NCBI Conserved Domain Search

Conserved domains on [gi|493533268|ref|WP_006487248|]

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MULTISPECIES: ABC transporter ATP-binding protein [Mesotoga]

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];

1-570

4.80e-152

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 448.84 E-value: 4.80e-152

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   1 MENEKKTVRRFVFKLFKVYWKRELLAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYF 80
Cdd:COG1132    1 MSKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  81 GEVVFETTALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFN 160
Cdd:COG1132   81 QRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVID 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 161 WKLTLLPLGFIVFSFLVIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRIAMPFAWVMNFFDRFQGDHIYAGKRF 240
Cdd:COG1132  161 WRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 241 IKSIKIAGTLKTSINGLISFSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQSWGGLLRTIEVLEA 320
Cdd:COG1132  241 ARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 321 PEEERSNSSPK-LEDVR-SISLENIAFGY-GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYIN 397
Cdd:COG1132  321 PPEIPDPPGAVpLPPVRgEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 398 GDPVSNSAL--LRPYIGFVEQTPTLFEKcTLLENITLGR-SISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSG 472
Cdd:COG1132  401 GVDIRDLTLesLRRQIGVVPQDTFLFSG-TIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGErgVNLSG 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 473 GERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRsEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTH 552
Cdd:COG1132  480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTH 558

                        570
                 ....*....|....*...
gi 493533268 553 NELLKTSSEYKKLYSLQL 570
Cdd:COG1132  559 EELLARGGLYARLYRLQF 576

Name

Accession

Description

Interval

E-value

MdlB

COG1132

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

1-570

4.80e-152

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 448.84 E-value: 4.80e-152

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   1 MENEKKTVRRFVFKLFKVYWKRELLAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYF 80
Cdd:COG1132    1 MSKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  81 GEVVFETTALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFN 160
Cdd:COG1132   81 QRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVID 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 161 WKLTLLPLGFIVFSFLVIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRIAMPFAWVMNFFDRFQGDHIYAGKRF 240
Cdd:COG1132  161 WRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 241 IKSIKIAGTLKTSINGLISFSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQSWGGLLRTIEVLEA 320
Cdd:COG1132  241 ARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 321 PEEERSNSSPK-LEDVR-SISLENIAFGY-GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYIN 397
Cdd:COG1132  321 PPEIPDPPGAVpLPPVRgEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 398 GDPVSNSAL--LRPYIGFVEQTPTLFEKcTLLENITLGR-SISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSG 472
Cdd:COG1132  401 GVDIRDLTLesLRRQIGVVPQDTFLFSG-TIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGErgVNLSG 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 473 GERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRsEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTH 552
Cdd:COG1132  480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTH 558

                        570
                 ....*....|....*...
gi 493533268 553 NELLKTSSEYKKLYSLQL 570
Cdd:COG1132  559 EELLARGGLYARLYRLQF 576

MsbA_lipidA

TIGR02203

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...

19-570

4.87e-73

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: 243.86 E-value: 4.87e-73

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   19 YWKRELLAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKY--VLLVVGLWFGslIFTYFGEVVFETTALMAKSDL 96
Cdd:TIGR02203  12 YKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVplVVIGLAVLRG--ICSFVSTYLLSWVSNKVVRDI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   97 RKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFL 176
Cdd:TIGR02203  90 RVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  177 VIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRIAMPFAWVMNFFDRFQGDHiyagKRFIKSIKIAGTLKTSING 256
Cdd:TIGR02203 170 LMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRN----RRLAMKMTSAGSISSPITQ 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  257 LISFSLLAYGGYLVM----KGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQSWGGLLRTIEVLEAPEEERSNSSPkL 332
Cdd:TIGR02203 246 LIASLALAVVLFIALfqaqAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTGTRA-I 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  333 EDVRS-ISLENIAFGYGNKQI--LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--L 407
Cdd:TIGR02203 325 ERARGdVEFRNVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLasL 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  408 RPYIGFVEQTPTLFEKcTLLENITLGR--SISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARA 483
Cdd:TIGR02203 405 RRQVALVSQDVVLFND-TIANNIAYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGEngVLLSGGQRQRLAIARA 483

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  484 LVSNPRLLILDEITANIDSKTEEIIQNTLLGLRsEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYK 563
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYA 562


                  ....*..
gi 493533268  564 KLYSLQL 570
Cdd:TIGR02203 563 QLHNMQF 569

PRK10790

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

20-574

9.31e-68

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

Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 230.38 E-value: 9.31e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  20 WKRELLAAVLVGVMIALA-VVFPLLIRLLIDVVIPSGDM--DLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDL 96
Cdd:PRK10790  21 WRKPLGLAVLMLWVAAAAeVSGPLLISYFIDNMVAKGNLplGLVAGLAAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  97 RKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLgFIVFSFL 176
Cdd:PRK10790 101 RTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAI-MIFPAVL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 177 VIMFfnIMVEKRSKVEREKFGELAGVT---SNIIDNMKLI---RIAMPFAWVMNFFDRfqgDHIYAGkrfIKSIKIAGTL 250
Cdd:PRK10790 180 VVMV--IYQRYSTPIVRRVRAYLADINdgfNEVINGMSVIqqfRQQARFGERMGEASR---SHYMAR---MQTLRLDGFL 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 251 ktsINGLIS-FSLLAYGGYLVM-----KGEITVGILMTFWAYVQSLFNP-IQLLMQVNILLRQSWGGLlRTIEVLEAPEE 323
Cdd:PRK10790 252 ---LRPLLSlFSALILCGLLMLfgfsaSGTIEVGVLYAFISYLGRLNEPlIELTTQQSMLQQAVVAGE-RVFELMDGPRQ 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 324 ERSNSSPKLEDVRsISLENIAFGYGN-KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS 402
Cdd:PRK10790 328 QYGNDDRPLQSGR-IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS 406

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 403 --NSALLRPYIGFVEQTPTLFEKcTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTLVADI--QLSGGERQLV 478
Cdd:PRK10790 407 slSHSVLRQGVAMVQQDPVVLAD-TFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQgnNLSVGQKQLL 485

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 479 ALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLmVAHRLSTVLLSDRVALISNGVIVASGTHNELLKT 558
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVV-IAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564

                        570
                 ....*....|....*.
gi 493533268 559 SSEYKKLYSLQLIKDE 574
Cdd:PRK10790 565 QGRYWQMYQLQLAGEE 580

ABC_MTABC3_MDL1_MDL2

cd03249

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...

338-569

7.17e-65

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: 212.01 E-value: 7.17e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNK---QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIG 412
Cdd:cd03249    1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRdlNLRWLRSQIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTPTLFEkCTLLENITLGRSisKASLENIFERT---NLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSN 487
Cdd:cd03249   81 LVSQEPVLFD-GTIAENIRYGKP--DATDEEVEEAAkkaNIHDFIMSLPDGYDTLVGErgSQLSGGQKQRIAIARALLRN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 488 PRLLILDEITANIDSKTEEIIQNTLLGLRsEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYKKLYS 567
Cdd:cd03249  158 PKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236


                 ..
gi 493533268 568 LQ 569
Cdd:cd03249  237 AQ 238

ABC_tran

pfam00005

ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...

353-498

5.26e-37

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

Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 134.31 E-value: 5.26e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIGFVEQTPTLFEKCTLLENI 430
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTddERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268  431 TLGRSISKASLENIFERtnLDVLLRRFENG--LDTLVADI--QLSGGERQLVALARALVSNPRLLILDEITA 498
Cdd:pfam00005  81 RLGLLLKGLSKREKDAR--AEEALEKLGLGdlADRPVGERpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

346-541

3.80e-27

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 108.48 E-value: 3.80e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 346 GYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTiyingdpVSNSALLRPyiGFVEQTPTLFEK-- 423
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT-------VRRAGGARV--AYVPQRSEVPDSlp 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 424 CTLLENITLGR-----------SISKASLENIFERTNLDVLLRRfenGLDTLvadiqlSGGERQLVALARALVSNPRLLI 492
Cdd:NF040873  72 LTVRDLVAMGRwarrglwrrltRDDRAAVDDALERVGLADLAGR---QLGEL------SGGQRQRALLAQGLAQEADLLL 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 493533268 493 LDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRVALI 541
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191

GguA

NF040905

sugar ABC transporter ATP-binding protein;

353-544

5.38e-17

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.07 E-value: 5.38e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQkPQ---SGTIYINGDPVSNSALL---RPYIGFVEQTPTLFEKCTL 426
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRdseALGIVIIHQELALIPYLSI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 427 LENITLGRSISKASLENiFERTNL--DVLLRRFenGL----DTLVADIQLsgGERQLVALARALVSNPRLLILDEITANI 500
Cdd:NF040905  96 AENIFLGNERAKRGVID-WNETNRraRELLAKV--GLdespDTLVTDIGV--GKQQLVEIAKALSKDVKLLILDEPTAAL 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 493533268 501 DSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNG 544
Cdd:NF040905 171 NEEDSAALLDLLLELKAQGITSIIISHKLNEIRrVADSITVLRDG 215

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

357-501

2.77e-11

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.69 E-value: 2.77e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 357 SLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV-SNSALLRPYIGFVEQTPTLFEKCTLLENITLgrs 435
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdAGDIATRRRVGYMSQAFSLYGELTVRQNLEL--- 362

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493533268 436 isKASL-----ENIFERtnLDVLLRRF--ENGLDTLVADIQLsgGERQLVALARALVSNPRLLILDEITANID 501
Cdd:NF033858 363 --HARLfhlpaAEIAAR--VAEMLERFdlADVADALPDSLPL--GIRQRLSLAVAVIHKPELLILDEPTSGVD 429

GguA

NF040905

sugar ABC transporter ATP-binding protein;

349-548

1.45e-10

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.66 E-value: 1.45e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 349 NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQ--SGTIYINGDPVSNSALL-------------RPYIGF 413
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRniSGTVFKDGKEVDVSTVSdaidaglayvtedRKGYGL 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VeqtptlfekctLLENITlgRSISKASLENIFERTNLD-----VLLRRFENGLDTLVADI-----QLSGGERQLVALARA 483
Cdd:NF040905 352 N-----------LIDDIK--RNITLANLGKVSRRGVIDeneeiKVAEEYRKKMNIKTPSVfqkvgNLSGGNQQKVVLSKW 418

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 484 LVSNPRLLILDEITANID--SKTE--EIIQNtllgLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVA 548
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDvgAKYEiyTIINE----LAAEGKGVIVISSELPELLgMCDRIYVMNEGRITG 484

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

338-501

7.36e-09

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.60 E-value: 7.36e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLR---PYIGFV 414
Cdd:NF033858   2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRavcPRIAYM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQT------PTLfekcTLLENIT-------LGRSISKASLENIFERTNLDvllrRFengLDTLVAdiQLSGGERQLVALA 481
Cdd:NF033858  82 PQGlgknlyPTL----SVFENLDffgrlfgQDAAERRRRIDELLRATGLA----PF---ADRPAG--KLSGGMKQKLGLC 148

                        170       180
                 ....*....|....*....|
gi 493533268 482 RALVSNPRLLILDEITANID 501
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVD 168

AAA

smart00382

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...

