 167
Cdd:cd18590  208 TYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAA 287


                 .
gi 767912304 168 R 168
Cdd:cd18590  288 K 288
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
213-424 8.10e-22

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 94.28  E-value: 8.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 213 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEpilfscsiaeni 292
Cdd:PRK10253  22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN------------ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 293 aygADDPSSVTAEEIQRVAEVANAVAFIRNFPQ------------GFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILL 360
Cdd:PRK10253  90 ---ATTPGDITVQELVARGRYPHQPLFTRWRKEdeeavtkamqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304 361 LDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLS 424
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT 233
cbiO PRK13643
energy-coupling factor transporter ATPase;
196-425 8.28e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 94.80  E-value: 8.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYpaRPEVPIFQ----DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDghDI--------R 263
Cdd:PRK13643   2 IKFEKVNYTY--QPNSPFASralfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstskqK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 264 QLNPVwlRSKIGTVSQEP--ILFSCSIAENIAYGADDpSSVTAEEIQRV-AEVANAVAFIRNFPQgfntvvgEKGVLLSG 340
Cdd:PRK13643  78 EIKPV--RKKVGVVFQFPesQLFEETVLKDVAFGPQN-FGIPKEKAEKIaAEKLEMVGLADEFWE-------KSPFELSG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 341 GQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGK 418
Cdd:PRK13643 148 GQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227


                 ....*..
gi 767912304 419 HEELLSK 425
Cdd:PRK13643 228 PSDVFQE 234
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
195-423 9.18e-22

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 95.26  E-value: 9.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSKI 274
Cdd:PRK13537   7 PIDFRNVEKRYGDKLVV---DGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQ----EPilfSCSIAENIA-----YGaddpssVTAEEIQrvAEVANAVAFIRnFPQGFNTVVGEkgvlLSGGQKQR 345
Cdd:PRK13537  83 GVVPQfdnlDP---DFTVRENLLvfgryFG------LSAAAAR--ALVPPLLEFAK-LENKADAKVGE----LSGGMKRR 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 346 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQG-KITEyGKHEEL 422
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGrKIAE-GAPHAL 225


                 .
gi 767912304 423 L 423
Cdd:PRK13537 226 I 226
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 196-394 1.30e-21

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: 90.59  E-value: 1.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlnpvwlrskig 275
Cdd:cd03221    1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 tvsqepilfscsiAENIAYgaddpssvtaeeiqrvaevanavafirnFPQgfntvvgekgvlLSGGQKQRIAIARALLKN 355
Cdd:cd03221   62 -------------TVKIGY----------------------------FEQ------------LSGGEKMRLALAKLLLEN 88

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767912304 356 PKILLLDEATSALDAENEYLVQEALDRLmdGRTVLVIAH 394
Cdd:cd03221   89 PNLLLLDEPTNHLDLESIEALEEALKEY--PGTVILVSH 125
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
196-394 1.54e-21

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 97.49  E-value: 1.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPE-VPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---- 270
Cdd:PRK10535   5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 271 RSKIGTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRvaevanAVAFIRNFpqGFNTVVGEKGVLLSGGQKQRIAIA 349
Cdd:PRK10535  85 REHFGFIFQRYHLLShLTAAQNVEVPAVYAGLERKQRLLR------AQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767912304 350 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAH 394
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTH 202
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 195-438 1.82e-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: 1.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYP-------------------ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTI 255
Cdd:COG1134    4 MIEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 256 SLDGhdirqlNPVWL-------------RskigtvsqEPILFSCSIaeniaYGaddpssVTAEEI-QRVAEVanaVAF-- 319
Cdd:COG1134   84 EVNG------RVSALlelgagfhpeltgR--------ENIYLNGRL-----LG------LSRKEIdEKFDEI---VEFae 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 320 IRNFpqgFNTVVGekgvLLSGGQKQRIAIARALLKNPKILLLDEATSALDAEneyLVQEALDRLMD----GRTVLVIAHR 395
Cdd:COG1134  136 LGDF---IDQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA---FQKKCLARIRElresGRTVIFVSHS 205

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 767912304 396 LSTIKN-ANMVAVLDQGKITEYGKHEELLSKpngiYRKLMNKQS 438
Cdd:COG1134  206 MGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA----YEALLAGRE 245
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
 12-169 1.93e-21

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: 94.03  E-value: 1.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18552  135 FYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRL 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  92 ARKEAFARAG------FFGATGLSGnlivlsVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGA 165
Cdd:cd18552  215 SMKIARARALssplmeLLGAIAIAL------VLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAA 288


                 ....
gi 767912304 166 GGRL 169
Cdd:cd18552  289 AERI 292
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 190-417 2.10e-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: 92.21  E-value: 2.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 190 KSFQGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlNPVW 269
Cdd:cd03220   14 KGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 270 LrskIG-TVSQEP-------ILFSCSIaeniaYGaddpssVTAEEIQRVaevanaVAFIRNF---PQGFNTVVGEkgvlL 338
Cdd:cd03220   88 L---LGlGGGFNPeltgrenIYLNGRL-----LG------LSRKEIDEK------IDEIIEFselGDFIDLPVKT----Y 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 339 SGGQKQRIAIARALLKNPKILLLDEATSALDAEneyLVQEALDRLM----DGRTVLVIAHRLSTIKN-ANMVAVLDQGKI 413
Cdd:cd03220  144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAA---FQEKCQRRLRellkQGKTVILVSHDPSSIKRlCDRALVLEKGKI 220


                 ....
gi 767912304 414 TEYG 417
Cdd:cd03220  221 RFDG 224
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 212-426 2.92e-21

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 91.84  E-value: 2.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 212 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRSK--IGTVSQEPILF-SCSI 288
Cdd:cd03218   14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL-PMHKRARlgIGYLPQEASIFrKLTV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 289 AENIaYGADDPSSVTAEEIQRVAEvanavAFIRNFpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSAL 368
Cdd:cd03218   93 EENI-LAVLEIRGLSKKEREEKLE-----ELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912304 369 D----AENEYLVQEALDRlmdGRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:cd03218  165 DpiavQDIQKIIKILKDR---GIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANE 224
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 196-363 3.25e-21

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 92.01  E-value: 3.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRSK-- 273
Cdd:COG1137    4 LEAENLVKSYGKRTVV---KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-PMHKRARlg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGTVSQEPILF-SCSIAENIaYGADDPSSVTAEEIQRVAEvanavAFIRNFpqGFNTVVGEKGVLLSGGQKQRIAIARAL 352
Cdd:COG1137   80 IGYLPQEASIFrKLTVEDNI-LAVLELRKLSKKEREERLE-----ELLEEF--GITHLRKSKAYSLSGGERRRVEIARAL 151

                        170
                 ....*....|.
gi 767912304 353 LKNPKILLLDE 363
Cdd:COG1137  152 ATNPKFILLDE 162
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 196-417 6.25e-21

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


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 90.42  E-value: 6.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNpvwlRSKIG 275
Cdd:cd03269    1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILF-SCSIAENIAYGADdPSSVTAEEIQRVAEvanavAFIRNFPQG--FNTVVGEkgvlLSGGQKQRIAIARAL 352
Cdd:cd03269   74 YLPEERGLYpKMKVIDQLVYLAQ-LKGLKKEEARRRID-----EWLERLELSeyANKRVEE----LSKGNQQKVQFIAAV 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304 353 LKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYG 417
Cdd:cd03269  144 IHDPELLILDEPFSGLDPVNVELLKDVIRELARaGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
195-420 1.00e-20

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 92.59  E-value: 1.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlNPV-----W 269
Cdd:PRK13536  41 AIDLAGVSKSYGDKAVV---NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG------VPVpararL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 270 LRSKIGTVSQEPIL-FSCSIAEN-IAYGAddPSSVTAEEIQRVaeVANAVAFIRnFPQGFNTVVGEkgvlLSGGQKQRIA 347
Cdd:PRK13536 112 ARARIGVVPQFDNLdLEFTVRENlLVFGR--YFGMSTREIEAV--IPSLLEFAR-LESKADARVSD----LSGGMKRRLT 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 348 IARALLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQG-KITEYGKHE 420
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPHA 258
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 196-434 1.02e-20

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 92.46  E-value: 1.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKN--VHF------AYPARPEVPI--FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQL 265
Cdd:PRK15079   9 LEVADlkVHFdikdgkQWFWQPPKTLkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 266 NPV-WL--RSKIGTVSQEPiLFSC----SIAENIAygadDP-----SSVTAEEI-QRVAEVANAVAFIRN----FPQGFn 328
Cdd:PRK15079  89 KDDeWRavRSDIQMIFQDP-LASLnprmTIGEIIA----EPlrtyhPKLSRQEVkDRVKAMMLKVGLLPNlinrYPHEF- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 329 tvvgekgvllSGGQKQRIAIARALLKNPKILLLDEATSALD----AENEYLVQEaLDRLMdGRTVLVIAHRLSTIKN-AN 403
Cdd:PRK15079 163 ----------SGGQCQRIGIARALILEPKLIICDEPVSALDvsiqAQVVNLLQQ-LQREM-GLSLIFIAHDLAVVKHiSD 230

                        250       260       270
                 ....*....|....*....|....*....|..
gi 767912304 404 MVAVLDQGKITEYGKHEELLSKPNGIYRK-LM 434
Cdd:PRK15079 231 RVLVMYLGHAVELGTYDEVYHNPLHPYTKaLM 262
cbiO PRK13645
energy-coupling factor transporter ATPase;
191-436 1.24e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 91.61  E-value: 1.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 191 SFQGALEFKNVHFAYPARP--EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASG-TISLD---GHDIRQ 264
Cdd:PRK13645   2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDyaiPANLKK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 265 LNPVW-LRSKIGTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNFpqgfntvVGEKGVLLSGG 341
Cdd:PRK13645  82 IKEVKrLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDY-------VKRSPFELSGG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 342 QKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYG- 417
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGs 234

                        250       260
                 ....*....|....*....|....*...
gi 767912304 418 -----KHEELLSK----PNGIYrKLMNK 436
Cdd:PRK13645 235 pfeifSNQELLTKieidPPKLY-QLMYK 261
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 216-422 1.38e-20

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 91.71  E-value: 1.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 216 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNpvwlRSKIGTVSQEPILF-SCSIAENIAY 294
Cdd:COG4152   19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMKVGEQLVY 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 295 -----GaddpssVTAEEIQR----------VAEVANAvafirnfpqgfntVVGEkgvlLSGGQKQRIAIARALLKNPKIL 359
Cdd:COG4152   95 larlkG------LSKAEAKRradewlerlgLGDRANK-------------KVEE----LSKGNQQKVQLIAALLHDPELL 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912304 360 LLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEEL 422
Cdd:COG4152  152 ILDEPFSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
 12-178 1.70e-20

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: 91.74  E-value: 1.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18578  150 FVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKK 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWE 171
Cdd:cd18578  230 GLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFR 309


                 ....*..
gi 767912304 172 LLEREPK 178
Cdd:cd18578  310 LLDRKPE 316
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 207-394 2.04e-20

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 88.78  E-value: 2.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 207 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTvsQEPILFSC 286
Cdd:PRK13539  11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGH--RNAMKPAL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 287 SIAENIA-----YGADDPSsvtaeeiqrVAEVANAVAF--IRNFPQGFntvvgekgvlLSGGQKQRIAIARALLKNPKIL 359
Cdd:PRK13539  89 TVAENLEfwaafLGGEELD---------IAAALEAVGLapLAHLPFGY----------LSAGQKRRVALARLLVSNRPIW 149

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767912304 360 LLDEATSALDAENEYLVQEAL-DRLMDGRTVLVIAH 394
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIrAHLAQGGIVIAATH 185
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 210-434 2.24e-20

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 93.77  E-value: 2.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 210 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI-----RQLNPvwLRSKIGTVSQEPILf 284
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspGKLQA--LRRDIQFIFQDPYA- 412

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 285 SCSIAENIAYGADDPSSVTA-----EEIQRVAEVANAVAFIRN----FPQGFntvvgekgvllSGGQKQRIAIARALLKN 355
Cdd:PRK10261 413 SLDPRQTVGDSIMEPLRVHGllpgkAAAARVAWLLERVGLLPEhawrYPHEF-----------SGGQRQRICIARALALN 481

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 356 PKILLLDEATSALDAE-NEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPNGIY-R 431
Cdd:PRK10261 482 PKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENPQHPYtR 561


                 ...
gi 767912304 432 KLM 434
Cdd:PRK10261 562 KLM 564
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 196-420 2.59e-20

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 89.74  E-value: 2.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHfaypARPE-VPIFQDFSLSIPSGSVTALVGPSGSGKSTvLSLLL---RLYDPASGTISLDGHDIRQLnPVWLR 271
Cdd:COG0396    1 LEIKNLH----VSVEgKEILKGVNLTIKPGEVHAIMGPNGSGKST-LAKVLmghPKYEVTSGSILLDGEDILEL-SPDER 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 272 SK--IGTVSQEPILFS-CSIAE--NIAYGADDPSSVTAEE-IQRVAEVANAVafirNFPQGF-----NtvVGekgvlLSG 340
Cdd:COG0396   75 ARagIFLAFQYPVEIPgVSVSNflRTALNARRGEELSAREfLKLLKEKMKEL----GLDEDFldryvN--EG-----FSG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 341 GQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAH--RLSTIKNANMVAVLDQGKITEYG 417
Cdd:COG0396  144 GEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSG 223


                 ...
gi 767912304 418 KHE 420
Cdd:COG0396  224 GKE 226
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
 15-165 2.86e-20

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: 90.61  E-value: 2.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  15 SPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARK 94
Cdd:cd18589  135 SPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKK 214

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912304  95 EAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGA 165
Cdd:cd18589  215 EAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGS 285
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 214-413 3.62e-20

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: 87.49  E-value: 3.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 214 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP-VWLRSKIGTVSQEP----ILFSCSI 288
Cdd:cd03215   16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLSV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 289 AENIAYGaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgVLLSGGQKQRIAIARALLKNPKILLLDEATSAL 368
Cdd:cd03215   96 AENIALS----------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767912304 369 DAENEYLVQEALDRLMD-GRTVLVIahrlST-----IKNANMVAVLDQGKI 413
Cdd:cd03215  136 DVGAKAEIYRLIRELADaGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 196-424 4.00e-20

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 89.18  E-value: 4.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRSK-- 273
Cdd:PRK10895   4 LTAKNLAKAYKGRRVV---EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL-PLHARARrg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQ-RVAEVANA--VAFIRNfpqgfntvvgEKGVLLSGGQKQRIAIA 349
Cdd:PRK10895  80 IGYLPQEASIFRrLSVYDNLMAVLQIRDDLSAEQREdRANELMEEfhIEHLRD----------SMGQSLSGGERRRVEIA 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304 350 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRL-STIKNANMVAVLDQGKITEYGKHEELLS 424
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 215-394 4.26e-20

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: 88.68  E-value: 4.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  215 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLrskigTVSQEPILFS-CSIAENIA 293
Cdd:TIGR01184   2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENIA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  294 YgADDPSSVTAEEIQRVAEVANAVAFIrnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENE 373
Cdd:TIGR01184  77 L-AVDRVLPDLSKSERRAIVEEHIALV-----GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150

                         170       180
                  ....*....|....*....|...
gi 767912304  374 YLVQEALDRLMD--GRTVLVIAH 394
Cdd:TIGR01184 151 GNLQEELMQIWEehRVTVLMVTH 173
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 196-413 5.74e-20

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 88.97  E-value: 5.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTIsLDG----HDIRQlnpvwlr 271
Cdd:PRK11247  13 LLLNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGtaplAEARE------- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 272 sKIGTVSQEPILFSC-SIAENIAYGaddpssVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIAR 350
Cdd:PRK11247  82 -DTRLMFQDARLLPWkKVIDNVGLG------LKGQWRDAALQALAAV--------GLADRANEWPAALSGGQKQRVALAR 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 351 ALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGKI 413
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
196-421 6.06e-20

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 88.01  E-value: 6.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPEVPIFQDFSLSipSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV---WLRS 272
Cdd:PRK10908   2 IRFEHVSKAYLGGRQALQGVTFHMR--PGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 273 KIGTVSQEP-ILFSCSIAENIAYgaddP---SSVTAEEIQR-VAEVANAVAFI---RNFPqgfntvvgekgVLLSGGQKQ 344
Cdd:PRK10908  80 QIGMIFQDHhLLMDRTVYDNVAI----PliiAGASGDDIRRrVSAALDKVGLLdkaKNFP-----------IQLSGGEQQ 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 345 RIAIARALLKNPKILLLDEATSALDAEneylVQEALDRLMD-----GRTVLVIAHRLSTIKNANM-VAVLDQGKITEyGK 418
Cdd:PRK10908 145 RVGIARAVVNKPAVLLADEPTGNLDDA----LSEGILRLFEefnrvGVTVLMATHDIGLISRRSYrMLTLSDGHLHG-GV 219


                 ...
gi 767912304 419 HEE 421
Cdd:PRK10908 220 GGE 222
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 196-409 6.96e-20

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: 86.44  E-value: 6.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPArpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHdirqlnpvwlrSKIG 275
Cdd:cd03223    1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDLL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEPILFSCSIAENIAYGADDpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvLLSGGQKQRIAIARALLKN 355
Cdd:cd03223   68 FLPQRPYLPLGTLREQLIYPWDD--------------------------------------VLSGGEQQRLAFARLLLHK 109

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767912304 356 PKILLLDEATSALDAENE-YLVQEALDRLMdgrTVLVIAHRLSTIKNANMVAVLD 409
Cdd:cd03223  110 PKFVFLDEATSALDEESEdRLYQLLKELGI---TVISVGHRPSLWKFHDRVLDLD 161
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
 12-145 7.24e-20

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: 89.41  E-value: 7.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18542  135 FSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDL 214

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWV 145
Cdd:cd18542  215 NIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWML 268
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
213-397 1.62e-19

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 87.18  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 213 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQL---NPVWLRS-KIGTVSQ-EPILFSCS 287
Cdd:PRK11629  24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNqKLGFIYQfHHLLPDFT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 288 IAENIAYGADDPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSA 367
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767912304 368 LDAENEYLVQEALDRL--MDGRTVLVIAHRLS 397
Cdd:PRK11629 176 LDARNADSIFQLLGELnrLQGTAFLVVTHDLQ 207
cbiO PRK13646
energy-coupling factor transporter ATPase;
196-427 1.70e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 88.30  E-value: 1.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAY-PARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI------RQLNP 267
Cdd:PRK13646   3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkdKYIRP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 268 VwlRSKIGTVSQ--EPILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNfpqgfntVVGEKGVLLSGGQKQR 345
Cdd:PRK13646  83 V--RKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRD-------VMSQSPFQMSGGQMRK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 346 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEEL 422
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233


                 ....*
gi 767912304 423 LSKPN 427
Cdd:PRK13646 234 FKDKK 238
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
199-423 2.05e-19

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 87.54  E-value: 2.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 199 KNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVS 278
Cdd:PRK10575  15 RNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 279 QE-PILFSCSIAENIA------YGAddPSSVTAEEIQRVAEvanAVAFIRNFPQGFNTVVGekgvlLSGGQKQRIAIARA 351
Cdd:PRK10575  92 QQlPAAEGMTVRELVAigrypwHGA--LGRFGAADREKVEE---AISLVGLKPLAHRLVDS-----LSGGERQRAWIAML 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912304 352 LLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAhrlsTIKNANMVA-------VLDQGKITEYGKHEELL 423
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA----VLHDINMAArycdylvALRGGEMIAQGTPAELM 236
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 196-427 2.48e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 87.55  E-value: 2.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYpaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 275
Cdd:PRK13652   4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALL 353
Cdd:PRK13652  82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML--------GLEELRDRVPHHLSGGEKKRVAIAGVIA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 354 KNPKILLLDEATSALDAENeylVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPN 427
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQG---VKELIDFLNDlpetyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD 230
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 210-395 4.03e-19

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 85.78  E-value: 4.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 210 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLY--DPASGTISLDGHDIrqlnpvwlrskigtvSQEpilfsCS 287
Cdd:COG2401   42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE-----AS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 288 IAENIaygADDPSSVTAEEIQRVAEVANAVAFIRNFPQgfntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSA 367
Cdd:COG2401  102 LIDAI---GRKGDFKDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSH 166

                        170       180       190
                 ....*....|....*....|....*....|
gi 767912304 368 LDAENEYLVQEALDRLMD--GRTVLVIAHR 395
Cdd:COG2401  167 LDRQTAKRVARNLQKLARraGITLVVATHH 196
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
212-431 5.62e-19

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 86.60  E-value: 5.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 212 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH--DIRQLNPVWLRSKIGTVSQEP--ILFSCS 287
Cdd:PRK13638  15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFYTD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 288 IAENIAYGADDPSSVTAEEIQRVAEVANAVAfirnfPQGFNTvvgEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSA 367
Cdd:PRK13638  95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVD-----AQHFRH---QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 368 LDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPNGIYR 431
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTEAMEQ 232
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
219-413 7.57e-19

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 85.83  E-value: 7.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 219 LSIPSGSVTALVGPSGSGKSTVLSLLLRLY--DPASGT-ISLDGH----------DIRQLnpvwlRSKIGTVSQEPILFS 285
Cdd:PRK09984  25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRtvqregrlarDIRKS-----RANTGYIFQQFNLVN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 286 -CSIAENIAYGA--DDP------SSVTAEEIQRVAEVANAVAFIRNFPQGFNTvvgekgvlLSGGQKQRIAIARALLKNP 356
Cdd:PRK09984 100 rLSVLENVLIGAlgSTPfwrtcfSWFTREQKQRALQALTRVGMVHFAHQRVST--------LSGGQQQRVAIARALMQQA 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 357 KILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGKI 413
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDyALRYCERIVALRQGHV 231
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
195-370 1.19e-18

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 86.82  E-value: 1.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKNVHFAYPARpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSkI 274
Cdd:PRK11650   3 GLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-DRD-I 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 275 GTVSQEPILFS-CSIAENIAYGADDpSSVTAEEI-QRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIAIA 349
Cdd:PRK11650  79 AMVFQNYALYPhMSVRENMAYGLKI-RGMPKAEIeERVAEAARILelePLLDRKPRE-----------LSGGQRQRVAMG 146

                        170       180
                 ....*....|....*....|.
gi 767912304 350 RALLKNPKILLLDEATSALDA 370
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDA 167
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
 12-141 1.40e-18

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


Pssm-ID: 349985 [Multi-domain]  Cd Length: 293  Bit Score: 85.54  E-value: 1.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18541  136 FTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEK 215

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 141
Cdd:cd18541  216 NLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSY 265
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 217-427 2.25e-18

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 84.12  E-value: 2.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 217 FSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYdPASGTISLDGHDIRQLNPVWLRSKIGTVSQE-PILFSCSIAENIAYG 295
Cdd:COG4138   15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQYLALH 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 296 AdDPSSVTAEEIQRVAEVANAVAFI----RNFPQgfntvvgekgvlLSGGQKQRIAIARALLK-----NP--KILLLDEA 364
Cdd:COG4138   94 Q-PAGASSEAVEQLLAQLAEALGLEdklsRPLTQ------------LSGGEWQRVRLAAVLLQvwptiNPegQLLLLDEP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 365 TSALD-AEneylvQEALDRLMD-----GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKPN 427
Cdd:COG4138  161 MNSLDvAQ-----QAALDRLLRelcqqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMTPEN 225
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 196-424 3.58e-18

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 84.75  E-value: 3.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARP--EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISL---DGHDIRQLNPVW- 269
Cdd:PRK13651   3 IKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEk 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 270 --------------------LRSKIGTVSQ--EPILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNFPQG- 326
Cdd:PRK13651  83 vleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRs 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 327 -FNtvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRL-STIKNAN 403
Cdd:PRK13651 163 pFE---------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLdNVLEWTK 233

                        250       260
                 ....*....|....*....|.
gi 767912304 404 MVAVLDQGKITEYGKHEELLS 424
Cdd:PRK13651 234 RTIFFKDGKIIKDGDTYDILS 254
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 190-422 4.01e-18

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 86.78  E-value: 4.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 190 KSFQgALEFKNVHFAYPARPEVPIFQ--DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP 267
Cdd:COG4615  323 ADFQ-TLELRGVTYRYPGEDGDEGFTlgPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNR 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 268 VWLRSKIGTVSQEPILFscsiaENIaYGADDPssVTAEEIQ---RVAEVANAVAFirnfpqgfntvvgEKGVL----LSG 340
Cdd:COG4615  402 EAYRQLFSAVFSDFHLF-----DRL-LGLDGE--ADPARARellERLELDHKVSV-------------EDGRFsttdLSQ 460

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 341 GQKQRIAIARALLKNPKILLLDEATSALDAEN-EYLVQEALDRLMD-GRTVLVIAH---------RLstIKnanmvavLD 409
Cdd:COG4615  461 GQRKRLALLVALLEDRPILVFDEWAADQDPEFrRVFYTELLPELKArGKTVIAISHddryfdladRV--LK-------MD 531

                        250
                 ....*....|...
gi 767912304 410 QGKITEYGKHEEL 422
Cdd:COG4615  532 YGKLVELTGPAAL 544
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 196-422 8.24e-18

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 85.49  E-value: 8.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSKIG 275
Cdd:PRK15439  12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 T--VSQEPILF-SCSIAENIAYGADDPSSVTAEEIQRVAEVanavafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARAL 352
Cdd:PRK15439  88 IylVPQEPLLFpNLSVKENILFGLPKRQASMQKMKQLLAAL------------GCQLDLDSSAGSLEVADRQIVEILRGL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912304 353 LKNPKILLLDEATSALD-AENEYLVQEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEEL 422
Cdd:PRK15439 156 MRDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
209-400 8.84e-18

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 85.61  E-value: 8.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 209 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP-VWLRSKIGTVSQE-PILFSC 286
Cdd:PRK09700  16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHkLAAQLGIGIIYQElSVIDEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 287 SIAENIAYGADDPSSVTAEEI---QRVAEVANAVAFIRNFPQGFNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDE 363
Cdd:PRK09700  96 TVLENLYIGRHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDE 171

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767912304 364 ATSAL-DAENEYLVQeALDRLM-DGRTVLVIAHRLSTIK 400
Cdd:PRK09700 172 PTSSLtNKEVDYLFL-IMNQLRkEGTAIVYISHKLAEIR 209
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 217-427 1.19e-17