362-547

7.92e-08

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

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.61 E-value: 7.92e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   362 KGEITTLVGESGAGKTTTLNILMG-LQKPQSGTIYINGDPVSNSALLRpyigfveqtptlfekctllenitlgrsiskas 440
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQ-------------------------------- 48

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   441 lenifertnldvllrrfENGLDTLVADIQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQ-----NTLLGL 515
Cdd:smart00382  49 -----------------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLL 111

                          170       180       190
                   ....*....|....*....|....*....|..
gi 493533268   516 RSEGIIVLMVAHRLSTVLLSDRVALISNGVIV 547
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143

40850658_otr

NF000106

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

347-555

3.62e-06

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.35 E-value: 3.62e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 347 YGNKQILKGLSLELRKGEITTLVGESGAGKTTTLnILMGLQKPQSGT-IYINGDPVSNSALLRPYIGFveQTPtlfekct 425
Cdd:NF000106  23 FGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRrPWRF*TWCANRRALRRTIG*--HRP------- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 426 llenITLGRSISKASLENIF------------ERTNLDVLLRRFENGLDTLVADIQLSGGERQLVALARALVSNPRLLIL 493
Cdd:NF000106  93 ----VR*GRRESFSGRENLYmigr*ldlsrkdARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493533268 494 DEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVIVASGTHNEL 555
Cdd:NF000106 169 DEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVIDRGRVIADGKVDEL 231

Name

Accession

Description

Interval

E-value

MdlB

COG1132

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

1-570

4.80e-152

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 448.84 E-value: 4.80e-152

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   1 MENEKKTVRRFVFKLFKVYWKRELLAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYF 80
Cdd:COG1132    1 MSKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  81 GEVVFETTALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFN 160
Cdd:COG1132   81 QRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVID 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 161 WKLTLLPLGFIVFSFLVIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRIAMPFAWVMNFFDRFQGDHIYAGKRF 240
Cdd:COG1132  161 WRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 241 IKSIKIAGTLKTSINGLISFSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQSWGGLLRTIEVLEA 320
Cdd:COG1132  241 ARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 321 PEEERSNSSPK-LEDVR-SISLENIAFGY-GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYIN 397
Cdd:COG1132  321 PPEIPDPPGAVpLPPVRgEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 398 GDPVSNSAL--LRPYIGFVEQTPTLFEKcTLLENITLGR-SISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSG 472
Cdd:COG1132  401 GVDIRDLTLesLRRQIGVVPQDTFLFSG-TIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGErgVNLSG 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 473 GERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRsEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTH 552
Cdd:COG1132  480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTH 558

                        570
                 ....*....|....*...
gi 493533268 553 NELLKTSSEYKKLYSLQL 570
Cdd:COG1132  559 EELLARGGLYARLYRLQF 576

SunT

COG2274

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...

2-570

4.96e-115

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: 357.61 E-value: 4.96e-115

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   2 ENEKKTVRRFVFKLFKVYWkRELLAAVLVGVMIAL-AVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYF 80
Cdd:COG2274  137 RGEKPFGLRWFLRLLRRYR-RLLLQVLLASLLINLlALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLL 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  81 GEVVFETTALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRlISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFN 160
Cdd:COG2274  216 RSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASR-FRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYS 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 161 WKLTLLPLGFIVFSFLVIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRIAMPFAWVMNFFDRFQGDHIYAGKRF 240
Cdd:COG2274  295 PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKL 374

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 241 IKSIKIAGTLKTSINGLISFSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQSWGGLLRTIEVLEA 320
Cdd:COG2274  375 RRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDL 454

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 321 PEEERSNSSPKLEDVR--SISLENIAFGYG--NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYI 396
Cdd:COG2274  455 PPEREEGRSKLSLPRLkgDIELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI 534

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 397 NGDPVS--NSALLRPYIGFVEQTPTLFEkCTLLENITLGR-SISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLS 471
Cdd:COG2274  535 DGIDLRqiDPASLRRQIGVVLQDVFLFS-GTIRENITLGDpDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEggSNLS 613

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 472 GGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRsEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGT 551
Cdd:COG2274  614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGT 692

                        570
                 ....*....|....*....
gi 493533268 552 HNELLKTSSEYKKLYSLQL 570
Cdd:COG2274  693 HEELLARKGLYAELVQQQL 711

CydD

COG4988

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...

5-558

2.63e-79

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: 260.08 E-value: 2.63e-79

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   5 KKTVRRFVFKLFKVYwKRELLAAVLVGVMIALAVVFP--LLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGE 82
Cdd:COG4988    1 QKPLDKRLKRLARGA-RRWLALAVLLGLLSGLLIIAQawLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  83 VVFETTALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWK 162
Cdd:COG4988   80 RAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 163 LTLLPLgfivFSFLVIMFFNIMVEKRSKVE-REKFGELAGVTSNIIDNMK---LIRIampfawvmnFF-DRFQGDHIY-A 236
Cdd:COG4988  160 SGLILL----VTAPLIPLFMILVGKGAAKAsRRQWRALARLSGHFLDRLRgltTLKL---------FGrAKAEAERIAeA 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 237 GKRFIKSikiagTLKT------SINGLISFSLLA------YGGYLVMKGEITVGILMTFWAYVQSLFNPIQLL------- 297
Cdd:COG4988  227 SEDFRKR-----TMKVlrvaflSSAVLEFFASLSialvavYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLgsfyhar 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 298 MQvnillrqswgGL--LRTI-EVLEAPEEERSNSSPKLEDVR--SISLENIAFGY-GNKQILKGLSLELRKGEITTLVGE 371
Cdd:COG4988  302 AN----------GIaaAEKIfALLDAPEPAAPAGTAPLPAAGppSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGP 371

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 372 SGAGKTTTLNILMGLQKPQSGTIYINGDPVSN--SALLRPYIGFVEQTPTLFEKcTLLENITLGR-SISKASLENIFERT 448
Cdd:COG4988  372 SGAGKSTLLNLLLGFLPPYSGSILINGVDLSDldPASWRRQIAWVPQNPYLFAG-TIRENLRLGRpDASDEELEAALEAA 450

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 449 NLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLrSEGIIVLMVA 526
Cdd:COG4988  451 GLDEFVAALPDGLDTPLGEggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILIT 529

                        570       580       590
                 ....*....|....*....|....*....|..
gi 493533268 527 HRLSTVLLSDRVALISNGVIVASGTHNELLKT 558
Cdd:COG4988  530 HRLALLAQADRILVLDDGRIVEQGTHEELLAK 561

MsbA_lipidA

TIGR02203

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...

19-570

4.87e-73

Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 243.86 E-value: 4.87e-73

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   19 YWKRELLAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKY--VLLVVGLWFGslIFTYFGEVVFETTALMAKSDL 96
Cdd:TIGR02203  12 YKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVplVVIGLAVLRG--ICSFVSTYLLSWVSNKVVRDI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   97 RKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFL 176
Cdd:TIGR02203  90 RVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  177 VIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRIAMPFAWVMNFFDRFQGDHiyagKRFIKSIKIAGTLKTSING 256
Cdd:TIGR02203 170 LMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRN----RRLAMKMTSAGSISSPITQ 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  257 LISFSLLAYGGYLVM----KGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQSWGGLLRTIEVLEAPEEERSNSSPkL 332
Cdd:TIGR02203 246 LIASLALAVVLFIALfqaqAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTGTRA-I 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  333 EDVRS-ISLENIAFGYGNKQI--LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--L 407
Cdd:TIGR02203 325 ERARGdVEFRNVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLasL 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  408 RPYIGFVEQTPTLFEKcTLLENITLGR--SISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARA 483
Cdd:TIGR02203 405 RRQVALVSQDVVLFND-TIANNIAYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGEngVLLSGGQRQRLAIARA 483

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  484 LVSNPRLLILDEITANIDSKTEEIIQNTLLGLRsEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYK 563
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYA 562


                  ....*..
gi 493533268  564 KLYSLQL 570
Cdd:TIGR02203 563 QLHNMQF 569

CydC

COG4987

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...

10-568

3.90e-70

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: 235.82 E-value: 3.90e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  10 RFVFKLFKVYWKReLLAAVLVGVMIALAVVFplLIRLlidvvipSGdmdllvkyvllvvglWFGS------LIFTYFGEV 83
Cdd:COG4987    4 LRLLRLLRPHRGR-LLLGVLLGLLTLLAGIG--LLAL-------SG---------------WLIAaaalapPILNLFVPI 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  84 V--------------FE-----TTALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQV-FPILL 143
Cdd:COG4987   59 VgvrafaigrtvfryLErlvshDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVlLPLLV 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 144 LGVVQITAILAIMFaFNWKLTLLPLGFIVFSFLVIMFFNIMVEKR-SKVEREKFGELAGVTSNIIDNMKLIRIAmpfawv 222
Cdd:COG4987  139 ALLVILAAVAFLAF-FSPALALVLALGLLLAGLLLPLLAARLGRRaGRRLAAARAALRARLTDLLQGAAELAAY------ 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 223 mNFFDRFQGDHIYAGKRFIKSIK-------IAGTLKTSINGLISFSLLAYGGYLVMKGEIT-----VGILMTFwayvqSL 290
Cdd:COG4987  212 -GALDRALARLDAAEARLAAAQRrlarlsaLAQALLQLAAGLAVVAVLWLAAPLVAAGALSgpllaLLVLAAL-----AL 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 291 FNPIQLLMQVNILLRQSWGGLLRTIEVLEAPEEERSNSSPK-LEDVRSISLENIAFGY--GNKQILKGLSLELRKGEITT 367
Cdd:COG4987  286 FEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPApAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVA 365

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 368 LVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIGFVEQTPTLFEKcTLLENITLGR-SISKASLENI 444
Cdd:COG4987  366 IVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdlDEDDLRRRIAVVPQRPHLFDT-TLRENLRLARpDATDEELWAA 444

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 445 FERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLrSEGIIV 522
Cdd:COG4987  445 LERVGLGDWLAALPDGLDTWLGEggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTV 523

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*.
gi 493533268 523 LMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYKKLYSL 568
Cdd:COG4987  524 LLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569