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 81.90  E-value: 1.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 217 FSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYdPASGTISLDGHDIRQLNPVWLRSKIGTVSQE-PILFSCSIAENIA-Y 294
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLTlH 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 295 GADdpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTvvgekgvlLSGGQKQRIAIARALLK-----NP--KILLLDEATSA 367
Cdd:PRK03695  94 QPD--KTRTEAVASALNEVAEALGLDDKLGRSVNQ--------LSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNS 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 368 LDAENeylvQEALDRLMD-----GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKPN 427
Cdd:PRK03695 164 LDVAQ----QAALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 216-435 1.45e-17

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 84.76  E-value: 1.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 216 DFSLSIPSGSVTALVGPSGSGKS-TVLSLLLRLYDPA----SGTISLDGHDIRQLNPVWLR----SKIGTVSQEPILfSC 286
Cdd:PRK15134  27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMV-SL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 287 SIAENIAYGADDPSSV---------TAEEIQ---RVAeVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLK 354
Cdd:PRK15134 106 NPLHTLEKQLYEVLSLhrgmrreaaRGEILNcldRVG-IRQAAKRLTDYPHQ-----------LSGGERQRVMIAMALLT 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 355 NPKILLLDEATSALD----AENEYLVQEALDRLmdGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPNGI 429
Cdd:PRK15134 174 RPELLIADEPTTALDvsvqAQILQLLRELQQEL--NMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAPTHP 251


                 ....*..
gi 767912304 430 Y-RKLMN 435
Cdd:PRK15134 252 YtQKLLN 258
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 202-414 1.52e-17

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


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 81.61  E-value: 1.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 202 HFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHD--IRQLNpvwLRSKIGTV-- 277
Cdd:cd03267   25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwKRRKK---FLRRIGVVfg 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 278 SQEPILFSCSIAENIA-----YGADDpssvtAEEIQRVAEVANAVafirNFPQGFNTVVGEkgvlLSGGQKQRIAIARAL 352
Cdd:cd03267  102 QKTQLWWDLPVIDSFYllaaiYDLPP-----ARFKKRLDELSELL----DLEELLDTPVRQ----LSLGQRMRAEIAAAL 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912304 353 LKNPKILLLDEATSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTI-KNANMVAVLDQGKIT 414
Cdd:cd03267  169 LHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRLL 233
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 209-426 1.73e-17

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 81.67  E-value: 1.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 209 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA----SGTISLDGhdiRQLNPVWLRSK-IGTVSQEP-- 281
Cdd:PRK10418  14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDG---KPVAPCALRGRkIATIMQNPrs 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 282 ------ILFSCSIAENIAYGADDPSSVTAEEIQRVAeVANAVAFIRNFPqgFNtvvgekgvlLSGGQKQRIAIARALLKN 355
Cdd:PRK10418  91 afnplhTMHTHARETCLALGKPADDATLTAALEAVG-LENAARVLKLYP--FE---------MSGGMLQRMMIALALLCE 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912304 356 PKILLLDEATSALDAENEYLVQEALDRLMDGRT--VLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNAP 232
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 208-424 2.43e-17

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 84.33  E-value: 2.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  208 RPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLrLYDPA----SGTISLDGHDIrqlNPVWLRSKIGTVSQEPIL 283
Cdd:TIGR00955  35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  284 F-SCSIAENIAYGAD--DPSSVTAEE-IQRVAEVANAVAFIRnfpqGFNTVVGEKGVL--LSGGQKQRIAIARALLKNPK 357
Cdd:TIGR00955 111 IpTLTVREHLMFQAHlrMPRRVTKKEkRERVDEVLQALGLRK----CANTRIGVPGRVkgLSGGERKRLAFASELLTDPP 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  358 ILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLST--IKNANMVAVLDQGKITEYGKHEELLS 424
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
193-399 2.78e-17

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 83.81  E-value: 2.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 193 QGALEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLR 271
Cdd:PRK11288   2 SPYLSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 272 SKIGTVSQE----PILfscSIAENI-------AYGADDPSSVTAEEIQRVAEVANAVAfirnfPqgfNTVVGEkgvlLSG 340
Cdd:PRK11288  79 AGVAIIYQElhlvPEM---TVAENLylgqlphKGGIVNRRLLNYEAREQLEHLGVDID-----P---DTPLKY----LSI 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912304 341 GQKQRIAIARALLKNPKILLLDEATSALDA-ENEYLVQeALDRLMD-GRTVLVIAHRLSTI 399
Cdd:PRK11288 144 GQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLFR-VIRELRAeGRVILYVSHRMEEI 203
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 207-371 4.42e-17

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: 79.32  E-value: 4.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  207 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSC 286
Cdd:TIGR01189   9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  287 SIAENIAYGADDPSSVtaeeiQRVAEVANAVAFIRNFPQgfnTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATS 366
Cdd:TIGR01189  89 SALENLHFWAAIHGGA-----QRTIEDALAAVGLTGFED---LPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTT 156


                  ....*
gi 767912304  367 ALDAE 371
Cdd:TIGR01189 157 ALDKA 161
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
214-414 1.52e-16

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 81.60  E-value: 1.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 214 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLRSKIGTVS----QEPILFSCSI 288
Cdd:COG1129  268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdAIRAGIAYVPedrkGEGLVLDLSI 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 289 AENIAYGADDPSSvTAEEIQRVAEVANAVAFIRNF---PQGFNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEAT 365
Cdd:COG1129  348 RENITLASLDRLS-RGGLLDRRRERALAEEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPT 422

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912304 366 SALD--AENEylVQEALDRLMD-GRTVLVI----------AHRlstiknanmVAVLDQGKIT 414
Cdd:COG1129  423 RGIDvgAKAE--IYRLIRELAAeGKAVIVIsselpellglSDR---------ILVMREGRIV 473
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 196-416 1.72e-16

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: 77.28  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYP-ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA--SGTISLDGhdiRQLNPVWLRS 272
Cdd:cd03232    4 LTWKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILING---RPLDKNFQRS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 273 kIGTVSQEPILFSCSiaeniaygaddpssvTAEEIQRVAevanavAFIRNfpqgfntvvgekgvlLSGGQKQRIAIARAL 352
Cdd:cd03232   81 -TGYVEQQDVHSPNL---------------TVREALRFS------ALLRG---------------LSVEQRKRLTIGVEL 123

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304 353 LKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLS--TIKNANMVAVLDQGKITEY 416
Cdd:cd03232  124 AAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADsGQAILCTIHQPSasIFEKFDRLLLLKRGGKTVY 190
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 207-380 2.58e-16

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: 77.15  E-value: 2.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 207 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSC 286
Cdd:cd03231    9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 287 SIAENIAYGADDPSSVTAEEIqrVAEVanavafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATS 366
Cdd:cd03231   89 SVLENLRFWHADHSDEQVEEA--LARV------------GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154

                        170
                 ....*....|....
gi 767912304 367 ALDAENEYLVQEAL 380
Cdd:cd03231  155 ALDKAGVARFAEAM 168
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
196-435 2.89e-16

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 78.65  E-value: 2.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAypaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---RS 272
Cdd:PRK11831   8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 273 KIGTVSQEPILFS-CSIAENIAYgaddPssvTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARA 351
Cdd:PRK11831  85 RMSMLFQSGALFTdMNVFDNVAY----P---LREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 352 LLKNPKILLLDEATSALDAeneyLVQEALDRLMD------GRTVLVIAHR----LSTIKNANMVAvlDQgKITEYGKHEE 421
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDP----ITMGVLVKLISelnsalGVTCVVVSHDvpevLSIADHAYIVA--DK-KIVAHGSAQA 230

                        250
                 ....*....|....
gi 767912304 422 LLSKPNGIYRKLMN 435
Cdd:PRK11831 231 LQANPDPRVRQFLD 244
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 212-438 3.43e-16

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: 81.60  E-value: 3.43e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   212 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIrQLNPVWLRSKIGTVSQEPILFS-CSIAE 290
Cdd:TIGR01257  944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAE 1022

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   291 NIAYGADDPSSvTAEEIQRVAEvanavAFIRNfpQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDA 370
Cdd:TIGR01257 1023 HILFYAQLKGR-SWEEAQLEME-----AMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304   371 ENEYLVQEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKIteYGKHEELLSKP---NGIY----RKLMNKQS 438
Cdd:TIGR01257 1095 YSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRL--YCSGTPLFLKNcfgTGFYltlvRKMKNIQS 1168
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 167-414 5.67e-16

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 79.69  E-value: 5.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 167 GRlwELLEREPKLPFNEGVILneksfqgaLEFKNVHfaYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLR 246
Cdd:COG3845  239 GR--EVLLRVEKAPAEPGEVV--------LEVENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAG 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 247 LYDPASGTISLDGHDIRQLNPVWLR-SKIGTVSQEPILFSC----SIAENIAYGA-DDPSSVTAEEIQRVAEVANAVAFI 320
Cdd:COG3845  307 LRPPASGSIRLDGEDITGLSPRERRrLGVAYIPEDRLGRGLvpdmSVAENLILGRyRRPPFSRGGFLDRKAIRAFAEELI 386

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 321 RNF---PQGFNTVVGekgvLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVI---- 392
Cdd:COG3845  387 EEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDaGAAVLLIsedl 462

                        250       260
                 ....*....|....*....|....*...
gi 767912304 393 ------AHRlstiknanmVAVLDQGKIT 414
Cdd:COG3845  463 deilalSDR---------IAVMYEGRIV 481
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
196-418 8.47e-16

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 76.46  E-value: 8.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlnpvW-----L 270
Cdd:PRK11614   6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD----WqtakiM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 271 RSKIGTVSQEPILFS-CSIAENIAYG---ADdpSSVTAEEIQRVAEVanavafirnFPQGFNTVVGEKGVLlSGGQKQRI 346
Cdd:PRK11614  79 REAVAIVPEGRRVFSrMTVEENLAMGgffAE--RDQFQERIKWVYEL---------FPRLHERRIQRAGTM-SGGEQQML 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304 347 AIARALLKNPKILLLDEATSALDAeneYLVQEALDRLM----DGRTVLVIAhrlstiKNANMVAVL-DQGKITEYGK 418
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAP---IIIQQIFDTIEqlreQGMTIFLVE------QNANQALKLaDRGYVLENGH 214
PLN03211 PLN03211
ABC transporter G-25; Provisional
 224-424 1.28e-15

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 79.15  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 224 GSVTALVGPSGSGKSTVLSLLL-RLYDPA-SGTISLDGhdiRQLNPVWLRsKIGTVSQEPILFS-CSIAENIAYGA--DD 298
Cdd:PLN03211  94 GEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RKPTKQILK-RTGFVTQDDILYPhLTVRETLVFCSllRL 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 299 PSSVTAEEIQRVAEvanAVAFIRNFPQGFNTVVGEKGVL-LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEY-LV 376
Cdd:PLN03211 170 PKSLTKQEKILVAE---SVISELGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYrLV 246

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767912304 377 QEALDRLMDGRTVLVIAHRLST--IKNANMVAVLDQGKITEYGKHEELLS 424
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 214-434 1.77e-15

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 76.12  E-value: 1.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 214 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDiRQLNPVW----------LRSKIGTVSQEP-- 281
Cdd:PRK11701  22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD-GQLRDLYalseaerrrlLRTEWGFVHQHPrd 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 282 -ILFSCSIAENI-----AYGADDPSSVTAEEIQRVAEVANAVAFIRNFPQGFntvvgekgvllSGGQKQRIAIARALLKN 355
Cdd:PRK11701 101 gLRMQVSAGGNIgerlmAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTF-----------SGGMQQRLQIARNLVTH 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 356 PKILLLDEATSALDAEneylVQEaldRLMD---------GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSK 425
Cdd:PRK11701 170 PRLVFMDEPTGGLDVS----VQA---RLLDllrglvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVLDD 242


                 ....*....
gi 767912304 426 PNGIYRKLM 434
Cdd:PRK11701 243 PQHPYTQLL 251
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 200-432 8.39e-15

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 76.43  E-value: 8.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 200 NVHFaYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP--VWLRSK---- 273
Cdd:PRK10261  19 NIAF-MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRqvIELSEQsaaq 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 --------IGTVSQEPI-----LFScsIAENIAYGADDPSSVTAEEiqRVAEVANAVAFIRnFPQGfNTVVGEKGVLLSG 340
Cdd:PRK10261  98 mrhvrgadMAMIFQEPMtslnpVFT--VGEQIAESIRLHQGASREE--AMVEAKRMLDQVR-IPEA-QTILSRYPHQLSG 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 341 GQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRT--VLVIAHRLSTIKN-ANMVAVLDQGKITEYG 417
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETG 251

                        250
                 ....*....|....*
gi 767912304 418 KHEELLSKPNGIYRK 432
Cdd:PRK10261 252 SVEQIFHAPQHPYTR 266
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
214-427 1.28e-14

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 73.76  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 214 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlnpVWLRSKIGTVSQ-EPILFSCSI-AEN 291
Cdd:PRK15056  23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLVAYVPQsEEVDWSFPVlVED 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 292 IA----YGADDPSSVTAEEIQRVAEVANAVAFIRNFPqgfNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATSA 367
Cdd:PRK15056 100 VVmmgrYGHMGWLRRAKKRDRQIVTAALARVDMVEFR---HRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTG 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912304 368 LDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPN 427
Cdd:PRK15056 173 VDVKTEARIISLLRELRDeGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAEN 233
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
 12-158 1.61e-14

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


Pssm-ID: 349987 [Multi-domain]  Cd Length: 291  Bit Score: 73.67  E-value: 1.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18543  134 LVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRAT 213

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAF---WVGISIGGLSSFYSE 158
Cdd:cd18543  214 RLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTmlvWPVRMLGWLLAMAQR 283
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 196-417 2.26e-14

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 72.75  E-value: 2.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLL--RLYDPASGTISLDGHDIRQLNPVwLRSK 273
Cdd:CHL00131   8 LEIKNLHASVN---ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEPE-ERAH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGT------------VSQEPILFSCSIAENIAYGADDPSSVTAEEI--QRVAEVANAVAFI-RNFPQGFntvvgekgvll 338
Cdd:CHL00131  84 LGIflafqypieipgVSNADFLRLAYNSKRKFQGLPELDPLEFLEIinEKLKLVGMDPSFLsRNVNEGF----------- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 339 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAH--RLSTIKNANMVAVLDQGKITE 415
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTsENSIILITHyqRLLDYIKPDYVHVMQNGKIIK 232


                 ..
gi 767912304 416 YG 417
Cdd:CHL00131 233 TG 234
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 223-409 2.66e-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: 2.66e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   223 SGSVTALVGPSGSGKSTVLSLLLRLYDPASGT-ISLDGHDIRQLNPVWLRskigtvsqepilfscsiaeniaygaddpss 301
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------ 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   302 vtaeeiqrvaevanavafirnfpqgfNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALD 381
Cdd:smart00382  51 --------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 767912304   382 RLMD-------GRTVLVIAHRLSTIKNANMVAVLD 409
Cdd:smart00382 105 LRLLlllksekNLTVILTTNDEKDLGPALLRRRFD 139
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
208-426 2.77e-14

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 72.51  E-value: 2.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 208 RPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILfSCS 287
Cdd:PRK15112  23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPST-SLN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 288 IAENIAYGADDP----SSVTAEEI-QRVAEVANAVAFIRN----FPQgfntvvgekgvLLSGGQKQRIAIARALLKNPKI 358
Cdd:PRK15112 102 PRQRISQILDFPlrlnTDLEPEQReKQIIETLRQVGLLPDhasyYPH-----------MLAPGQKQRLGLARALILRPKV 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912304 359 LLLDEATSALDAEneylVQEALDRLM------DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKP 426
Cdd:PRK15112 171 IIADEALASLDMS----MRSQLINLMlelqekQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASP 241
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 218-429 5.66e-14

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 71.56  E-value: 5.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 218 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRSKIGTVS--QEPILF-SCSIAEN--I 292
Cdd:PRK11300  25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQIARMGVVRtfQHVRLFrEMTVIENllV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 293 AYGADDPSSVTA-------------EEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKIL 359
Cdd:PRK11300 104 AQHQQLKTGLFSgllktpafrraesEALDRAATWLERV--------GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912304 360 LLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPNGI 429
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPDVI 248
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
217-426 5.83e-14

ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 72.63  E-value: 5.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 217 FSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPaSGTIS-----LDGHDIRQLNPV----WLRSKIGTVSQEPIlfSCS 287
Cdd:COG4170   26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD-NWHVTadrfrWNGIDLLKLSPRerrkIIGREIAMIFQEPS--SCL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 288 iaeniaygadDPSSVTAEEIqrvAEVANAVAFIRNFPQGFNTV----------VG---EKGVL------LSGGQKQRIAI 348
Cdd:COG4170  103 ----------DPSAKIGDQL---IEAIPSWTFKGKWWQRFKWRkkraiellhrVGikdHKDIMnsypheLTEGECQKVMI 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 349 ARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSK 425
Cdd:COG4170  170 AMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnqLQGTSILLISHDLESISQwADTITVLYCGQTVESGPTEQILKS 249


                 .
gi 767912304 426 P 426
Cdd:COG4170  250 P 250
GguA NF040905
sugar ABC transporter ATP-binding protein;
209-415 7.68e-14

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 73.29  E-value: 7.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 209 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYdPA---SGTISLDG-----HDIRQLNpvwlRSKIGTVSQE 280
Cdd:NF040905  12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfKDIRDSE----ALGIVIIHQE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 281 ----PILfscSIAENI-------AYGADDPSSVTAEEIQRVAEVAnavafIRNFPQgfnTVVGEKGVllsgGQKQRIAIA 349
Cdd:NF040905  87 laliPYL---SIAENIflgneraKRGVIDWNETNRRARELLAKVG-----LDESPD---TLVTDIGV----GKQQLVEIA 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912304 350 RALLKNPKILLLDEATSAL-DAENEYLvqeaLDRLMD----GRTVLVIAHRLSTI-KNANMVAVLDQGKITE 415
Cdd:NF040905 152 KALSKDVKLLILDEPTAALnEEDSAAL----LDLLLElkaqGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 210-369 7.97e-14

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 70.58  E-value: 7.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 210 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP---VWLRSK-IGTVSQEPILFS 285
Cdd:PRK10584  22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRAKhVGFVFQSFMLIP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 286 CSIA-ENIAYgaddPSSVTAEEIQRVAEvaNAVAFIRNFpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEA 364
Cdd:PRK10584 102 TLNAlENVEL----PALLRGESSRQSRN--GAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173


                 ....*
gi 767912304 365 TSALD 369
Cdd:PRK10584 174 TGNLD 178
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 196-412 9.15e-14

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 73.04  E-value: 9.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYdPA---SGTISLDG-----HDIRQLNp 267
Cdd:PRK13549   6 LEMKNITKTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGeelqaSNIRDTE- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 268 vwlRSKIGTVSQEPILFS-CSIAENIAYGAD-------DPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEkgvlLS 339
Cdd:PRK13549  81 ---RAGIAIIHQELALVKeLSVLENIFLGNEitpggimDYDAMYLRAQKLLAQLKLDI--------NPATPVGN----LG 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912304 340 GGQKQRIAIARALLKNPKILLLDEATSAL-DAENEYLvqeaLDRLMD----GRTVLVIAHRLSTIKN-ANMVAVLDQGK 412
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLtESETAVL----LDIIRDlkahGIACIYISHKLNEVKAiSDTICVIRDGR 220
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 193-399 1.10e-13

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 72.73  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 193 QGALEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwlRS 272
Cdd:PRK10762   2 QALLQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGP---KS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 273 K----IGTVSQE-PILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEkgvlLSGGQKQRIA 347
Cdd:PRK10762  76 SqeagIGIIHQElNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVE 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 348 IARALLKNPKILLLDEATSAL-DAENEYL---VQEALDRlmdGRTVLVIAHRLSTI 399
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALtDTETESLfrvIRELKSQ---GRGIVYISHRLKEI 204
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 216-436 1.12e-13

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 70.51  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 216 DFSLSIPSGS-----VTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIrQLNPVWLRSKI-GTVSQepILFScsia 289
Cdd:cd03237   12 EFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKADYeGTVRD--LLSS---- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 290 eniaygaDDPSSVTAEEIQrvAEVANAVAFIRNFPQGFNTvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALD 369
Cdd:cd03237   85 -------ITKDFYTHPYFK--TEIAKPLQIEQILDREVPE--------LSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 370 AENEYLVQEALDRLMDG--RTVLVIAHRLSTIKN-ANMVAVLDqGKITEYGkheeLLSKPNGIyRKLMNK 436
Cdd:cd03237  148 VEQRLMASKVIRRFAENneKTAFVVEHDIIMIDYlADRLIVFE-GEPSVNG----VANPPQSL-RSGMNR 211
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 196-395 1.22e-13

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 69.59  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI--------RQLNP 267
Cdd:PRK13540   2 LDVIELDFDYH---DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdlctyqKQLCF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 268 VWLRSKIgtvsqEPILfscSIAENIAYgaDDPSSVTAEEIQRVAEVANAVAFIrNFPQGfntvvgekgvLLSGGQKQRIA 347
Cdd:PRK13540  79 VGHRSGI-----NPYL---TLRENCLY--DIHFSPGAVGITELCRLFSLEHLI-DYPCG----------LLSSGQKRQVA 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767912304 348 IARALLKNPKILLLDEATSALDAEN-EYLVQEALDRLMDGRTVLVIAHR 395
Cdd:PRK13540 138 LLRLWMSKAKLWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQ 186
hmuV PRK13547
heme ABC transporter ATP-binding protein;
200-417 1.60e-13

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 70.63  E-value: 1.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 200 NVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLL-RLYDPA-------SGTISLDGHDIRQLNPVWLR 271
Cdd:PRK13547   3 TADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 272 SKIGTVSQ--EPIlFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAvAFIRnfpQGFNTVVGEKGVLLSGGQKQRIAIA 349
Cdd:PRK13547  83 RLRAVLPQaaQPA-FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQ-ALAL---AGATALVGRDVTTLSGGELARVQFA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 350 RALLK---------NPKILLLDEATSALDAENEYLVQEALDRLM-DGRT-VLVIAHRLS-TIKNANMVAVLDQGKITEYG 417
Cdd:PRK13547 158 RVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHG 237
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 196-425 3.95e-13

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 71.16  E-value: 3.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARP-EV-PIfqdfSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSK 273
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVgPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGTVSQEPILFSCSIaeNIAYGADDPSSVTA--EEIQ---RVAEVANAVAFIRnfpqgfntvvgekgvlLSGGQKQRIAI 348
Cdd:PRK10522 399 FSAVFTDFHLFDQLL--GPEGKPANPALVEKwlERLKmahKLELEDGRISNLK----------------LSKGQKKRLAL 460

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 349 ARALLKNPKILLLDEATSALDAE-NEYLVQEALDRLMD-GRTVLVIAHRLSTIKNANMVAVLDQGKITE-YGKHEELLSK 425
Cdd:PRK10522 461 LLALAEERDILLLDEWAADQDPHfRREFYQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASR 540
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
 12-149 4.13e-13

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


Pssm-ID: 349992 [Multi-domain]  Cd Length: 292  Bit Score: 69.35  E-value: 4.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18548  135 FRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDT 214

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISI 149
Cdd:cd18548  215 SLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSL 272
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
 215-405 4.76e-13

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: 68.80  E-value: 4.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 215 QDFSLSIPSGSVTALVGPSGSGKSTVL------SLLLRLYdpASGTISLDGHDIRQLNPVwlrSKIGTVSQEPI------ 282
Cdd:cd03271   12 KNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLH--LKKEQPGNHDRIEGLEHI---DKVIVIDQSPIgrtprs 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 283 --------------LFsCSIAE----------------NIAygadDPSSVTAEEiqrvaevanAVAFIRNFPQGFNTV-- 330
Cdd:cd03271   87 npatytgvfdeireLF-CEVCKgkrynretlevrykgkSIA----DVLDMTVEE---------ALEFFENIPKIARKLqt 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 331 ----------VGEKGVLLSGGQKQRIAIARALLK---NPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRL 396
Cdd:cd03271  153 lcdvglgyikLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNL 232


                 ....*....
gi 767912304 397 STIKNANMV 405
Cdd:cd03271  233 DVIKCADWI 241
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
208-371 5.80e-13

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 67.52  E-value: 5.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 208 RPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS--KIGTVS------- 278
Cdd:PRK13538  11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllYLGHQPgiktelt 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 279 -QEPILFSCSIAENiaygADDpssvtaeeiqrvAEVANAVAfirnfpqgfntVVGEKGVL------LSGGQKQRIAIARA 351
Cdd:PRK13538  91 aLENLRFYQRLHGP----GDD------------EALWEALA-----------QVGLAGFEdvpvrqLSAGQQRRVALARL 143

                        170       180
                 ....*....|....*....|
gi 767912304 352 LLKNPKILLLDEATSALDAE 371
Cdd:PRK13538 144 WLTRAPLWILDEPFTAIDKQ 163
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 12-142 5.99e-13

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


Pssm-ID: 350007 [Multi-domain]  Cd Length: 296  Bit Score: 69.08  E-value: 5.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKL-TKVTQDSLAQATQLAEErIGNVRTVRAFGKEMTEIEKYASKVDHVMQ 90
Cdd:cd18563  139 FSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLfHRQWRRWSRLNSVLNDT-LPGIRVVKAFGQEKREIKRFDEANQELLD 217

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767912304  91 LARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA 142
Cdd:cd18563  218 ANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYL 269
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
 12-141 6.34e-13

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


Pssm-ID: 349990 [Multi-domain]  Cd Length: 292  Bit Score: 69.05  E-value: 6.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18546  135 LVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDA 214

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 141
Cdd:cd18546  215 RLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLY 264
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
 12-141 8.71e-13

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


Pssm-ID: 349993 [Multi-domain]  Cd Length: 295  Bit Score: 68.63  E-value: 8.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVmQL 91
Cdd:cd18549  138 LTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRF-LE 216

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767912304  92 ARKEAF-ARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 141
Cdd:cd18549  217 SKKKAYkAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLY 267
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 196-398 1.35e-12

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: 69.58  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  196 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLdGHDIrqlnpvwlrsKIG 275
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  276 TVSQ--EPILFSCSIAENIAYGADdpssvtaeeIQRVAEVA-NAVAFIRNFpqGFNTVVGEKGV-LLSGGQKQRIAIARA 351
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGGLD---------IIKLGKREiPSRAYVGRF--NFKGSDQQKKVgQLSGGERNRVHLAKT 457

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767912304  352 LLKNPKILLLDEATSALDAENEYLVQEALDRLmdGRTVLVIAH------RLST 398
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
 12-141 1.83e-12