PRK10790

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

20-574

9.31e-68

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

Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 230.38 E-value: 9.31e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  20 WKRELLAAVLVGVMIALA-VVFPLLIRLLIDVVIPSGDM--DLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDL 96
Cdd:PRK10790  21 WRKPLGLAVLMLWVAAAAeVSGPLLISYFIDNMVAKGNLplGLVAGLAAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  97 RKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLgFIVFSFL 176
Cdd:PRK10790 101 RTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAI-MIFPAVL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 177 VIMFfnIMVEKRSKVEREKFGELAGVT---SNIIDNMKLI---RIAMPFAWVMNFFDRfqgDHIYAGkrfIKSIKIAGTL 250
Cdd:PRK10790 180 VVMV--IYQRYSTPIVRRVRAYLADINdgfNEVINGMSVIqqfRQQARFGERMGEASR---SHYMAR---MQTLRLDGFL 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 251 ktsINGLIS-FSLLAYGGYLVM-----KGEITVGILMTFWAYVQSLFNP-IQLLMQVNILLRQSWGGLlRTIEVLEAPEE 323
Cdd:PRK10790 252 ---LRPLLSlFSALILCGLLMLfgfsaSGTIEVGVLYAFISYLGRLNEPlIELTTQQSMLQQAVVAGE-RVFELMDGPRQ 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 324 ERSNSSPKLEDVRsISLENIAFGYGN-KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS 402
Cdd:PRK10790 328 QYGNDDRPLQSGR-IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS 406

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 403 --NSALLRPYIGFVEQTPTLFEKcTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTLVADI--QLSGGERQLV 478
Cdd:PRK10790 407 slSHSVLRQGVAMVQQDPVVLAD-TFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQgnNLSVGQKQLL 485

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 479 ALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLmVAHRLSTVLLSDRVALISNGVIVASGTHNELLKT 558
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVV-IAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564

                        570
                 ....*....|....*.
gi 493533268 559 SSEYKKLYSLQLIKDE 574
Cdd:PRK10790 565 QGRYWQMYQLQLAGEE 580

MsbA_rel

TIGR02204

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...

94-570

3.22e-66

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: 225.73 E-value: 3.22e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   94 SDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVF 173
Cdd:TIGR02204  91 ADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPL 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  174 SFLVIMFFNIMVEKRSkveREKFGELAGVTSNIIDNMKLIRIAMPFAWVMNFFDRFQGDHIYAGKRFIKSIKIAGTLkTS 253
Cdd:TIGR02204 171 VLLPILLFGRRVRKLS---RESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALL-TA 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  254 INGLISFS----LLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQSWGGLLRTIEVLEAPEEERSNSS 329
Cdd:TIGR02204 247 IVIVLVFGaivgVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAH 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  330 PKLEDVR---SISLENIAFGYG---NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV-- 401
Cdd:TIGR02204 327 PKTLPVPlrgEIEFEQVNFAYParpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLrq 406

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  402 SNSALLRPYIGFVEQTPTLFEKcTLLENITLGR-SISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLV 478
Cdd:TIGR02204 407 LDPAELRARMALVPQDPVLFAA-SVMENIRYGRpDATDEEVEAAARAAHAHEFISALPEGYDTYLGErgVTLSGGQRQRI 485

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  479 ALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLrSEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKT 558
Cdd:TIGR02204 486 AIARAILKDAPILLLDEATSALDAESEQLVQQALETL-MKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK 564

                         490
                  ....*....|..
gi 493533268  559 SSEYKKLYSLQL 570
Cdd:TIGR02204 565 GGLYARLARLQF 576

ABC_MTABC3_MDL1_MDL2

cd03249

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...

338-569

7.17e-65

Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 212.01 E-value: 7.17e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNK---QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIG 412
Cdd:cd03249    1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRdlNLRWLRSQIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTPTLFEkCTLLENITLGRSisKASLENIFERT---NLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSN 487
Cdd:cd03249   81 LVSQEPVLFD-GTIAENIRYGKP--DATDEEVEEAAkkaNIHDFIMSLPDGYDTLVGErgSQLSGGQKQRIAIARALLRN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 488 PRLLILDEITANIDSKTEEIIQNTLLGLRsEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYKKLYS 567
Cdd:cd03249  158 PKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236


                 ..
gi 493533268 568 LQ 569
Cdd:cd03249  237 AQ 238

ABCC_Glucan_exporter_like

cd03254

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...

338-557

6.79e-63

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: 206.31 E-value: 6.79e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNK-QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIGFV 414
Cdd:cd03254    3 IEFENVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRdiSRKSLRSMIGVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQTPTLFEKcTLLENITLGRSISKASLENI-FERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPRLL 491
Cdd:cd03254   83 LQDTFLFSG-TIMENIRLGRPNATDEEVIEaAKEAGAHDFIMKLPNGYDTVLGEngGNLSQGERQLLAIARAMLRDPKIL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 492 ILDEITANIDSKTEEIIQNTLLGLRsEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLK 557
Cdd:cd03254  162 ILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226

3a01208

TIGR00958

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

13-565

1.21e-61

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

Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 216.13 E-value: 1.21e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   13 FKLFKVYWKRELLAAVLVgVMIALAVVF-PLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALM 91
Cdd:TIGR00958 153 LGLSGRDWPWLISAFVFL-TLSSLGEMFiPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMAR 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   92 AKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFI 171
Cdd:TIGR00958 232 INLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINL 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  172 VFSFLVIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRiamPFAWVMNFFDRFQG---DHIYAGKRfiKSIKIAG 248
Cdd:TIGR00958 312 PLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVR---SFAAEEGEASRFKEaleETLQLNKR--KALAYAG 386

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  249 -TLKTSINGLISF-SLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQSWGGLLRTIEVLE-APEEER 325
Cdd:TIGR00958 387 yLWTTSVLGMLIQvLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDrKPNIPL 466

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  326 SNSSPKLEDVRSISLENIAFGYGN---KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS 402
Cdd:TIGR00958 467 TGTLAPLNLEGLIEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV 546

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  403 --NSALLRPYIGFVEQTPTLFEKcTLLENITLG-RSISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQL 477
Cdd:TIGR00958 547 qyDHHYLHRQVALVGQEPVLFSG-SVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEkgSQLSGGQKQR 625

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  478 VALARALVSNPRLLILDEITANIDSKTEEIIQNTllgLRSEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLK 557
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAECEQLLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702


                  ....*...
gi 493533268  558 TSSEYKKL 565
Cdd:TIGR00958 703 DQGCYKHL 710

NHLM_micro_ABC1

TIGR03796

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...

24-565

1.73e-60

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: 212.88 E-value: 1.73e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   24 LLAAVLVGVMIAL-AVVFPLLIRLLIDVVIPSGDMDllvkyvllvvglWFGSLIFTYFGEVVFE----------TTALMA 92
Cdd:TIGR03796 156 LLYLLLAGLLLVLpGLVIPAFSQIFVDEILVQGRQD------------WLRPLLLGMGLTALLQgvltwlqlyyLRRLEI 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   93 KSDLRK--QLLEKMFVLPFDFFHKNKTGELVSRLISDlELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGF 170
Cdd:TIGR03796 224 KLAVGMsaRFLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAF 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  171 IVFSFLVIMFFNIMVEKRSKVEREKFGELAGVTsniIDNMKLIRIAMPFAWVMNFFDRFQGDH---IYAGKRFIKSIKIA 247
Cdd:TIGR03796 303 AAINVLALQLVSRRRVDANRRLQQDAGKLTGVA---ISGLQSIETLKASGLESDFFSRWAGYQaklLNAQQELGVLTQIL 379

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  248 GTLKTSINGLISFSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQSWGGLLRTIEVLEAP----EE 323
Cdd:TIGR03796 380 GVLPTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRNPvdplLE 459

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  324 ERSNSSPKLEDVRSIS----LENIAFGYG--NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYIN 397
Cdd:TIGR03796 460 EPEGSAATSEPPRRLSgyveLRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFD 539

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  398 GDPVSN--SALLRPYIGFVEQTPTLFEkCTLLENITL-GRSISKASLEN------IfertnLDVLLRRfENGLDTLVAD- 467
Cdd:TIGR03796 540 GIPREEipREVLANSVAMVDQDIFLFE-GTVRDNLTLwDPTIPDADLVRackdaaI-----HDVITSR-PGGYDAELAEg 612

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  468 -IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEII-QNtllgLRSEGIIVLMVAHRLSTVLLSDRVALISNGV 545
Cdd:TIGR03796 613 gANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIdDN----LRRRGCTCIIVAHRLSTIRDCDEIIVLERGK 688

                         570       580
                  ....*....|....*....|
gi 493533268  546 IVASGTHNELLKTSSEYKKL 565
Cdd:TIGR03796 689 VVQRGTHEELWAVGGAYARL 708

ABCC_MRP_Like

cd03228

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...

338-544

2.15e-57

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: 189.90 E-value: 2.15e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGN--KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGF 413
Cdd:cd03228    1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLesLRKNIAY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPTLFEKcTLLENItlgrsiskaslenifertnldvllrrfengldtlvadiqLSGGERQLVALARALVSNPRLLIL 493
Cdd:cd03228   81 VPQDPFLFSG-TIRENI---------------------------------------LSGGQRQRIAIARALLRDPPILIL 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 493533268 494 DEITANIDSKTEEIIQNTLLGLRsEGIIVLMVAHRLSTVLLSDRVALISNG 544
Cdd:cd03228  121 DEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDADRIIVLDDG 170

ABCC_MsbA

cd03251

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...

338-566

2.56e-57

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: 192.06 E-value: 2.56e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQ--ILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGF 413
Cdd:cd03251    1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLasLRRQIGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPTLFEKcTLLENITLGRS-ISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPRL 490
Cdd:cd03251   81 VSQDVFLFND-TVAENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGErgVKLSGGQRQRIAIARALLKDPPI 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 491 LILDEITANIDSKTEEIIQNTLLGLrSEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYKKLY 566
Cdd:cd03251  160 LILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234

ABCC_ATM1_transporter

cd03253

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...

338-569

1.27e-55

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: 187.44 E-value: 1.27e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYG-NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGFV 414
Cdd:cd03253    1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLdsLRRAIGVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQTPTLFEKcTLLENITLGRSisKASLENIFE---RTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPR 489
Cdd:cd03253   81 PQDTVLFND-TIGYNIRYGRP--DATDEEVIEaakAAQIHDKIMRFPDGYDTIVGErgLKLSGGEKQRVAIARAILKNPP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 490 LLILDEITANIDSKTEEIIQNTLLGLrSEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYKKLYSLQ 569
Cdd:cd03253  158 ILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236

CcmA

COG1131

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

338-557

1.94e-55

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

Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 186.81 E-value: 1.94e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING-DPVSNSALLRPYIGFVEQ 416
Cdd:COG1131    1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGeDVARDPAEVRRRIGYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 TPTLFEKCTLLENITLGRSISKASLENIFERTnlDVLLRRF--ENGLDTLVAdiQLSGGERQLVALARALVSNPRLLILD 494
Cdd:COG1131   81 EPALYPDLTVRENLRFFARLYGLPRKEARERI--DELLELFglTDAADRKVG--TLSGGMKQRLGLALALLHDPELLILD 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493533268 495 EITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVIVASGTHNELLK 557
Cdd:COG1131  157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKA 220

bacteriocin_ABC

TIGR01193

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...