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


Pssm-ID: 349988 [Multi-domain]  Cd Length: 294  Bit Score: 67.41  E-value: 1.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQA-TQLAEeRIGNVRTVRAFGKEMTEIEKYASKVDHVMQ 90
Cdd:cd18544  137 FLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLnAFLQE-SISGMSVIQLFNREKREFEEFDEINQEYRK 215

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767912304  91 LARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 141
Cdd:cd18544  216 ANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQY 266
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 198-370 1.93e-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: 66.13  E-value: 1.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 198 FKNVHF-AYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL---LRLYDPASGTISLDGHDIRqlnpvwlrsK 273
Cdd:cd03233    6 WRNISFtTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYK---------E 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 274 IGTVSQEPILFScsiaeniayGADD--PSSVTAEEIQRVAEVANAVAFIRnfpqgfntvvgekGVllSGGQKQRIAIARA 351
Cdd:cd03233   77 FAEKYPGEIIYV---------SEEDvhFPTLTVRETLDFALRCKGNEFVR-------------GI--SGGERKRVSIAEA 132

                        170
                 ....*....|....*....
gi 767912304 352 LLKNPKILLLDEATSALDA 370
Cdd:cd03233  133 LVSRASVLCWDNSTRGLDS 151
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 196-425 1.95e-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: 69.06  E-value: 1.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  196 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL--LRLYDPASGTISLDGHDIRQLNPVWLRSK 273
Cdd:TIGR03269   1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHVALCEKCGYVERPSK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  274 IGTvsqepilfSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNFP-QGFNTVV-------------GEKGVL-- 337
Cdd:TIGR03269  78 VGE--------PCPVCGGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFAlYGDDTVLdnvlealeeigyeGKEAVGra 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  338 -------------------LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRL 396
Cdd:TIGR03269 150 vdliemvqlshrithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWP 229

                         250       260       270
                  ....*....|....*....|....*....|
gi 767912304  397 STIKNANMVAV-LDQGKITEYGKHEELLSK 425
Cdd:TIGR03269 230 EVIEDLSDKAIwLENGEIKEEGTPDEVVAV 259
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 215-425 2.25e-12

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 67.80  E-value: 2.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 215 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRsKIGTV----SQ----EPILFSC 286
Cdd:COG4586   39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQlwwdLPAIDSF 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 287 SIAENIaYGADDpssvtAEEIQRVAEvanavafirnfpqgFNTVVGEKGVL------LSGGQKQRIAIARALLKNPKILL 360
Cdd:COG4586  118 RLLKAI-YRIPD-----AEYKKRLDE--------------LVELLDLGELLdtpvrqLSLGQRMRCELAAALLHRPKILF 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304 361 LDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSK 425
Cdd:COG4586  178 LDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 12-138 3.22e-12

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


Pssm-ID: 349994 [Multi-domain]  Cd Length: 294  Bit Score: 66.74  E-value: 3.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEER--IGNVRTVRAFGKEMTEIEKYASKVDHVM 89
Cdd:cd18550  135 LALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELR 214

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767912304  90 QLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSF 138
Cdd:cd18550  215 DLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAF 263
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
 12-168 3.41e-12

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


Pssm-ID: 349991 [Multi-domain]  Cd Length: 298  Bit Score: 66.66  E-value: 3.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18547  141 LYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKA 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  92 ARKeafarAGFFG-----ATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAG 166
Cdd:cd18547  221 SFK-----AQFYSgllmpIMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGA 295


                 ..
gi 767912304 167 GR 168
Cdd:cd18547  296 ER 297
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 209-418 4.40e-12

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 68.60  E-value: 4.40e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   209 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVL-SLLLRLYD---PASGTISLDGHDIRQLNPvWLRSKIGTVSQEPILF 284
Cdd:TIGR00956   72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTDGfhiGVEGVITYDGITPEEIKK-HYRGDVVYNAETDVHF 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   285 -SCSIAENIAYGA------DDPSSVTAEEiqRVAEVANAVAFIRNFPQGFNTVVGE---KGVllSGGQKQRIAIARALLK 354
Cdd:TIGR00956  151 pHLTVGETLDFAArcktpqNRPDGVSREE--YAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLG 226

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912304   355 NPKILLLDEATSALDAENEYLVQEALD---RLMDGrTVLVIAHRLS--TIKNANMVAVLDQGKITEYGK 418
Cdd:TIGR00956  227 GAKIQCWDNATRGLDSATALEFIRALKtsaNILDT-TPLVAIYQCSqdAYELFDKVIVLYEGYQIYFGP 294
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 204-394 6.08e-12

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: 67.27  E-value: 6.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  204 AYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTisldghdirqlnpVWLRS--KIGTVSQEP 281
Cdd:TIGR03719  13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE-------------ARPQPgiKVGYLPQEP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  282 IL-FSCSIAENIAYGADDpssvTAEEIQRVAEVANAVAfirNFPQGFNTVVGEKGVL----------------------- 337
Cdd:TIGR03719  78 QLdPTKTVRENVEEGVAE----IKDALDRFNEISAKYA---EPDADFDKLAAEQAELqeiidaadawdldsqleiamdal 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304  338 -----------LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLmDGrTVLVIAH 394
Cdd:TIGR03719 151 rcppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTH 216
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 216-430 8.77e-12

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 65.90  E-value: 8.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 216 DFSLSIPSGSVTALVGPSGSGKS-TVLSL--LLRLYDPASGTISLDGHDI-----RQLNPvwLRS-KIGTVSQEPIlfsC 286
Cdd:PRK09473  34 DLNFSLRAGETLGIVGESGSGKSqTAFALmgLLAANGRIGGSATFNGREIlnlpeKELNK--LRAeQISMIFQDPM---T 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 287 SIaeniaygadDPSSVTAEEIQRV----AEVANAVAF------------------IRNFPQGFntvvgekgvllSGGQKQ 344
Cdd:PRK09473 109 SL---------NPYMRVGEQLMEVlmlhKGMSKAEAFeesvrmldavkmpearkrMKMYPHEF-----------SGGMRQ 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 345 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEE 421
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARD 248


                 ....*....
gi 767912304 422 LLSKPNGIY 430
Cdd:PRK09473 249 VFYQPSHPY 257
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
 12-159 9.84e-12

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


Pssm-ID: 349989 [Multi-domain]  Cd Length: 293  Bit Score: 65.57  E-value: 9.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18545  136 FSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKA 215

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA--FWVGISigGLSSFYSEL 159
Cdd:cd18545  216 NMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVgrFWQPIR--NLSNFYNQL 283
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 218-424 1.66e-11

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: 65.98  E-value: 1.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  218 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISL----DGHDIRQLNPVwLRSK----IGTVSQEPILFS-CSI 288
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD-GRGRakryIGILHQEYDLYPhRTV 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  289 AENI--AYGADDPSsvtaeeiqrvaEVANAVAFIRNFPQGFNTVVGEKgVL------LSGGQKQRIAIARALLKNPKILL 360
Cdd:TIGR03269 383 LDNLteAIGLELPD-----------ELARMKAVITLKMVGFDEEKAEE-ILdkypdeLSEGERHRVALAQVLIKEPRIVI 450

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304  361 LDEATSALDAENEYLVQEAL--DRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLS 424
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 197-394 1.69e-11

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 66.13  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 197 EFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTIsldghdirqlnpvwlrsKIGT 276
Cdd:PRK11147 321 EMENVNYQIDGKQLV---KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----------------HCGT 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 277 vSQEPILFSC---------SIAENIAYGADDpssVTAEEIQRvaevaNAVAFIRNF---PQGFNTVVGEkgvlLSGGQKQ 344
Cdd:PRK11147 381 -KLEVAYFDQhraeldpekTVMDNLAEGKQE---VMVNGRPR-----HVLGYLQDFlfhPKRAMTPVKA----LSGGERN 447

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767912304 345 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRlMDGrTVLVIAH 394
Cdd:PRK11147 448 RLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDS-YQG-TVLLVSH 495
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 224-399 1.91e-11

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 66.29  E-value: 1.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   224 GSVTALVGPSGSGKSTVLSLLLRLYDPA---SGTISLDGhdiRQLNPVWLRSkIGTVSQEPI-LFSCSIAENIAYGA--D 297
Cdd:TIGR00956  789 GTLTALMGASGAGKTTLLNVLAERVTTGvitGGDRLVNG---RPLDSSFQRS-IGYVQQQDLhLPTSTVRESLRFSAylR 864

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   298 DPSSVTAEEIQRVAEvanAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILL-LDEATSALDAENEYLV 376
Cdd:TIGR00956  865 QPKSVSKSEKMEYVE---EVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSI 941

                          170       180
                   ....*....|....*....|....
gi 767912304   377 QEALDRLMD-GRTVLVIAHRLSTI 399
Cdd:TIGR00956  942 CKLMRKLADhGQAILCTIHQPSAI 965
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 199-396 1.99e-11

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 63.98  E-value: 1.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 199 KNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlnpvwlRSKIGTVS 278
Cdd:PRK09544   8 ENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYVP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 279 QEpILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAvAFIRNFPQgfntvvgEKgvlLSGGQKQRIAIARALLKNPKI 358
Cdd:PRK09544  74 QK-LYLDTTLPLTVNRFLRLRPGTKKEDILPALKRVQA-GHLIDAPM-------QK---LSGGETQRVLLARALLNRPQL 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767912304 359 LLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRL 396
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDL 181
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 164-409 2.21e-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: 65.93  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  164 GAGGRLWELLEREPKLPFNEGVIlneksfqgalEFKNVHFAYPARpEVPIfQDFSLSIPSGSVTALVGPSGSGKSTVLSL 243
Cdd:TIGR00954 430 REGGRNSNLVPGRGIVEYQDNGI----------KFENIPLVTPNG-DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRI 497

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  244 LLRLYDPASGTISLDGhdirqlnpvwlRSKIGTVSQEPILFSCSIAENIAYgaddPSSV---------TAEEIQRVAEVA 314
Cdd:TIGR00954 498 LGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQIIY----PDSSedmkrrglsDKDLEQILDNVQ 562

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  315 NAVAFIRNfpQGFNTVVGEKGVLlSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLmdGRTVLVIAH 394
Cdd:TIGR00954 563 LTHILERE--GGWSAVQDWMDVL-SGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSH 637

                         250
                  ....*....|....*
gi 767912304  395 RLSTIKNANMVAVLD 409
Cdd:TIGR00954 638 RKSLWKYHEYLLYMD 652
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 216-369 2.66e-11

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 65.41  E-value: 2.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 216 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLRSKIGTVSQEP----ILFSCSIAE 290
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISEDRkrdgLVLGMSVKE 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 291 NIAYGADDPSSVTAEEIQRVAEVANAVAFIRNF----PqGFNTVVGekgvLLSGGQKQRIAIARALLKNPKILLLDEATS 366
Cdd:PRK10762 350 NMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFniktP-SMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTR 424


                 ...
gi 767912304 367 ALD 369
Cdd:PRK10762 425 GVD 427
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 12-141 3.07e-11

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


Pssm-ID: 350008 [Multi-domain]  Cd Length: 307  Bit Score: 64.07  E-value: 3.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18564  150 FWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRA 229

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 141
Cdd:cd18564  230 GLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAY 279
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 204-371 7.23e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 63.98  E-value: 7.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 204 AYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTisldghdirqlnpVWLRS--KIGTVSQEP 281
Cdd:PRK11819  15 VVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-------------ARPAPgiKVGYLPQEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 282 IL-FSCSIAENIAYGADDpssvTAEEIQRVAEVANAVAfirNFPQGFNTVVGEKGVL----------------------- 337
Cdd:PRK11819  80 QLdPEKTVRENVEEGVAE----VKAALDRFNEIYAAYA---EPDADFDALAAEQGELqeiidaadawdldsqleiamdal 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767912304 338 -----------LSGGQKQRIAIARALLKNPKILLLDEATSALDAE 371
Cdd:PRK11819 153 rcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE 197
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
216-399 9.24e-11

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 63.67  E-value: 9.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 216 DFSLSIPSGS-----VTALVGPSGSGKSTVLSLLLRLYDPASGTISLDghdIR-QLNPVWLRSKI-GTVSQepilFSCSI 288
Cdd:PRK13409 352 DFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKiSYKPQYIKPDYdGTVED----LLRSI 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 289 AENIAygaddpSSVTAEEIQRvaevanavafirnfPQGFNTV----VGEkgvlLSGGQKQRIAIARALLKNPKILLLDEA 364
Cdd:PRK13409 425 TDDLG------SSYYKSEIIK--------------PLQLERLldknVKD----LSGGELQRVAIAACLSRDADLYLLDEP 480

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767912304 365 TSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTI 399
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI 517
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 196-419 2.07e-10

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 60.96  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLL--RLYDPASGTISLDGHDIRQLNP------ 267
Cdd:PRK09580   2 LSIKDLHVSVE---DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPedrage 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 268 -VWLR----SKIGTVSQEpILFSCSIAENIAYGADDP------SSVTAEEIQRVAEVANAVAfiRNFPQGFntvvgekgv 336
Cdd:PRK09580  79 gIFMAfqypVEIPGVSNQ-FFLQTALNAVRSYRGQEPldrfdfQDLMEEKIALLKMPEDLLT--RSVNVGF--------- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 337 llSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDG-RTVLVIAH--RLSTIKNANMVAVLDQGKI 413
Cdd:PRK09580 147 --SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRI 224


                 ....*.
gi 767912304 414 TEYGKH 419
Cdd:PRK09580 225 VKSGDF 230
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 214-399 2.35e-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: 62.49  E-value: 2.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 214 FQDFSLSIPSGS-----VTALVGPSGSGKSTVLSLLLRLYDPASGTISLDghdirqLN----PVWLRSKI-GTVSQepIL 283
Cdd:COG1245  351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------LKisykPQYISPDYdGTVEE--FL 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 284 FScsiaeniAYGADDPSSVTAEEIQRvaevanavafirnfPQGFNTVVgEKGVL-LSGGQKQRIAIARALLKNPKILLLD 362
Cdd:COG1245  423 RS-------ANTDDFGSSYYKTEIIK--------------PLGLEKLL-DKNVKdLSGGELQRVAIAACLSRDADLYLLD 480

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767912304 363 EATSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTI 399
Cdd:COG1245  481 EPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI 519
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 200-422 2.65e-10

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 62.28  E-value: 2.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 200 NVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLlrlydpaSGTISLDGHDIR----------QLNPVw 269
Cdd:PRK11147   5 SIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRIIyeqdlivarlQQDPP- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 270 lRSKIGTVsqepilFScSIAENIAYGAD--------------DPSSVTAEEIQRVAEV---ANAvafiRNFPQGFNTVVG 332
Cdd:PRK11147  77 -RNVEGTV------YD-FVAEGIEEQAEylkryhdishlvetDPSEKNLNELAKLQEQldhHNL----WQLENRINEVLA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 333 EKGV-------LLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-EYLvqEALdrLMDGRTVLV-IAHRLSTIKN-A 402
Cdd:PRK11147 145 QLGLdpdaalsSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETiEWL--EGF--LKTFQGSIIfISHDRSFIRNmA 220

                        250       260
                 ....*....|....*....|....*....
gi 767912304 403 NMVAVLDQGKITEY---------GKHEEL 422
Cdd:PRK11147 221 TRIVDLDRGKLVSYpgnydqyllEKEEAL 249
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
218-430 5.40e-10

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 60.59  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 218 SLSIPSGSVTALVGPSGSGKSTVLSLLLRL----YDPASGTISLDGHDIRQLNPVWLRSKIG-TVS---QEPIlfSCSia 289
Cdd:PRK15093  27 SMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRKLVGhNVSmifQEPQ--SCL-- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 290 eniaygadDPS-SVTAEEIQ--------------------RVAEVANAVAF------IRNFPQGfntvvgekgvlLSGGQ 342
Cdd:PRK15093 103 --------DPSeRVGRQLMQnipgwtykgrwwqrfgwrkrRAIELLHRVGIkdhkdaMRSFPYE-----------LTEGE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 343 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKH 419
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnqNNNTTILLISHDLQMLsQWADKINVLYCGQTVETAPS 243

                        250
                 ....*....|.
gi 767912304 420 EELLSKPNGIY 430
Cdd:PRK15093 244 KELVTTPHHPY 254
PLN03073 PLN03073
ABC transporter F family; Provisional
 196-416 5.58e-10

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 61.41  E-value: 5.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPevPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTI--------------SLDGHD 261
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLD 586

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 262 IrqlnpvwlrskigtvSQEPILFscsiaeniaygaddpssvtaeeiqrvaevanavaFIRNFP----QGFNTVVGEKGV- 336
Cdd:PLN03073 587 L---------------SSNPLLY----------------------------------MMRCFPgvpeQKLRAHLGSFGVt 617

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 337 ---------LLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-EYLVQEALdrLMDGrTVLVIAHRLSTIKNA-NMV 405
Cdd:PLN03073 618 gnlalqpmyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQGLV--LFQG-GVLMVSHDEHLISGSvDEL 694

                        250
                 ....*....|.
gi 767912304 406 AVLDQGKITEY 416
Cdd:PLN03073 695 WVVSEGKVTPF 705
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 218-430 8.49e-10

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 59.76  E-value: 8.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 218 SLSIPSGSVTALVGPSGSGKStVLSL-LLRLYD-PA---SGTISLDGHDIRQLNPVWLRSKIGT----VSQEPILfSCSI 288
Cdd:PRK11022  27 SYSVKQGEVVGIVGESGSGKS-VSSLaIMGLIDyPGrvmAEKLEFNGQDLQRISEKERRNLVGAevamIFQDPMT-SLNP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 289 AENIAYGADDPSSV-----TAEEIQRVAEVANAVAF------IRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPK 357
Cdd:PRK11022 105 CYTVGFQIMEAIKVhqggnKKTRRQRAIDLLNQVGIpdpasrLDVYPHQ-----------LSGGMSQRVMIAMAIACRPK 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 358 ILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSKPNGIY 430
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFRAPRHPY 249
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 218-419 9.49e-10

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 60.61  E-value: 9.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  218 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPAS--GTISLDGHDIRQLNPVWLRSK-IGTVSQEPILF-SCSIAENIA 293
Cdd:TIGR02633  21 DLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVpELSVAENIF 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  294 YGAD--DPSSVT--AEEIQRVAEVANAVafirNFPQGFNT-VVGEKGvllsGGQKQRIAIARALLKNPKILLLDEATSAL 368
Cdd:TIGR02633 101 LGNEitLPGGRMayNAMYLRAKNLLREL----QLDADNVTrPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767912304  369 -DAENEYLVQEALDRLMDGRTVLVIAHRLSTIKnanmvAVLDQGKITEYGKH 419
Cdd:TIGR02633 173 tEKETEILLDIIRDLKAHGVACVYISHKLNEVK-----AVCDTICVIRDGQH 219
PLN03140 PLN03140
ABC transporter G family member; Provisional
 224-397 1.45e-09

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 60.63  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  224 GSVTALVGPSGSGKSTVLSLLL--RLYDPASGTISLDGHDIRQLNpvwlRSKIGTVSQEPILFS--CSIAENIAYGA--D 297
Cdd:PLN03140  906 GVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGFPKKQET----FARISGYCEQNDIHSpqVTVRESLIYSAflR 981

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  298 DPSSVTAEEIQR-VAEVANAVAfIRNFPqgfNTVVGEKGVL-LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYL 375
Cdd:PLN03140  982 LPKEVSKEEKMMfVDEVMELVE-LDNLK---DAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1057

                         170       180
                  ....*....|....*....|...
gi 767912304  376 VQEALDRLMD-GRTVLVIAHRLS 397
Cdd:PLN03140 1058 VMRTVRNTVDtGRTVVCTIHQPS 1080
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
214-409 1.59e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 59.82  E-value: 1.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 214 FQDFSLSIPS-GSVTALVGPSGSGKSTVLSLLlrlydpaSGTI--SLDGHDIrqlNPVW---LRSKIGTVSQEpiLFSCS 287
Cdd:PRK13409  88 FKLYGLPIPKeGKVTGILGPNGIGKTTAVKIL-------SGELipNLGDYEE---EPSWdevLKRFRGTELQN--YFKKL 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 288 IAENIAygaddpssvTAEEIQRVAEVANAVafirnfpQGfnTV------VGEKGVL-------------------LSGGQ 342
Cdd:PRK13409 156 YNGEIK---------VVHKPQYVDLIPKVF-------KG--KVrellkkVDERGKLdevverlglenildrdiseLSGGE 217

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304 343 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLstiknanmvAVLD 409
Cdd:PRK13409 218 LQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL---------AVLD 275
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 12-175 1.91e-09

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


Pssm-ID: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 58.32  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18778  136 FSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKA 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYafwvgisiggLSSFYSElmkgLGAGGRLWE 171
Cdd:cd18778  216 QLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLY----------LGLFYEP----ITSLHGLNE 281


                 ....
gi 767912304 172 LLER 175
Cdd:cd18778  282 MLQR 285
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 196-413 2.01e-09

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: 59.45  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  196 LEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA-SGTISLDGHDIRQLNPV-WLRSK 273
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAqAIRAG 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  274 IGTVSQE-------PILfscSIAENIAYGA----------DDPSSVTA--EEIQRVaEVANAVAFIrnfPQGfntvvgek 334
Cdd:TIGR02633 338 IAMVPEDrkrhgivPIL---GVGKNITLSVlksfcfkmriDAAAELQIigSAIQRL-KVKTASPFL---PIG-------- 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  335 gvLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQGK 412
Cdd:TIGR02633 403 --RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAEVLGlSDRVLVIGEGK 480


                  .
gi 767912304  413 I 413
Cdd:TIGR02633 481 L 481
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 197-401 2.60e-09

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 58.87  E-value: 2.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 197 EFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL-----------LRLYDPASG---TIsldgHDI 262
Cdd:PRK10938 262 VLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndLTLFGRRRGsgeTI----WDI 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 263 RQlnpvwlrsKIGTVSQEPIL---FSCSIAENIAYGADDPSSVtaeeIQRVAEVANAVAfirnfPQ-----GFNTVVGEK 334
Cdd:PRK10938 335 KK--------HIGYVSSSLHLdyrVSTSVRNVILSGFFDSIGI----YQAVSDRQQKLA-----QQwldilGIDKRTADA 397

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 335 GVL-LSGGQkQRIA-IARALLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLV------------IAHRLSTI 399
Cdd:PRK10938 398 PFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsEGETQLLfvshhaedapacITHRLEFV 476


                 ..
gi 767912304 400 KN 401
Cdd:PRK10938 477 PD 478
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
 18-165 3.25e-09

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


Pssm-ID: 350002 [Multi-domain]  Cd Length: 312  Bit Score: 58.06  E-value: 3.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  18 LATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAF 97
Cdd:cd18558  161 LTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAI 240

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304  98 ARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGA 165
Cdd:cd18558  241 TFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGA 308
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
207-394 3.73e-09

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 56.40  E-value: 3.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 207 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNpvwlRSK-IGTVSQEPILFS 285
Cdd:PRK13543  20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRfMAYLGHLPGLKA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 286 -CSIAENIAYgaddPSSVTAEEIQRVAEVANAVAFIRNFPQgfnTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEA 364
Cdd:PRK13543  96 dLSTLENLHF----LCGLHGRRAKQMPGSALAIVGLAGYED---TLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEP 164

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767912304 365 TSALDAENEYLVQEALD-RLMDGRTVLVIAH 394
Cdd:PRK13543 165 YANLDLEGITLVNRMISaHLRGGGAALVTTH 195
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 167-414 4.40e-09

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 58.40  E-value: 4.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 167 GRlwELLEREPKLPFNEGVILneksfqgaLEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLR 246
Cdd:PRK13549 241 GR--ELTALYPREPHTIGEVI--------LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 247 LYDPAS-GTISLDGHDIRQLNPV-WLRSKIGTVSQE-------PILfscSIAENIAYGA----------DDPSSVTA--E 305
Cdd:PRK13549 311 AYPGRWeGEIFIDGKPVKIRNPQqAIAQGIAMVPEDrkrdgivPVM---GVGKNITLAAldrftggsriDDAAELKTilE 387

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 306 EIQRVaEVANAVAFIRnfpqgfntvVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEY--------LVQ 377
Cdd:PRK13549 388 SIQRL-KVKTASPELA---------IAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYeiyklinqLVQ 453

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 767912304 378 EaldrlmdGRTVLVIAHRLSTIKN-ANMVAVLDQGKIT 414
Cdd:PRK13549 454 Q-------GVAIIVISSELPEVLGlSDRVLVMHEGKLK 484
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 214-409 7.58e-09

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: 57.87  E-value: 7.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 214 FQDFSLSIP-SGSVTALVGPSGSGKSTVLSLLlrlydpaSGtisldghdirQLNPvwlrsKIGTVSQEP----IL--FSC 286
Cdd:COG1245   88 FRLYGLPVPkKGKVTGILGPNGIGKSTALKIL-------SG----------ELKP-----NLGDYDEEPswdeVLkrFRG 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 287 SIAENiaYgaddpssvtaeeIQRVAE----VANAVAFIRNFPQGFNTVVG-------EKGVL------------------ 337
Cdd:COG1245  146 TELQD--Y------------FKKLANgeikVAHKPQYVDLIPKVFKGTVRellekvdERGKLdelaeklglenildrdis 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 338 -LSGGQKQRIAIARALLKNPKILLLDEATSALD-------AEneyLVQEALDrlmDGRTVLVIAHRLstiknanmvAVLD 409
Cdd:COG1245  212 eLSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrlnvAR---LIRELAE---EGKYVLVVEHDL---------AILD 276
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 177-394 1.17e-08

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 57.21  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 177 PKLPFNEGvilnEKSFQGALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTIS 256
Cdd:PRK15064 305 PFIRFEQD----KKLHRNALEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 257 ldghdirqlnpvWlrskigtvsqepilfscsiAEN--IAYGADDPSSVTAEEIqrvaevaNAVAFIRNF--PQGFNTVVg 332
Cdd:PRK15064 378 ------------W-------------------SENanIGYYAQDHAYDFENDL-------TLFDWMSQWrqEGDDEQAV- 418

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912304 333 eKGVL----------------LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDrLMDGrTVLVIAH 394
Cdd:PRK15064 419 -RGTLgrllfsqddikksvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE-KYEG-TLIFVSH 493
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 214-414 1.44e-08