25-566

3.88e-54

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: 195.34 E-value: 3.88e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   25 LAAVLVgVMIALAVVFPLliRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLEKM 104
Cdd:TIGR01193 163 IAAIIV-TLISIAGSYYL--QKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHL 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  105 FVLPFDFFHKNKTGELVSRLiSDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFI-VFSFLVIMFFNI 183
Cdd:TIGR01193 240 FELPMSFFSTRRTGEIVSRF-TDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIpVYAVIIILFKRT 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  184 MvekrSKVEREKFGELAGVTSNIIDNMKLIRIAMPF---AWVMNFFDRFQGDHIYAGKRFIKSIKIAGTLKTSINGLISF 260
Cdd:TIGR01193 319 F----NKLNHDAMQANAVLNSSIIEDLNGIETIKSLtseAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNV 394

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  261 SLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQSWGGLLRTIEVLEAP-EEERSNSSPKLEDVR-SI 338
Cdd:TIGR01193 395 VILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDsEFINKKKRTELNNLNgDI 474

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  339 SLENIAFGYG-NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN--SALLRPYIGFVE 415
Cdd:TIGR01193 475 VINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDidRHTLRQFINYLP 554

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  416 QTPTLFEKcTLLENITLG--RSISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPRLL 491
Cdd:TIGR01193 555 QEPYIFSG-SILENLLLGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEegSSISGGQKQRIALARALLTDSKVL 633

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268  492 ILDEITANIDSKTEEIIQNTLLGLRSEGIIvlMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYKKLY 566
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQDKTII--FVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706

ATM1

COG5265

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...

9-569

4.09e-54

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: 193.50 E-value: 4.09e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   9 RRFVFKLFKVYWKRELLAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVV----GLWFGSLIFTYFGEVV 84
Cdd:COG5265   22 LLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLLlaygLLRLLSVLFGELRDAL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  85 FETTALMAKSDLRKQLLEKMFVLPFDFfHKN-KTGELvSRlisDLE--------LVGTVIAQVFPILLlgvvQITAILAI 155
Cdd:COG5265  102 FARVTQRAVRRLALEVFRHLHALSLRF-HLErQTGGL-SR---DIErgtkgiefLLRFLLFNILPTLL----EIALVAGI 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 156 MF-AFNWKLTLLPLG----FIVFSFLVimffnimVEKRSKVEREkfgelagvtSNIID---NMKLIRIAMPFAWVMNF-- 225
Cdd:COG5265  173 LLvKYDWWFALITLVtvvlYIAFTVVV-------TEWRTKFRRE---------MNEADseaNTRAVDSLLNYETVKYFgn 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 226 -------FDRFQGDhiYAGKRfIKSIKIAGTLKTSINGLISFSL---LAYGGYLVMKGEITVGILMTFWAYVqslfnpIQ 295
Cdd:COG5265  237 earearrYDEALAR--YERAA-VKSQTSLALLNFGQALIIALGLtamMLMAAQGVVAGTMTVGDFVLVNAYL------IQ 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 296 LLMQVNIL------LRQSWG------GLL-RTIEVLEAPEEERSNSSPKledvrSISLENIAFGY-GNKQILKGLSLELR 361
Cdd:COG5265  308 LYIPLNFLgfvyreIRQALAdmermfDLLdQPPEVADAPDAPPLVVGGG-----EVRFENVSFGYdPERPILKGVSFEVP 382

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 362 KGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGFVEQTPTLFEKcTLLENITLGR-SISK 438
Cdd:COG5265  383 AGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQasLRAAIGIVPQDTVLFND-TIAYNIAYGRpDASE 461

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 439 ASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLr 516
Cdd:COG5265  462 EEVEAAARAAQIHDFIESLPDGYDTRVGErgLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV- 540

                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493533268 517 SEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYKKLYSLQ 569
Cdd:COG5265  541 ARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593

ABC_TM1139_LivF_branched

cd03224

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...

338-556

6.22e-52

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: 177.24 E-value: 6.22e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNsalLRPY------I 411
Cdd:cd03224    1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG---LPPHeraragI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 412 GFVEQTPTLFEKCTLLENITLG-----RSISKASLENIFERtnLDVLLRRfengLDTLVAdiQLSGGERQLVALARALVS 486
Cdd:cd03224   78 GYVPEGRRIFPELTVEENLLLGayarrRAKRKARLERVYEL--FPRLKER----RKQLAG--TLSGGEQQMLAIARALMS 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493533268 487 NPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELL 556
Cdd:cd03224  150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALeIADRAYVLERGRVVLEGTAAELL 220

NatA

COG4555

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...

338-574

1.21e-51

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: 176.97 E-value: 1.21e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING-DPVSNSALLRPYIGFVEQ 416
Cdd:COG4555    2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGeDVRKEPREARRQIGVLPD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 TPTLFEKCTLLENITLGRSISKASLENIFERTnlDVLLRRFE--NGLDTLVADiqLSGGERQLVALARALVSNPRLLILD 494
Cdd:COG4555   82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRI--EELIELLGleEFLDRRVGE--LSTGMKKKVALARALVHDPKVLLLD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 495 EITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLK--TSSEYKKLYsLQLI 571
Cdd:COG4555  158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLDELREeiGEENLEDAF-VALI 236


                 ...
gi 493533268 572 KDE 574
Cdd:COG4555  237 GSE 239

LolD

COG1136

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

338-548

1.73e-51

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

Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 176.00 E-value: 1.73e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNK----QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN------SALL 407
Cdd:COG1136    5 LELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserelARLR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 408 RPYIGFVEQTPTLFEKCTLLENITLGRSISKASLENIFERtnLDVLLRRF--ENGLDTLVAdiQLSGGERQLVALARALV 485
Cdd:COG1136   85 RRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRER--ARELLERVglGDRLDHRPS--QLSGGQQQRVAIARALV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493533268 486 SNPRLLILDEITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAHRLSTVLLSDRVALISNGVIVA 548
Cdd:COG1136  161 NRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224

CydD

TIGR02857

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...

21-538

3.93e-51

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: 183.64 E-value: 3.93e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   21 KRELLAAVLVGVMIALAVVFP--LLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRK 98
Cdd:TIGR02857   2 RRALALLALLGVLGALLIIAQawLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   99 QLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLplgfIVFSFLVI 178
Cdd:TIGR02857  82 RLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLI----LLLTAPLI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  179 MFFNIMVEKR-SKVEREKFGELAGVTSNIID-------------------------------NMKLIRIAMPFAWVMNFF 226
Cdd:TIGR02857 158 PIFMILIGWAaQAAARKQWAALSRLSGHFLDrlrglptlklfgrakaqaaairrsseeyrerTMRVLRIAFLSSAVLELF 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  227 drfqgdhiyagkrfiKSIKIAGTLKTsinglISFSLLAygGYLVMKGEITVGILmtfwayVQSLFNPIQLL-------MQ 299
Cdd:TIGR02857 238 ---------------ATLSVALVAVY-----IGFRLLA--GDLDLATGLFVLLL------APEFYLPLRQLgaqyharAD 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  300 VNILLRQSWggllrtiEVLEAPEEERSNSSPKLE-DVRSISLENIAFGYGNK-QILKGLSLELRKGEITTLVGESGAGKT 377
Cdd:TIGR02857 290 GVAAAEALF-------AVLDAAPRPLAGKAPVTAaPASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKS 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  378 TTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIGFVEQTPTLFEKcTLLENITLGRS-ISKASLENIFERTNLDVLL 454
Cdd:TIGR02857 363 TLLNLLLGFVDPTEGSIAVNGVPLAdaDADSWRDQIAWVPQHPFLFAG-TIAENIRLARPdASDAEIREALERAGLDEFV 441

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  455 RRFENGLDTLVAD--IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLrSEGIIVLMVAHRLSTV 532
Cdd:TIGR02857 442 AALPQGLDTPIGEggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALA 520


                  ....*.
gi 493533268  533 LLSDRV 538
Cdd:TIGR02857 521 ALADRI 526

ZnuC

COG1121

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

338-570

4.77e-51

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

Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 175.66 E-value: 4.77e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVsnsALLRPYIGFVEQ- 416
Cdd:COG1121    7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP---RRARRRIGYVPQr 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 ------TPTlfekcTLLENITLGR-----------SISKASLENIFERTNLDVLLRRfengldtlvaDI-QLSGGERQLV 478
Cdd:COG1121   84 aevdwdFPI-----TVRDVVLMGRygrrglfrrpsRADREAVDEALERVGLEDLADR----------PIgELSGGQQQRV 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 479 ALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIvASGTHNELLk 557
Cdd:COG1121  149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVReYFDRVLLLNRGLV-AHGPPEEVL- 226

                        250
                 ....*....|...
gi 493533268 558 TSSEYKKLYSLQL 570
Cdd:COG1121  227 TPENLSRAYGGPV 239

ArpD

COG4618

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...

153-557

7.62e-51

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: 183.80 E-value: 7.62e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 153 LAIMFAFNwkltllP-LGFIVFSFLVIMF-FNIMVEKRSKVEREKFGELAGVTSNIIDNM----KLIRiAMPfawvM--N 224
Cdd:COG4618  147 LAVLFLFH------PlLGLLALVGALVLVaLALLNERLTRKPLKEANEAAIRANAFAEAAlrnaEVIE-AMG----MlpA 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 225 FFDRFQGDHIYAGKRFIKSIKIAGTLkTSINGLISFSL----LAYGGYLVMKGEITVG------ILMTFwayvqsLFNPI 294
Cdd:COG4618  216 LRRRWQRANARALALQARASDRAGGF-SALSKFLRLLLqsavLGLGAYLVIQGEITPGamiaasILMGR------ALAPI 288

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 295 QLLM----QVnILLRQSWGgllRTIEVLEA-PEEERSNSSPKLEdvRSISLENIAFGY--GNKQILKGLSLELRKGEITT 367
Cdd:COG4618  289 EQAIggwkQF-VSARQAYR---RLNELLAAvPAEPERMPLPRPK--GRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLG 362

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 368 LVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIGFVEQTPTLFEKcTLLENItlGRSiSKASLENIF 445
Cdd:COG4618  363 VIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwDREELGRHIGYLPQDVELFDG-TIAENI--ARF-GDADPEKVV 438

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 446 E---RTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGI 520
Cdd:COG4618  439 AaakLAGVHEMILRLPDGYDTRIGEggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGA 518

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 493533268 521 IVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLK 557
Cdd:COG4618  519 TVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555

ABC_6TM_exporters

cd07346

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...

24-313

5.62e-50

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: 174.28 E-value: 5.62e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLEK 103
Cdd:cd07346    2 LLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 104 MFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIMFFNI 183
Cdd:cd07346   82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 184 MVEKRSKVEREKFGELAGVTSNIIDNMKLIRIAMPFAWVMNFFDRFQGDHIYAGKRFIKSIKIAGTLKTSINGLISFSLL 263
Cdd:cd07346  162 RIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVL 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 493533268 264 AYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQSWGGLLR 313
Cdd:cd07346  242 LYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLER 291

ABC_MJ0796_LolCDE_FtsE

cd03255

ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...

338-546

1.76e-49

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: 170.36 E-value: 1.76e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGN----KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN------SALL 407
Cdd:cd03255    1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekelAAFR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 408 RPYIGFVEQTPTLFEKCTLLENITLGRSISKASLENIFERtnLDVLLRRF--ENGLDTLVAdiQLSGGERQLVALARALV 485
Cdd:cd03255   81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRER--AEELLERVglGDRLNHYPS--ELSGGQQQRVAIARALA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268 486 SNPRLLILDEITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAHRLSTVLLSDRVALISNGVI 546
Cdd:cd03255  157 NDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218

CydC

TIGR02868

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...

76-529

1.33e-48

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.

Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 176.78 E-value: 1.33e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   76 IFTYFGEVVFETTALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQV-FPILLLGVVQITAILA 154
Cdd:TIGR02868  68 VFRYLERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRViVPAGVALVVGAAAVAA 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  155 ImFAFNWKLTLLPLGFIVFSFLVIMFFNIMVEKRSKV-EREKFGELAGVTSNIIDNMKLIRIAMPFAWVMNFFDRFQGDH 233
Cdd:TIGR02868 148 I-AVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQaLARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADREL 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  234 IYAGKRFIKSIKIAGTLKTSINGLISFSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQSWGGLLR 313
Cdd:TIGR02868 227 TRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAER 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  314 TIEVLEAPEEERSNSSPKLEDVRS----ISLENIAFGY-GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQK 388
Cdd:TIGR02868 307 IVEVLDAAGPVAEGSAPAAGAVGLgkptLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD 386

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  389 PQSGTIYINGDPVS--NSALLRPYIGFVEQTPTLFEKcTLLENITLGR-SISKASLENIFERTNLDVLLRRFENGLDTLV 465
Cdd:TIGR02868 387 PLQGEVTLDGVPVSslDQDEVRRRVSVCAQDAHLFDT-TVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTVL 465

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268  466 AD--IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLrSEGIIVLMVAHRL 529
Cdd:TIGR02868 466 GEggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA-LSGRTVVLITHHL 530

EcfA2

COG1122

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...

338-557

2.47e-48

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: 167.89 E-value: 2.47e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGY-GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGFV 414
Cdd:COG1122    1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLreLRRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQTPT--LFEKcTLLENITLGrsiskasLEN-------IFERTnlDVLLRRFenGLDTLvADI---QLSGGERQLVALAR 482
Cdd:COG1122   81 FQNPDdqLFAP-TVEEDVAFG-------PENlglpreeIRERV--EEALELV--GLEHL-ADRpphELSGGQKQRVAIAG 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 483 ALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLK 557
Cdd:COG1122  148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPREVFS 223

ABC_DR_subfamily_A

cd03230

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...

338-546

3.20e-48

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: 165.65 E-value: 3.20e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING-DPVSNSALLRPYIGFVEQ 416
Cdd:cd03230    1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkDIKKEPEEVKRRIGYLPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 TPTLFEKCTLLENitlgrsiskaslenifertnldvllrrfengldtlvadIQLSGGERQLVALARALVSNPRLLILDEI 496
Cdd:cd03230   81 EPSLYENLTVREN--------------------------------------LKLSGGMKQRLALAQALLHDPELLILDEP 122

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 493533268 497 TANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVI 546
Cdd:cd03230  123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173

ABC_Carb_Solutes_like

cd03259

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...

338-550

5.25e-48

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: 166.54 E-value: 5.25e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLRPYIGFVEQT 417
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PTLFEKCTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTLVAdiQLSGGERQLVALARALVSNPRLLILDEIT 497
Cdd:cd03259   81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPH--ELSGGQQQRVALARALAREPSLLLLDEPL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 498 ANIDSKTEEIIQNTLLGL-RSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASG 550
Cdd:cd03259  159 SALDAKLREELREELKELqRELGITTIYVTHDQEEALaLADRIAVMNEGRIVQVG 213

FepC

COG1120

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...

338-556

1.14e-47

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: 166.76 E-value: 1.14e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNsalLRP-----YIG 412
Cdd:COG1120    2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS---LSRrelarRIA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTPTLFEKCTLLENITLGR--------SISKASLE---NIFERTNLDVLLRRFengLDTLvadiqlSGGERQLVALA 481
Cdd:COG1120   79 YVPQEPPAPFGLTVRELVALGRyphlglfgRPSAEDREaveEALERTGLEHLADRP---VDEL------SGGERQRVLIA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 482 RALVSNPRLLILDEITANIDskteeiIQNT--LLGL-----RSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHN 553
Cdd:COG1120  150 RALAQEPPLLLLDEPTSHLD------LAHQleVLELlrrlaRERGRTVVMVLHDLNLAArYADRLVLLKDGRIVAQGPPE 223


                 ...
gi 493533268 554 ELL 556
Cdd:COG1120  224 EVL 226

LivF

COG0410

ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...

339-556

2.93e-47

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: 165.16 E-value: 2.93e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 339 SLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNsalLRPY------IG 412
Cdd:COG0410    5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG---LPPHriarlgIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTPTLFEKCTLLENITLG------RSISKASLENIFERtnLDVLLRRfengLDTLVAdiQLSGGERQLVALARALVS 486
Cdd:COG0410   82 YVPEGRRIFPSLTVEENLLLGayarrdRAEVRADLERVYEL--FPRLKER----RRQRAG--TLSGGEQQMLAIGRALMS 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 487 NPRLLILDEITA----NIdskTEEIIQnTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELL 556
Cdd:COG0410  154 RPKLLLLDEPSLglapLI---VEEIFE-IIRRLNREGVTILLVEQNARFALeIADRAYVLERGRIVLEGTAAELL 224

ABCC_bacteriocin_exporters

cd03245

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...

337-550

1.27e-46

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: 162.76 E-value: 1.27e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGNKQI--LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIG 412
Cdd:cd03245    2 RIEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPADLRRNIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTPTLFeKCTLLENITLGR-SISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPR 489
Cdd:cd03245   82 YVPQDVTLF-YGTLRDNITLGApLADDERILRAAELAGVTDFVNKHPNGLDLQIGErgRGLSGGQRQAVALARALLNDPP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268 490 LLILDEITANIDSKTEE-IIQNTLLGLRseGIIVLMVAHRLSTVLLSDRVALISNGVIVASG 550
Cdd:cd03245  161 ILLLDEPTSAMDMNSEErLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220

ABCC_Hemolysin

cd03252

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...

338-569

1.32e-46

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: 163.43 E-value: 1.32e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYG--NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIGF 413
Cdd:cd03252    1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAlaDPAWLRRQVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPTLFEKcTLLENITLGRSisKASLENIFERTNL---DVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNP 488
Cdd:cd03252   81 VLQENVLFNR-SIRDNIALADP--GMSMERVIEAAKLagaHDFISELPEGYDTIVGEqgAGLSGGQRQRIAIARALIHNP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 489 RLLILDEITANIDSKTEEIIQNTLLGLrSEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYKKLYSL 568
Cdd:cd03252  158 RILIFDEATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236


                 .
gi 493533268 569 Q 569
Cdd:cd03252  237 Q 237

PotA

COG3842

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...

337-551

1.70e-46

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

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 166.81 E-value: 1.70e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNsalLRPY---IGF 413
Cdd:COG3842    5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG---LPPEkrnVGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPTLFEKCTLLENITLG---RSISKA----SLENIFERTNLDVLLRRFENgldtlvadiQLSGGERQLVALARALVS 486
Cdd:COG3842   82 VFQDYALFPHLTVAENVAFGlrmRGVPKAeiraRVAELLELVGLEGLADRYPH---------QLSGGQQQRVALARALAP 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268 487 NPRLLILDEITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGT 551
Cdd:COG3842  153 EPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALaLADRIAVMNDGRIEQVGT 219

PRK13657

glucan ABC transporter ATP-binding protein/ permease;

15-556

8.57e-46

glucan ABC transporter ATP-binding protein/ permease;

Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 170.14 E-value: 8.57e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  15 LFKVYW-------KRELLAAVLVGVMIALAVVF---PLLIRLLIDVVIPSGDMdllvkyvLLVVGLWFGsliFTYFGEVV 84
Cdd:PRK13657   3 LFRLYArvlqylgAEKRLGILLAVANVLLAAATfaePILFGRIIDAISGKGDI-------FPLLAAWAG---FGLFNIIA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  85 FETTALMA-------KSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMF 157
Cdd:PRK13657  73 GVLVARHAdrlahrrRLAVLTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLAL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 158 AFNWKLTLLPLGF-IVFSFLvimffNIMVEKRSK-----VErEKFGELAGVTSNIIDNMKLIRIampfawvmnfFDRFQG 231
Cdd:PRK13657 153 FMNWRLSLVLVVLgIVYTLI-----TTLVMRKTKdgqaaVE-EHYHDLFAHVSDAIGNVSVVQS----------YNRIEA 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 232 DhIYAGKRFIKSIKIAGT-------LKTSINGLIS-FSLLA---YGGYLVMKGEITVGILMTFWAYVQSLfnpIQLLMQV 300
Cdd:PRK13657 217 E-TQALRDIADNLLAAQMpvlswwaLASVLNRAAStITMLAilvLGAALVQKGQLRVGEVVAFVGFATLL---IGRLDQV 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 301 ----NILLRQSwGGLLRTIEVLEA-PEEERSNSSPKLEDVR-SISLENIAFGYGNK-QILKGLSLELRKGEITTLVGESG 373
Cdd:PRK13657 293 vafiNQVFMAA-PKLEEFFEVEDAvPDVRDPPGAIDLGRVKgAVEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTG 371

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 374 AGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIGFVEQTPTLFEKcTLLENITLGR-SISKASLENIFERTN- 449
Cdd:PRK13657 372 AGKSTLINLLQRVFDPQSGRILIDGTDIRtvTRASLRRNIAVVFQDAGLFNR-SIEDNIRVGRpDATDEEMRAAAERAQa 450

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 450 LDVLLRRfENGLDTLVAD--IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRsEGIIVLMVAH 527
Cdd:PRK13657 451 HDFIERK-PDGYDTVVGErgRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAH 528

                        570       580
                 ....*....|....*....|....*....
gi 493533268 528 RLSTVLLSDRVALISNGVIVASGTHNELL 556
Cdd:PRK13657 529 RLSTVRNADRILVFDNGRVVESGSFDELV 557

MlaF

COG1127

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...