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 56.60  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 214 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSKIGTV-----SQEPILF-SCS 287
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYlDAP 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 288 IAENIaygaddpSSVTAEE----IQRVAEVANAVAFIRNFPQGFNTVvgEKGV-LLSGGQKQRIAIARALLKNPKILLLD 362
Cdd:PRK15439 358 LAWNV-------CALTHNRrgfwIKPARENAVLERYRRALNIKFNHA--EQAArTLSGGNQQKVLIAKCLEASPQLLIVD 428

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 363 EATSALD--AENE-YLVQEALDRlmDGRTVLVIAHRLSTI-KNANMVAVLDQGKIT 414
Cdd:PRK15439 429 EPTRGVDvsARNDiYQLIRSIAA--QNVAVLFISSDLEEIeQMADRVLVMHQGEIS 482
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 215-402 1.48e-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: 54.25  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 215 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRlydpASGTISLDGhdirqLNPVWLRSKIGTVSQEPILfscsIAENIAY 294
Cdd:cd03238   12 QNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----ASGKARLIS-----FLPKFSRNKLIFIDQLQFL----IDVGLGY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 295 gaddpssVTaeeiqrvaevanavafirnfpqgfntvVGEKGVLLSGGQKQRIAIARALLKNPK--ILLLDEATSALDAEN 372
Cdd:cd03238   79 -------LT---------------------------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767912304 373 EYLVQEALDRLMD-GRTVLVIAHRLSTIKNA 402
Cdd:cd03238  125 INQLLEVIKGLIDlGNTVILIEHNLDVLSSA 155
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 209-412 1.99e-08

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 56.28  E-value: 1.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 209 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIR-QLNPVWLRSKIGTVSQE-PILFSC 286
Cdd:PRK10982   9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 287 SIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIrnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATS 366
Cdd:PRK10982  89 SVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDEL-----DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767912304 367 AL-DAENEYLVQeALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGK 412
Cdd:PRK10982 164 SLtEKEVNHLFT-IIRKLKErGCGIVYISHKMEEIfQLCDEITILRDGQ 211
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
215-414 2.15e-08

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 56.07  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 215 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwlRSKI--GTV------SQEPILFSC 286
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSP---RDAIraGIMlcpedrKAEGIIPVH 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 287 SIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNF----PQGfntvvGEKGVLLSGGQKQRIAIARALLKNPKILLLD 362
Cdd:PRK11288 347 SVADNINISARRHHLRAGCLINNRWEAENADRFIRSLniktPSR-----EQLIMNLSGGNQQKAILGRWLSEDMKVILLD 421

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 363 EATSALD--AENE-YLVQEALDRlmDGRTVLVIAHRL-STIKNANMVAVLDQGKIT 414
Cdd:PRK11288 422 EPTRGIDvgAKHEiYNVIYELAA--QGVAVLFVSSDLpEVLGVADRIVVMREGRIA 475
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 215-405 2.59e-08

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 56.17  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  215 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLL------RLYdpASGTISLDGHDIRQLNPVwlrSKIGTVSQEPI------ 282
Cdd:TIGR00630 625 KNITVSIPLGLFTCITGVSGSGKSTLINDTLypalanRLN--GAKTVPGRYTSIEGLEHL---DKVIHIDQSPIgrtprs 699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  283 --------------LFscsiAE----------------NIAYGA----------------DDPSSVTAE----------- 305
Cdd:TIGR00630 700 npatytgvfdeireLF----AEtpeakvrgytpgrfsfNVKGGRceacqgdgvikiemhfLPDVYVPCEvckgkrynret 775

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  306 -EIQ----RVAEVAN-----AVAFIRNFPQ-----------GFNTV-VGEKGVLLSGGQKQRIAIARALLK---NPKILL 360
Cdd:TIGR00630 776 lEVKykgkNIADVLDmtveeAYEFFEAVPSisrklqtlcdvGLGYIrLGQPATTLSGGEAQRIKLAKELSKrstGRTLYI 855

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767912304  361 LDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNANMV 405
Cdd:TIGR00630 856 LDEPTTGLHFDDIKKLLEVLQRLVDkGNTVVVIEHNLDVIKTADYI 901
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 336-433 3.39e-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: 52.96  E-value: 3.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 336 VLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKI 413
Cdd:cd03222   70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFEGEP 149

                         90       100
                 ....*....|....*....|
gi 767912304 414 TEYGKHEELLSKPNGIYRKL 433
Cdd:cd03222  150 GVYGIASQPKGTREGINRFL 169
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 214-397 5.93e-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: 53.52  E-value: 5.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 214 FQDFSLSIP-SGSVTALVGPSGSGKSTVLSLLLRLYDPASGTIsldghdirQLNPVW---LRSKIGTVSQEpilFSCSIA 289
Cdd:cd03236   15 FKLHRLPVPrEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--------DDPPDWdeiLDEFRGSELQN---YFTKLL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 290 ENIAYGADDPSSV----------TAEEIQRVAEvanavafiRNFPQGFNTVVGEKGVL------LSGGQKQRIAIARALL 353
Cdd:cd03236   84 EGDVKVIVKPQYVdlipkavkgkVGELLKKKDE--------RGKLDELVDQLELRHVLdrnidqLSGGELQRVAIAAALA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767912304 354 KNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLS 397
Cdd:cd03236  156 RDADFYFFDEPSSYLDIKQRLNAARLIRELAeDDNYVLVVEHDLA 200
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 226-394 8.22e-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: 52.22  E-value: 8.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 226 VTALVGPSGSGKSTVLSLLLrlydpasgtISLDGHDIRQLNPVWLRSKIgtvsqepilfsCSIAENIAYGADDPSSVTAE 305
Cdd:cd03240   24 LTLIVGQNGAGKTTIIEALK---------YALTGELPPNSKGGAHDPKL-----------IREGEVRAQVKLAFENANGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 306 E--IQRVAEVANAVAFIRnfpQG-FNTVVGEKGVLLSGGQKQ------RIAIARALLKNPKILLLDEATSALDAENeylV 376
Cdd:cd03240   84 KytITRSLAILENVIFCH---QGeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---I 157

                        170       180
                 ....*....|....*....|....
gi 767912304 377 QEALDRLMD------GRTVLVIAH 394
Cdd:cd03240  158 EESLAEIIEerksqkNFQLIVITH 181
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
215-415 1.15e-07

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 54.02  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 215 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLRSKIGTVSQ---EPILFS-CSIA 289
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdAVKKGMAYITEsrrDNGFFPnFSIA 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 290 ENIA-------------YGADDPSsvtaeEIQRVAEVANAVAFIRNfpQGFNTVVGEkgvlLSGGQKQRIAIARALLKNP 356
Cdd:PRK09700 360 QNMAisrslkdggykgaMGLFHEV-----DEQRTAENQRELLALKC--HSVNQNITE----LSGGNQQKVLISKWLCCCP 428

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912304 357 KILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNA-NMVAVLDQGKITE 415
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADdGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 218-424 1.34e-07

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 53.48  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 218 SLSIPSGSVTALVGPSGSGKSTvLSLLLrlydpaSGTISL-DGHDIRQLNPVWLRS-----KIgtVSQEpilFSCSIAEN 291
Cdd:PRK10938  23 SLTLNAGDSWAFVGANGSGKSA-LARAL------AGELPLlSGERQSQFSHITRLSfeqlqKL--VSDE---WQRNNTDM 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 292 IAYGADDPSSVTAEEIQ-------RVAEVANAVA----FIRNFPQgfntvvgekgvlLSGGQKQRIAIARALLKNPKILL 360
Cdd:PRK10938  91 LSPGEDDTGRTTAEIIQdevkdpaRCEQLAQQFGitalLDRRFKY------------LSTGETRKTLLCQALMSEPDLLI 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304 361 LDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLS 424
Cdd:PRK10938 159 LDEPFDGLDVASRQQLAELLASLHqSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ 224
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 217-405 1.88e-07

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 51.41  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 217 FSLSI---PSgSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLrSKIGtvSQEPILFSCSIAENIA 293
Cdd:PRK13541  17 FDLSItflPS-AITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC-TYIG--HNLGLKLEMTVFENLK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 294 YGADDPSSVTAeeiqrvaeVANAVAFIRnfpqgFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENE 373
Cdd:PRK13541  93 FWSEIYNSAET--------LYAAIHYFK-----LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767912304 374 YLVQEALD-RLMDGRTVLVIAHRLSTIKNANMV 405
Cdd:PRK13541 160 DLLNNLIVmKANSGGIVLLSSHLESSIKSAQIL 192
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 196-394 1.88e-07

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 53.20  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 196 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLdGHDIrqlnpvwlrsKIG 275
Cdd:PRK11819 325 IEAENLSKSFGDRL---LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLA 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 276 TVSQ--EPILFSCSIAENIAYGADdpssvtaeeIQRVA--EVaNAVAFIRNFpqGFNTVVGEKGV-LLSGGQKQRIAIAR 350
Cdd:PRK11819 391 YVDQsrDALDPNKTVWEEISGGLD---------IIKVGnrEI-PSRAYVGRF--NFKGGDQQKKVgVLSGGERNRLHLAK 458

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767912304 351 ALLKNPKILLLDEATSALDAENEYLVQEALDRLmdGRTVLVIAH 394
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDVETLRALEEALLEF--PGCAVVISH 500
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
216-369 2.03e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 53.59  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 216 DFSLSIPSGSVTALVGPSGSGKSTVLSLLlrlydpA------SGTISLDGHDI------RQLNPvwlrsKIGTVSQ---- 279
Cdd:NF033858  19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLI------AgarkiqQGRVEVLGGDMadarhrRAVCP-----RIAYMPQglgk 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 280 --EPILfscSIAENIA-----YGADdpssvTAEEIQRVAEVANAV---AFiRNFPQGfntvvgeKgvlLSGGQKQRIAIA 349
Cdd:NF033858  88 nlYPTL---SVFENLDffgrlFGQD-----AAERRRRIDELLRATglaPF-ADRPAG-------K---LSGGMKQKLGLC 148

                        170       180
                 ....*....|....*....|
gi 767912304 350 RALLKNPKILLLDEATSALD 369
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVD 168
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
 12-160 2.20e-07

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


Pssm-ID: 350055 [Multi-domain]  Cd Length: 294  Bit Score: 52.21  E-value: 2.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18782  137 FSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGE 216

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELM 160
Cdd:cd18782  217 GFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQ 285
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 218-437 2.33e-07

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 52.97  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 218 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVsqepilfscsiaENIAYGAD 297
Cdd:PRK13545  44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI------------ENIELKGL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 298 dPSSVTAEEIQ----RVAEVANAVAFIRnfpQGFNTvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDaenE 373
Cdd:PRK13545 112 -MMGLTKEKIKeiipEIIEFADIGKFIY---QPVKT--------YSSGMKSRLGFAISVHINPDILVIDEALSVGD---Q 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912304 374 YLVQEALDRLMD----GRTVLVIAHRLSTIKNANMVAV-LDQGKITEYGKHEELLSKPNGIYRKL--MNKQ 437
Cdd:PRK13545 177 TFTKKCLDKMNEfkeqGKTIFFISHSLSQVKSFCTKALwLHYGQVKEYGDIKEVVDHYDEFLKKYnqMSVE 247
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
332-428 3.19e-07

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 52.04  E-value: 3.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 332 GEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLV-QEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLD 409
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVID 218

                         90
                 ....*....|....*....
gi 767912304 410 QGKITEYGKHEELLSKPNG 428
Cdd:NF000106 219 RGRVIADGKVDELKTKVGG 237
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
215-435 3.21e-06

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 48.27  E-value: 3.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 215 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH-DIRQLNpVWLRSKIGTVsqEPILFSCSIaenIA 293
Cdd:PRK13546  41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAIS-AGLSGQLTGI--ENIEFKMLC---MG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 294 YGADDPSSVTAEEIqrvaEVANAVAFIRNFPQGFntvvgekgvllSGGQKQRIAIARALLKNPKILLLDEATSALDaenE 373
Cdd:PRK13546 115 FKRKEIKAMTPKII----EFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD---Q 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304 374 YLVQEALDRLMD----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKpngiYRKLMN 435
Cdd:PRK13546 177 TFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK----YEAFLN 239
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 218-403 3.65e-06

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 46.97  E-value: 3.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 218 SLSIPSGSVTALVGPSGSGKSTVLSlllrlydpasgTISLdghdirqlnpvwlrskigtvsqepILFSCSIAENIAYGAD 297
Cdd:cd03227   15 DVTFGEGSLTIITGPNGSGKSTILD-----------AIGL------------------------ALGGAQSATRRRSGVK 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 298 DPSSVTAEEIQrvaevanavaFIRNFPQgfntvvgekgvlLSGGQKQRIAIARAL---LKNPKIL-LLDEATSALDAENE 373
Cdd:cd03227   60 AGCIVAAVSAE----------LIFTRLQ------------LSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDG 117

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767912304 374 YLVQEAL-DRLMDGRTVLVIAHRLSTIKNAN 403
Cdd:cd03227  118 QALAEAIlEHLVKGAQVIVITHLPELAELAD 148
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
 12-142 4.29e-06

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


Pssm-ID: 349998 [Multi-domain]  Cd Length: 299  Bit Score: 48.18  E-value: 4.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLaTFVLSVVPPVSIIAV--IYGRyLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVM 89
Cdd:cd18554  142 LVLNPKL-TFVSLVIFPFYILAVkyFFGR-LRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFL 219

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767912304  90 QLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA 142
Cdd:cd18554  220 TRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYM 272
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
 12-142 4.49e-06