338-562

8.72e-46

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: 161.30 E-value: 8.72e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV---SNSAL--LRPYIG 412
Cdd:COG1127    6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglSEKELyeLRRRIG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTPTLFEKCTLLENITLG-RSISKASLENIFERTNLdvLLRRFenGLDTlVADI---QLSGGERQLVALARALVSNP 488
Cdd:COG1127   86 MLFQGGALFDSLTVFENVAFPlREHTDLSEAEIRELVLE--KLELV--GLPG-AADKmpsELSGGMRKRVALARALALDP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 489 RLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLKTSSEY 562
Cdd:COG1127  161 EILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFaIADRVAVLADGKIIAEGTPEELLASDDPW 236

PRK11176

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

96-570

8.96e-46

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

Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 170.20 E-value: 8.96e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  96 LRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVfpilLLGVVQ----ITAILAIMFAFNWKLTLlplgfI 171
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGA----LITVVRegasIIGLFIMMFYYSWQLSL-----I 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 172 VFSFLVIMFFNI-MVEKR----SKVEREKFGELAGVTSNIIDNMKLIRIampfawvmnffdrFQGDHIyAGKRF------ 240
Cdd:PRK11176 171 LIVIAPIVSIAIrVVSKRfrniSKNMQNTMGQVTTSAEQMLKGHKEVLI-------------FGGQEV-ETKRFdkvsnr 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 241 --IKSIKIAGTLKTSiNGLISF--SL-LAYGGYLV----MKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQSWGGL 311
Cdd:PRK11176 237 mrQQGMKMVSASSIS-DPIIQLiaSLaLAFVLYAAsfpsVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAAC 315

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 312 LRTIEVLEApEEERSNSSPKLEDVR-SISLENIAFGYGNKQI--LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQK 388
Cdd:PRK11176 316 QTLFAILDL-EQEKDEGKRVIERAKgDIEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYD 394

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 389 PQSGTIYINGDPVSNSAL--LRPYIGFVEQTPTLFEKcTLLENITLGRS--ISKASLENIFERTNLDVLLRRFENGLDTL 464
Cdd:PRK11176 395 IDEGEILLDGHDLRDYTLasLRNQVALVSQNVHLFND-TIANNIAYARTeqYSREQIEEAARMAYAMDFINKMDNGLDTV 473

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 465 VAD--IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIiVLMVAHRLSTVLLSDRVALIS 542
Cdd:PRK11176 474 IGEngVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRT-SLVIAHRLSTIEKADEILVVE 552

                        490       500
                 ....*....|....*....|....*...
gi 493533268 543 NGVIVASGTHNELLKTSSEYKKLYSLQL 570
Cdd:PRK11176 553 DGEIVERGTHAELLAQNGVYAQLHKMQF 580

ABC_cobalt_CbiO_domain1

cd03225

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...

339-544

9.66e-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: 160.33 E-value: 9.66e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 339 SLENIAFGYGN--KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGFV 414
Cdd:cd03225    1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkeLRRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQ-------TPTLFEKCTL-LENITLGRSISKASLENIFERTNLDVLLRRfengldtlvaDI-QLSGGERQLVALARALV 485
Cdd:cd03225   81 FQnpddqffGPTVEEEVAFgLENLGLPEEEIEERVEEALELVGLEGLRDR----------SPfTLSGGQKQRVAIAGVLA 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 486 SNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNG 544
Cdd:cd03225  151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLeLADRVIVLEDG 210

ABC_Metallic_Cations

cd03235

ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...

339-550

1.02e-45

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: 160.39 E-value: 1.02e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 339 SLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSallRPYIGFVEQTp 418
Cdd:cd03235    1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE---RKRIGYVPQR- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 419 TLFEKC---TLLENITLGR-----------SISKASLENIFERTNL-DVLLRRFEngldtlvadiQLSGGERQLVALARA 483
Cdd:cd03235   77 RSIDRDfpiSVRDVVLMGLyghkglfrrlsKADKAKVDEALERVGLsELADRQIG----------ELSGGQQQRVLLARA 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 484 LVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALIsNGVIVASG 550
Cdd:cd03235  147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLeYFDRVLLL-NRTVVASG 213

GsiA

COG1123

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...

312-556

1.10e-45

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: 168.54 E-value: 1.10e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 312 LRTIEVLEAPEEERSNSSPKLEDVrsISLENIAFGYGNK-----QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGL 386
Cdd:COG1123  237 LAAVPRLGAARGRAAPAAAAAEPL--LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 387 QKPQSGTIYINGDPVSN-----SALLRPYIGFVEQTPT--LFEKCTLLENITLG----RSISKASLEnifERTnlDVLLR 455
Cdd:COG1123  315 LRPTSGSILFDGKDLTKlsrrsLRELRRRVQMVFQDPYssLNPRMTVGDIIAEPlrlhGLLSRAERR---ERV--AELLE 389

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 456 RFenGLDTLVADI---QLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLST 531
Cdd:COG1123  390 RV--GLPPDLADRyphELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAV 467

                        250       260
                 ....*....|....*....|....*.
gi 493533268 532 VL-LSDRVALISNGVIVASGTHNELL 556
Cdd:COG1123  468 VRyIADRVAVMYDGRIVEDGPTEEVF 493

ABCC_MRP_domain2

cd03244

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...

337-551

3.80e-45

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: 158.81 E-value: 3.80e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGN--KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIG 412
Cdd:cd03244    2 DIEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLhdLRSRIS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTPTLFEKcTLLENI-TLGRSiSKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPR 489
Cdd:cd03244   82 IIPQDPVLFSG-TIRSNLdPFGEY-SDEELWQALERVGLKEFVESLPGGLDTVVEEggENLSVGQRQLLCLARALLRKSK 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493533268 490 LLILDEITANIDSKTEEIIQNTllgLRSE--GIIVLMVAHRLSTVLLSDRVALISNGVIVASGT 551
Cdd:cd03244  160 ILVLDEATASVDPETDALIQKT---IREAfkDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220

ABC_Org_Solvent_Resistant

cd03261

ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...

338-562

4.33e-45

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: 159.20 E-value: 4.33e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV---SNSAL--LRPYIG 412
Cdd:cd03261    1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELyrLRRRMG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTPTLFEKCTLLENITLG-RSISKASLENIFERTNLD---VLLRRFENGLDTlvadiQLSGGERQLVALARALVSNP 488
Cdd:cd03261   81 MLFQSGALFDSLTVFENVAFPlREHTRLSEEEIREIVLEKleaVGLRGAEDLYPA-----ELSGGMKKRVALARALALDP 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 489 RLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLKTSSEY 562
Cdd:cd03261  156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFaIADRIAVLYDGKIVAEGTPEELRASDDPL 231

ABC_Iron-Siderophores_B12_Hemin

cd03214

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...

339-550

4.47e-45

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: 157.21 E-value: 4.47e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 339 SLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN--SALLRPYIGFVEQ 416
Cdd:cd03214    1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlsPKELARKIAYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 tptlfekctllenitlgrsiskaslenIFERTNLDVLLRRFENgldtlvadiQLSGGERQLVALARALVSNPRLLILDEI 496
Cdd:cd03214   81 ---------------------------ALELLGLAHLADRPFN---------ELSGGERQRVLLARALAQEPPILLLDEP 124

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 497 TANIDSKTeeiiQNTLLGL-----RSEGIIVLMVAHRLSTVLL-SDRVALISNGVIVASG 550
Cdd:cd03214  125 TSHLDIAH----QIELLELlrrlaRERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180

TauB

COG1116

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...

338-544

6.26e-45

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

Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 159.48 E-value: 6.26e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGY----GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNsalLRPYIGF 413
Cdd:COG1116    8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG---PGPDRGV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPTLFEKCTLLENITLGRSISKASLENIFERTnlDVLLRRFenGL----DTLVAdiQLSGGERQLVALARALVSNPR 489
Cdd:COG1116   85 VFQEPALLPWLTVLDNVALGLELRGVPKAERRERA--RELLELV--GLagfeDAYPH--QLSGGMRQRVAIARALANDPE 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268 490 LLILDEITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAHRLS-TVLLSDRVALISNG 544
Cdd:COG1116  159 VLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDeAVFLADRVVVLSAR 215

ABC_NrtD_SsuB_transporters

cd03293

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...

338-543

6.46e-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: 158.40 E-value: 6.46e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQ----ILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSallRPYIGF 413
Cdd:cd03293    1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP---GPDRGY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPTLFEKCTLLENITLG---RSISKASLENIFERTNLDVLLRRFENGLDTlvadiQLSGGERQLVALARALVSNPRL 490
Cdd:cd03293   78 VFQQDALLPWLTVLDNVALGlelQGVPKAEARERAEELLELVGLSGFENAYPH-----QLSGGMRQRVALARALAVDPDV 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 491 LILDEITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAHRLS-TVLLSDRVALISN 543
Cdd:cd03293  153 LLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDeAVFLADRVVVLSA 207

DppF

COG1124

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...

338-562

5.66e-44

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: 156.89 E-value: 5.66e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYG----NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYI 411
Cdd:COG1124    2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkaFRRRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 412 GFVEQTP--------TLFEkcTLLENITL-GRSISKASLENIFERTNLDV-LLRRFENgldtlvadiQLSGGERQLVALA 481
Cdd:COG1124   82 QMVFQDPyaslhprhTVDR--ILAEPLRIhGLPDREERIAELLEQVGLPPsFLDRYPH---------QLSGGQRQRVAIA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 482 RALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLK-T 558
Cdd:COG1124  151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAhLCDRVAVMQNGRIVEELTVADLLAgP 230


                 ....
gi 493533268 559 SSEY 562
Cdd:COG1124  231 KHPY 234

ABCC_Protease_Secretion

cd03246

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...

338-546

1.53e-43

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: 153.14 E-value: 1.53e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQ--ILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIGF 413
Cdd:cd03246    1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwDPNELGDHVGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPTLFEKcTLLENItlgrsiskaslenifertnldvllrrfengldtlvadiqLSGGERQLVALARALVSNPRLLIL 493
Cdd:cd03246   81 LPQDDELFSG-SIAENI---------------------------------------LSGGQRQRLGLARALYGNPRILVL 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493533268 494 DEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRVALISNGVI 546
Cdd:cd03246  121 DEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173

ABC_Class3

cd03229

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...

338-544

4.40e-43

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 151.96 E-value: 4.40e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV----SNSALLRPYIGF 413
Cdd:cd03229    1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdleDELPPLRRRIGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPTLFEKCTLLENITLGrsiskaslenifertnldvllrrfengldtlvadiqLSGGERQLVALARALVSNPRLLIL 493
Cdd:cd03229   81 VFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALARALAMDPDVLLL 124

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493533268 494 DEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNG 544
Cdd:cd03229  125 DEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAArLADRVVVLRDG 177

ABCC_TAP

cd03248

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...

338-546

1.14e-42

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: 152.62 E-value: 1.14e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNK---QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIG 412
Cdd:cd03248   12 VKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqyEHKYLHSKVS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTPTLFEKcTLLENITLGrsISKASLENIFE---RTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSN 487
Cdd:cd03248   92 LVGQEPVLFAR-SLQDNIAYG--LQSCSFECVKEaaqKAHAHSFISELASGYDTEVGEkgSQLSGGQKQRVAIARALIRN 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493533268 488 PRLLILDEITANIDSKTEEIIQNTLLGlRSEGIIVLMVAHRLSTVLLSDRVALISNGVI 546
Cdd:cd03248  169 PQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVERADQILVLDGGRI 226

ABC_NikE_OppD_transporters

cd03257

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...

338-550

1.14e-42

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: 152.66 E-value: 1.14e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNK----QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNS-----ALLR 408
Cdd:cd03257    2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrlrKIRR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 409 PYIGFVEQTP--------TLFEkcTLLENITLGRSISKASLENIFERTNLDVLlrrfenGLDTLVAD---IQLSGGERQL 477
Cdd:cd03257   82 KEIQMVFQDPmsslnprmTIGE--QIAEPLRIHGKLSKKEARKEAVLLLLVGV------GLPEEVLNrypHELSGGQRQR 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 478 VALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASG 550
Cdd:cd03257  154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAkIADRVAVMYAGKIVEEG 228

FetA

COG4619

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

338-546

1.20e-42

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

Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 151.89 E-value: 1.20e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGFVE 415
Cdd:COG4619    1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpeWRRQVAYVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 416 QTPTLFEKcTLLENITLGRSISKASleniFERTNLDVLLRRFENGLDTLVADI-QLSGGERQLVALARALVSNPRLLILD 494
Cdd:COG4619   81 QEPALWGG-TVRDNLPFPFQLRERK----FDRERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPDVLLLD 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493533268 495 EITANIDSKTEEIIQNTLLGLR-SEGIIVLMVAH------RlstvlLSDRVALISNGVI 546
Cdd:COG4619  156 EPTSALDPENTRRVEELLREYLaEEGRAVLWVSHdpeqieR-----VADRVLTLEAGRL 209

ABC_PstB_phosphate_transporter

cd03260

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...

338-555

1.31e-42

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: 152.33 E-value: 1.31e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGL-----QKPQSGTIYINGDPVSNSA----LLR 408
Cdd:cd03260    1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDvdvlELR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 409 PYIGFVEQTPTLFEKcTLLENITLG----RSISKASLENIFErtnldVLLRR---FENGLDTLVADiQLSGGERQLVALA 481
Cdd:cd03260   81 RRVGMVFQKPNPFPG-SIYDNVAYGlrlhGIKLKEELDERVE-----EALRKaalWDEVKDRLHAL-GLSGGQQQRLCLA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 482 RALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEgIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNEL 555
Cdd:cd03260  154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAArVADRTAFLLNGRLVEFGPTEQI 227

ABC_YhbG

cd03218

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...

338-566

2.92e-40

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: 146.15 E-value: 2.92e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL---LRPYIGFV 414
Cdd:cd03218    1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhkrARLGIGYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQTPTLFEKCTLLENITLGRSISKASLENIFERtnLDVLLRRFenGLDTLVAD--IQLSGGERQLVALARALVSNPRLLI 492
Cdd:cd03218   81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEK--LEELLEEF--HITHLRKSkaSSLSGGERRRVEIARALATNPKFLL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 493 LDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLkTSSEYKKLY 566
Cdd:cd03218  157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLsITDRAYIIYEGKVLAEGTPEEIA-ANELVRKVY 230

ABC_ATPase

cd00267

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...

339-544

3.59e-40

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: 143.15 E-value: 3.59e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 339 SLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGFVeq 416
Cdd:cd00267    1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeeLRRRIGYV-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 tptlfekctllenitlgrsiskaslenifertnldvllrrfengldtlvadIQLSGGERQLVALARALVSNPRLLILDEI 496
Cdd:cd00267   79 ---------------------------------------------------PQLSGGQRQRVALARALLLNPDLLLLDEP 107

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 493533268 497 TANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNG 544
Cdd:cd00267  108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAeLAADRVIVLKDG 156

MglA

COG1129

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

338-555

4.19e-40

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 152.48 E-value: 4.19e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNS---ALLRPYIGFV 414
Cdd:COG1129    5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRsprDAQAAGIAII 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQTPTLFEKCTLLENITLGRSISKASL----------ENIFERTNLDVllrrfenGLDTLVADiqLSGGERQLVALARAL 484
Cdd:COG1129   85 HQELNLVPNLSVAENIFLGREPRRGGLidwramrrraRELLARLGLDI-------DPDTPVGD--LSVAQQQLVEIARAL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268 485 VSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNEL 555
Cdd:COG1129  156 SRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFeIADRVTVLRDGRLVGTGPVAEL 227

LptB

COG1137

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...

338-566

4.42e-40

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

Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 145.94 E-value: 4.42e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNsalLRPY------I 411
Cdd:COG1137    4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH---LPMHkrarlgI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 412 GFVEQTPTLFEKCTLLENITLGRSISKASLENIFERtnLDVLLRRFenGLdTLVAD---IQLSGGERQLVALARALVSNP 488
Cdd:COG1137   81 GYLPQEASIFRKLTVEDNILAVLELRKLSKKEREER--LEELLEEF--GI-THLRKskaYSLSGGERRRVEIARALATNP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 489 RLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHR----LSTVllsDRVALISNGVIVASGTHNELLKtSSEYKK 564
Cdd:COG1137  156 KFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNvretLGIC---DRAYIISEGKVLAEGTPEEILN-NPLVRK 231


                 ..
gi 493533268 565 LY 566
Cdd:COG1137  232 VY 233

MalK

COG3839

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

337-555

7.28e-40

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

Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 148.68 E-value: 7.28e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNsalLRPY---IGF 413
Cdd:COG3839    3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD---LPPKdrnIAM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPTLFEKCTLLENITLG---RSISKAS----LENIFERTNLDVLLRRfengldtLVAdiQLSGGERQLVALARALVS 486
Cdd:COG3839   80 VFQSYALYPHMTVYENIAFPlklRKVPKAEidrrVREAAELLGLEDLLDR-------KPK--QLSGGQRQRVALGRALVR 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268 487 NPRLLILDEITANIDSKT-----EEI--IQNTLlglrseGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNEL 555
Cdd:COG3839  151 EPKVFLLDEPLSNLDAKLrvemrAEIkrLHRRL------GTTTIYVTHDQVEAMtLADRIAVMNDGRIQQVGTPEEL 221

PRK11174

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

316-567

1.18e-39

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

Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 152.69 E-value: 1.18e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 316 EVLEAPEEERSNSSPKLEDVRSISLEN---IAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQkPQSG 392
Cdd:PRK11174 326 TFLETPLAHPQQGEKELASNDPVTIEAedlEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQG 404

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 393 TIYINGDPVSNSAL--LRPYIGFVEQTPTLFEKcTLLENITLGRS-ISKASLENIFERTNLDVLLRRFENGLDTLVAD-- 467
Cdd:PRK11174 405 SLKINGIELRELDPesWRKHLSWVGQNPQLPHG-TLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDqa 483

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 468 IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLrSEGIIVLMVAHRLSTVLLSDRVALISNGVIV 547
Cdd:PRK11174 484 AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA-SRRQTTLMVTHQLEDLAQWDQIWVMQDGQIV 562

                        250       260
                 ....*....|....*....|
gi 493533268 548 ASGTHNELLKTSSEYKKLYS 567
Cdd:PRK11174 563 QQGDYAELSQAGGLFATLLA 582

ABC_6TM_TmrA_like

cd18544

Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...

24-303

1.63e-39

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: 145.99 E-value: 1.63e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALAVVFPLLIRLLIDVVI--PSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLL 101
Cdd:cd18544    2 ILALLLLLLATALELLGPLLIKRAIDDYIvpGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 102 EKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIMFF 181
Cdd:cd18544   82 SHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLF 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 182 NIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRIampF---AWVMNFFDRFQGDHIYAGkrfIKSIKIAGTLKTSINGLI 258
Cdd:cd18544  162 RKKSRKAYREVREKLSRLNAFLQESISGMSVIQL---FnreKREFEEFDEINQEYRKAN---LKSIKLFALFRPLVELLS 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 493533268 259 SFSL---LAYGGYLVMKGEITVGILMTFWAYVQSLFNPI-QLLMQVNIL 303
Cdd:cd18544  236 SLALalvLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIrDLAEKFNIL 284

FtsE

COG2884

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

338-550

1.80e-39

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

Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 143.65 E-value: 1.80e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQ-ILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN-----SALLRPYI 411
Cdd:COG2884    2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrreIPYLRRRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 412 GFVEQTPTLFEKCTLLENITLGRSISKASLENIFERTNLdvLLRRFenGLDTLvAD---IQLSGGERQLVALARALVSNP 488
Cdd:COG2884   82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVRE--VLDLV--GLSDK-AKalpHELSGGEQQRVAIARALVNRP 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493533268 489 RLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVIVASG 550
Cdd:COG2884  157 ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVdRMPKRVLELEDGRLVRDE 219

GlnQ

COG1126

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...

338-551

9.63e-39

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

Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 142.06 E-value: 9.63e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNS----ALLRPYIGF 413
Cdd:COG1126    2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSkkdiNKLRRKVGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPTLFEKCTLLENITLG----RSISKASLENIFERtnldvLLRRFenGLdtlvAD------IQLSGGERQLVALARA 483
Cdd:COG1126   82 VFQQFNLFPHLTVLENVTLApikvKKMSKAEAEERAME-----LLERV--GL----ADkadaypAQLSGGQQQRVAIARA 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493533268 484 LVSNPRLLILDEITANIDSkteEIIQ---NTLLGLRSEGIIVLMVAHRLS---TVllSDRVALISNGVIVASGT 551
Cdd:COG1126  151 LAMEPKVMLFDEPTSALDP---ELVGevlDVMRDLAKEGMTMVVVTHEMGfarEV--ADRVVFMDGGRIVEEGP 219

ABC_PotA_N

cd03300

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...