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


Pssm-ID: 350032 [Multi-domain]  Cd Length: 294  Bit Score: 48.26  E-value: 4.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASkvdhvmQL 91
Cdd:cd18588  137 FYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEE------LL 210

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304  92 AR--KEAFARAGFFGATGLSGNLI----VLSVLYKGGLLMGSAHMTVGELSSFLMYA 142
Cdd:cd18588  211 ARyvKASFKTANLSNLASQIVQLIqkltTLAILWFGAYLVMDGELTIGQLIAFNMLA 267
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
 12-169 6.79e-06

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


Pssm-ID: 350014 [Multi-domain]  Cd Length: 294  Bit Score: 47.44  E-value: 6.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPpvsIIAVIYGRYLRKLTKVTQDSLAQATQLAE---ERIGNVRTVRAFGKEMTEIEKYASKVDHV 88
Cdd:cd18570  137 FFYNWKLFLITLLIIP---LYILIILLFNKPFKKKNREVMESNAELNSyliESLKGIETIKSLNAEEQFLKKIEKKFSKL 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  89 MQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFL-MYAFWVGiSIGGLSSFYSELMKGLGAGG 167
Cdd:cd18570  214 LKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNaLLGYFLG-PIENLINLQPKIQEAKVAAD 292


                 ..
gi 767912304 168 RL 169
Cdd:cd18570  293 RL 294
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
338-402 8.64e-06

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 48.10  E-value: 8.64e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912304 338 LSGGQKQRIAIARALLK--NPKIL-LLDEATSAL---DaeneylVQ---EALDRLMD-GRTVLVIAHRLSTIKNA 402
Cdd:COG0178  827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLhfhD------IRkllEVLHRLVDkGNTVVVIEHNLDVIKTA 895
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 215-405 1.19e-05

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: 46.10  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 215 QDFSLSIPSGSVTALVGPSGSGKSTV----------------LSLLLR-----LYDPA-------SGTISLDGHDIRQlN 266
Cdd:cd03270   12 KNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAYARqflgqMDKPDvdsieglSPAIAIDQKTTSR-N 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 267 PvwlRSKIGTVSQ----EPILFScsiaeniaygaddpssvtaeeiqRVAeVANAVAFIRNFPQGFNTVVGEKGVLlSGGQ 342
Cdd:cd03270   91 P---RSTVGTVTEiydyLRLLFA-----------------------RVG-IRERLGFLVDVGLGYLTLSRSAPTL-SGGE 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304 343 KQRIAIARALLKNPK--ILLLDEATSAL-DAENEYLVqEALDRLMD-GRTVLVIAHRLSTIKNANMV 405
Cdd:cd03270  143 AQRIRLATQIGSGLTgvLYVLDEPSIGLhPRDNDRLI-ETLKRLRDlGNTVLVVEHDEDTIRAADHV 208
uvrA PRK00349
excinuclease ABC subunit UvrA;
338-402 1.39e-05

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 47.37  E-value: 1.39e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912304 338 LSGGQKQRIAIARALLKNP--KIL-LLDEATSALDAENeylVQ---EALDRLMD-GRTVLVIAHRLSTIKNA 402
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFED---IRkllEVLHRLVDkGNTVVVIEHNLDVIKTA 899
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 212-425 2.69e-05

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: 46.93  E-value: 2.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   212 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIGTVSQEPILFSCSIAEN 291
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLTGRE 2031

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304   292 IAYGADDPSSVTAEEIQRVAEVAnavafIRNFpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 371
Cdd:TIGR01257 2032 HLYLYARLRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304   372 NEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSK 425
Cdd:TIGR01257 2105 ARRMLWNTIVSIIrEGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSK 2160
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
 10-160 3.61e-05

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


Pssm-ID: 350012 [Multi-domain]  Cd Length: 294  Bit Score: 45.24  E-value: 3.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  10 LQFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKL-TKVTQDSLAQATQLAEErIGNVRTVRAFGKEMTEI----EKYASK 84
Cdd:cd18568  135 LMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNsREIFQANAEQQSFLVEA-LTGIATIKALAAERPIRwrweNKFAKA 213

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912304  85 VDHVMQLARKEAFARAgffgATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELM 160
Cdd:cd18568  214 LNTRFRGQKLSIVLQL----ISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQ 285
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 212-369 8.28e-05

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 44.88  E-value: 8.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 212 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDirqlnpvwlrsKIGTVSQEPILF-SCSIAE 290
Cdd:PRK15064  15 PLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNE-----------RLGKLRQDQFAFeEFTVLD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 291 NIAYGADDPSSV-------------TAEEIQRVAEVANAVAFIRNFpqgfnTVVGEKGVLLSG----------------- 340
Cdd:PRK15064  84 TVIMGHTELWEVkqerdriyalpemSEEDGMKVADLEVKFAEMDGY-----TAEARAGELLLGvgipeeqhyglmsevap 158

                        170       180
                 ....*....|....*....|....*....
gi 767912304 341 GQKQRIAIARALLKNPKILLLDEATSALD 369
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLD 187
GguA NF040905
sugar ABC transporter ATP-binding protein;
195-392 8.50e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 44.78  E-value: 8.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 195 ALEFKN--VHfaYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKsTVL--SLLLRLYDP-ASGTISLDGHDIRqlnpvw 269
Cdd:NF040905 257 VFEVKNwtVY--HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGR-TELamSVFGRSYGRnISGTVFKDGKEVD------ 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 270 lrskIGTVSQepilfscSIAENIAYGADD------------PSSVTAEEIQRVAE--VANAVAFIR---NFPQGFNT--- 329
Cdd:NF040905 328 ----VSTVSD-------AIDAGLAYVTEDrkgyglnliddiKRNITLANLGKVSRrgVIDENEEIKvaeEYRKKMNIktp 396

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912304 330 VVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVI 392
Cdd:NF040905 397 SVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAeGKGVIVI 460
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 338-405 1.56e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 44.43  E-value: 1.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912304  338 LSGGQKQRIAIARALL---KNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNANMV 405
Cdd:PRK00635  810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHqGHTVVIIEHNMHVVKVADYV 881
COG4639 COG4639
Predicted kinase [General function prediction only];
224-265 1.71e-04

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 41.74  E-value: 1.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767912304 224 GSVTALVGPSGSGKSTVLSlllRLYDPASgTISLDghDIRQL 265
Cdd:COG4639    2 LSLVVLIGLPGSGKSTFAR---RLFAPTE-VVSSD--DIRAL 37
AAA_29 pfam13555
P-loop containing region of AAA domain;
214-252 1.80e-04

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 39.51  E-value: 1.80e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 767912304  214 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPAS 252
Cdd:pfam13555  12 FDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
PLN03073 PLN03073
ABC transporter F family; Provisional
 339-394 2.06e-04

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 43.70  E-value: 2.06e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912304 339 SGGQKQRIAIARALLKNPKILLLDEATSALDAE-----NEYLVQEAldrlmdgRTVLVIAH 394
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHavlwlETYLLKWP-------KTFIVVSH 399
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 212-369 2.86e-04

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 43.18  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 212 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP-----------VWLRSKIGTVSQE 280
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAneainhgfalvTEERRSTGIYAYL 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 281 PILFSCSIAENIAY----GADDPSSVTAEeIQRVAEVANAVAfirnfpQGFNTVVGEkgvlLSGGQKQRIAIARALLKNP 356
Cdd:PRK10982 342 DIGFNSLISNIRNYknkvGLLDNSRMKSD-TQWVIDSMRVKT------PGHRTQIGS----LSGGNQQKVIIGRWLLTQP 410

                        170
                 ....*....|...
gi 767912304 357 KILLLDEATSALD 369
Cdd:PRK10982 411 EILMLDEPTRGID 423
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
221-394 2.98e-04

RecA-family ATPase [Replication, recombination and repair];


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 42.58  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 221 IPSGSVTALVGPSGSGKST-VLSLLLRLydpASGTiSLDGHDIRQLNPVWLrskigtvsqepilfscsiaeniayGADDP 299
Cdd:COG3598   10 LPEGGVTLLAGPPGTGKSFlALQLAAAV---AAGG-PWLGRRVPPGKVLYL------------------------AAEDD 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 300 ssvtAEEIQ-RVAEVANAVAFIRNFPQG-FNTVVGEKGVLLSGGQKQRIAIARAllKNPKILLLDEATSAL-----DAEN 372
Cdd:COG3598   62 ----RGELRrRLKALGADLGLPFADLDGrLRLLSLAGDLDDTDDLEALERAIEE--EGPDLVVIDPLARVFggdenDAEE 135

                        170       180
                 ....*....|....*....|....
gi 767912304 373 EYLVQEALDRLMD--GRTVLVIAH 394
Cdd:COG3598  136 MRAFLNPLDRLAErtGAAVLLVHH 159
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 12-142 5.09e-04

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


Pssm-ID: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 41.78  E-value: 5.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18565  150 FYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDA 229

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLL------MGSAHMTVGELSSFLMYA 142
Cdd:cd18565  230 NWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWvldgppLFTGTLTVGTLVTFLFYT 286
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
 214-261 1.25e-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: 40.76  E-value: 1.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 767912304 214 FQDFSLSIPSGsVTALVGPSGSGKSTVLSLLLRLYDPaSGTISLDGHD 261
Cdd:COG3593   14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGP-SSSRKFDEED 59
ABC_6TM_CvaB_RaxB_like cd18567
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...
 12-142 1.28e-03

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


Pssm-ID: 350011 [Multi-domain]  Cd Length: 294  Bit Score: 40.52  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQL 91
Cdd:cd18567  137 FLYSPKLALIVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINA 216

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767912304  92 ARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA 142
Cdd:cd18567  217 DIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYK 267
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 12-159 1.51e-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: 349984 [Multi-domain]  Cd Length: 295  Bit Score: 40.16  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  12 FFVSPNLATFVLSVVPPVSIIAVIYGRYL----RKLTKVTqdslAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDH 87
Cdd:cd18540  138 LILNWKLALIVLAVVPVLAVVSIYFQKKIlkayRKVRKIN----SRITGAFNEGITGAKTTKTLVREEKNLREFKELTEE 213

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912304  88 VMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA---FWvgiSIGGLSSFYSEL 159
Cdd:cd18540  214 MRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIGTLVAFISYAtqfFE---PIQQLARVLAEL 285
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 215-430 1.53e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 40.97  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  215 QDFSLSIPSGSVTALVGPSGSGKSTVLS---------LLLRLYDPASGTISLDGHDIrqlnPVWLRSKIGT--------- 276
Cdd:PRK00635 1507 QNLNVSAPLHSLVAISGVSGSGKTSLLLegfykqacaLIEKGPSVFSEIIFLDSHPQ----ISSQRSDISTyfdiapslr 1582

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  277 -----VSQEPIL------FS-------CSIAENIAYGADDPSSVTAEE----------IQRVA----------------- 311
Cdd:PRK00635 1583 nfyasLTQAKALnisasmFStntkqgqCSDCWGLGYQWIDRAFYALEKrpcptcsgfrIQPLAqevvyegkhfgqllqtp 1662

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304  312 --EVANAVAFIRNFPQGFNTVV---------GEKGVLLSGGQKQRIAIARALL---KNPKILLLDEATSALDAENEYLVQ 377
Cdd:PRK00635 1663 ieEVAETFPFLKKIQKPLQALIdnglgylplGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALL 1742

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767912304  378 EALDRLMD-GRTVLVIAHRLSTIKNANMVAVLDQGKiTEYGKHEELLSKPNGIY 430
Cdd:PRK00635 1743 VQLRTLVSlGHSVIYIDHDPALLKQADYLIEMGPGS-GKTGGKILFSGPPKDIS 1795
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 337-405 1.78e-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: 40.73  E-value: 1.78e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912304   337 LLSGGQKQRIAIA--RALLK-NPK-ILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMV 405
Cdd:pfam02463 1077 LLSGGEKTLVALAliFAIQKyKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKL 1149
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
 226-287 2.19e-03

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 40.07  E-value: 2.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912304  226 VTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKI-GTVSQEPILFSCS 287
Cdd:pfam13304   1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLnGIDPKEPIEFEIS 63
PRK01156 PRK01156
chromosome segregation protein; Provisional
 325-404 2.78e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.27  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912304 325 QGFNTVVGEKGVL-----LSGGQKQ------RIAIARALLKNPKILLLDEATSALDAENEY----LVQEALDRLMDGRTV 389
Cdd:PRK01156 784 QDFNITVSRGGMVegidsLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTnlkdIIEYSLKDSSDIPQV 863

                         90
                 ....*....|....*
gi 767912304 390 LVIAHRLSTIKNANM 404
Cdd:PRK01156 864 IMISHHRELLSVADV 878
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 337-404 3.36e-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: 38.60  E-value: 3.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912304 337 LLSGGQKQRIAIAR--ALLK-NPK-ILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANM 404
Cdd:cd03278  113 LLSGGEKALTALALlfAIFRvRPSpFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADR 184
Zeta_toxin pfam06414
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ...
 229-267 3.37e-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: 3.37e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 767912304  229 LVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP 267
Cdd:pfam06414  16 LGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELHP 54
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 229-250 6.39e-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: 36.74  E-value: 6.39e-03
                         10        20
                 ....*....|....*....|..
gi 767912304 229 LVGPSGSGKSTVLSLLLRLYDP 250
Cdd:cd00071    4 LSGPSGVGKSTLLKRLLEEFDP 25
 
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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