338-555

9.75e-39

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: 141.99 E-value: 9.75e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNsalLRPY---IGFV 414
Cdd:cd03300    1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN---LPPHkrpVNTV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQTPTLFEKCTLLENITLGRSISKASLENIFER-------TNLDVLLRRFENgldtlvadiQLSGGERQLVALARALVSN 487
Cdd:cd03300   78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERvaealdlVQLEGYANRKPS---------QLSGGQQQRVAIARALVNE 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 488 PRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNEL 555
Cdd:cd03300  149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALtMSDRIAVMNKGKIQQIGTPEEI 218

CcmA

COG4133

ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...

338-540

1.26e-38

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: 140.69 E-value: 1.26e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL-LRPYIGFVEQ 416
Cdd:COG4133    3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdYRRRLAYLGH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 TPTLFEKCTLLENITL-----GRSISKASLENIFERTNLDVLlrrfengLDTLVAdiQLSGGERQLVALARALVSNPRLL 491
Cdd:COG4133   83 ADGLKPELTVRENLRFwaalyGLRADREAIDEALEAVGLAGL-------ADLPVR--QLSAGQKRRVALARLLLSPAPLW 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 493533268 492 ILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRVAL 540
Cdd:COG4133  154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDL 202

ABC_HisP_GlnQ

cd03262

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...

338-546

1.54e-38

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.

Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 140.74 E-value: 1.54e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNS----ALLRPYIGF 413
Cdd:cd03262    1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDkkniNELRQKVGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPTLFEKCTLLENITLG----RSISKASLENIFERtnldvLLRRFenGLDTlVAD---IQLSGGERQLVALARALVS 486
Cdd:cd03262   81 VFQQFNLFPHLTVLENITLApikvKGMSKAEAEERALE-----LLEKV--GLAD-KADaypAQLSGGQQQRVAIARALAM 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493533268 487 NPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVI 546
Cdd:cd03262  153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAReVADRVIFMDDGRI 213

ABC_Mj1267_LivG_branched

cd03219

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...

353-551

2.16e-38

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: 141.04 E-value: 2.16e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNsalLRPY------IGFVEQTPTLFEKCTL 426
Cdd:cd03219   16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG---LPPHeiarlgIGRTFQIPRLFPELTV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 427 LENITLG-RSISKASLENIFERTNLDVLLRRFENGLDTL----VADIQ---LSGGERQLVALARALVSNPRLLILDEITA 498
Cdd:cd03219   93 LENVMVAaQARTGSGLLLARARREEREARERAEELLERVgladLADRPageLSYGQQRRLEIARALATDPKLLLLDEPAA 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493533268 499 NIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGT 551
Cdd:cd03219  173 GLNPEETEELAELIRELRERGITVLLVEHDMDVVMsLADRVTVLDQGRVIAEGT 226

ABC_Carb_Monos_I

cd03216

First domain of the ATP-binding cassette component of monosaccharide transport system; This ...

338-549

2.60e-38

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: 138.33 E-value: 2.60e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSallrpyigfveqT 417
Cdd:cd03216    1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA------------S 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PTlfekctllENITLGrsiskasLENIFertnldvllrrfengldtlvadiQLSGGERQLVALARALVSNPRLLILDEIT 497
Cdd:cd03216   69 PR--------DARRAG-------IAMVY-----------------------QLSVGERQMVEIARALARNARLLILDEPT 110

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493533268 498 ANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVAS 549
Cdd:cd03216  111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFeIADRVTVLRDGRVVGT 163

ABC_subfamily_A

cd03263

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...

345-555

3.01e-38

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: 140.33 E-value: 3.01e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 345 FGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING-DPVSNSALLRPYIGFVEQTPTLFEK 423
Cdd:cd03263   10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGySIRTDRKAARQSLGYCPQFDALFDE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 424 CTLLENITL-------GRSISKASLENIFERTNLdvllrrfENGLDTLVadIQLSGGERQLVALARALVSNPRLLILDEI 496
Cdd:cd03263   90 LTVREHLRFyarlkglPKSEIKEEVELLLRVLGL-------TDKANKRA--RTLSGGMKRKLSLAIALIGGPSVLLLDEP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 497 TANIDSKTEEIIQNTLLGLRSEGIIVLmVAHRLSTV-LLSDRVALISNGVIVASGTHNEL 555
Cdd:cd03263  161 TSGLDPASRRAIWDLILEVRKGRSIIL-TTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219

CysA

COG1118

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...

337-557

4.80e-38

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

Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 143.36 E-value: 4.80e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING-DPVSNSALLRPYIGFVE 415
Cdd:COG1118    2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrDLFTNLPPRERRVGFVF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 416 QTPTLFEKCTLLENITLGRSISKASLENIFERTnlDVLLRRFenGLDTLvAD---IQLSGGERQLVALARALVSNPRLLI 492
Cdd:COG1118   82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARV--EELLELV--QLEGL-ADrypSQLSGGQRQRVALARALAVEPEVLL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268 493 LDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLK 557
Cdd:COG1118  157 LDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALeLADRVVVMNQGRIEQVGTPDEVYD 223

GsiA

COG1123

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...

338-556

9.17e-38

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: 146.20 E-value: 9.17e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGY--GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQ---SGTIYINGDPV--SNSALLRPY 410
Cdd:COG1123    5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLleLSEALRGRR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 411 IGFVEQTPT--------LFEKCTLLENITLGRSISKASLENIFERTNLDVLLRRFENgldtlvadiQLSGGERQLVALAR 482
Cdd:COG1123   85 IGMVFQDPMtqlnpvtvGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPH---------QLSGGQRQRVAIAM 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 483 ALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELL 556
Cdd:COG1123  156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAeIADRVVVMDDGRIVEDGPPEEIL 231

LivG

COG0411

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...

351-551

1.39e-37

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: 139.40 E-value: 1.39e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 351 QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNsalLRPY------IG--FveQTPTLFE 422
Cdd:COG0411   18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG---LPPHriarlgIArtF--QNPRLFP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 423 KCTLLENITLGR-SISKASLENIFERTNLDV------------LLRRFenGL----DTLVADiqLSGGERQLVALARALV 485
Cdd:COG0411   93 ELTVLENVLVAAhARLGRGLLAALLRLPRARreereareraeeLLERV--GLadraDEPAGN--LSYGQQRRLEIARALA 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493533268 486 SNPRLLILDEITANIDSK-TEEIIQnTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGT 551
Cdd:COG0411  169 TEPKLLLLDEPAAGLNPEeTEELAE-LIRRLRDErGITILLIEHDMDLVMgLADRIVVLDFGRVIAEGT 236

ABC_ModC_like

cd03299

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...

338-563

1.44e-37

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: 139.01 E-value: 1.44e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQiLKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLRPYIGFVEQT 417
Cdd:cd03299    1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PTLFEKCTLLENITLG---RSISKASLE----NIFERTNLDVLLRRFENgldtlvadiQLSGGERQLVALARALVSNPRL 490
Cdd:cd03299   80 YALFPHMTVYKNIAYGlkkRKVDKKEIErkvlEIAEMLGIDHLLNRKPE---------TLSGGEQQRVAIARALVVNPKI 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 491 LILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLKTSSEYK 563
Cdd:cd03299  151 LLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWaLADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225

ABC_CysA_sulfate_importer

cd03296

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...

337-555

1.70e-37

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: 138.63 E-value: 1.70e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLRPYIGFVEQ 416
Cdd:cd03296    2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 TPTLFEKCTLLENITLGRSISKAS-----------LENIFERTNLDVLLRRFENgldtlvadiQLSGGERQLVALARALV 485
Cdd:cd03296   82 HYALFRHMTVFDNVAFGLRVKPRSerppeaeirakVHELLKLVQLDWLADRYPA---------QLSGGQRQRVALARALA 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268 486 SNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNEL 555
Cdd:cd03296  153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALeVADRVVVMNKGRIEQVGTPDEV 224

ABC_MalK_N

cd03301

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...

338-550

3.22e-37

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: 137.00 E-value: 3.22e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNsalLRPY---IGFV 414
Cdd:cd03301    1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD---LPPKdrdIAMV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQTPTLFEKCTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTLVAdiQLSGGERQLVALARALVSNPRLLILD 494
Cdd:cd03301   78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPK--QLSGGQRQRVALGRAIVREPKVFLMD 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 495 EITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAH-RLSTVLLSDRVALISNGVIVASG 550
Cdd:cd03301  156 EPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213

ABC_tran

pfam00005

ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...

353-498

5.26e-37

Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 134.31 E-value: 5.26e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIGFVEQTPTLFEKCTLLENI 430
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTddERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268  431 TLGRSISKASLENIFERtnLDVLLRRFENG--LDTLVADI--QLSGGERQLVALARALVSNPRLLILDEITA 498
Cdd:pfam00005  81 RLGLLLKGLSKREKDAR--AEEALEKLGLGdlADRPVGERpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

ABC_MetN_methionine_transporter

cd03258

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...

338-556

1.20e-36

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: 136.17 E-value: 1.20e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIA--FGYGNKQI--LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING---DPVSNSAL--LR 408
Cdd:cd03258    2 IELKNVSkvFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdlTLLSGKELrkAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 409 PYIGFVEQTPTLFEKCTLLENITLGRSISKASLENIFERTnldvllrrfeNGLDTLV-----ADI---QLSGGERQLVAL 480
Cdd:cd03258   82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERV----------LELLELVgledkADAypaQLSGGQKQRVGI 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 481 ARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELL 556
Cdd:cd03258  152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKrICDRVAVMEKGEVVEEGTVEEVF 229

ABCC_cytochrome_bd

cd03247

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...

338-550

3.60e-36

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: 133.21 E-value: 3.60e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYG--NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN-SALLRPYIGFV 414
Cdd:cd03247    1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDlEKALSSLISVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQTPTLFEKcTLLENitLGRsiskaslenifertnldvllrrfengldtlvadiQLSGGERQLVALARALVSNPRLLILD 494
Cdd:cd03247   81 NQRPYLFDT-TLRNN--LGR----------------------------------RFSGGERQRLALARILLQDAPIVLLD 123

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 495 EITANIDSKTEEIIQNTLLGLrSEGIIVLMVAHRLSTVLLSDRVALISNGVIVASG 550
Cdd:cd03247  124 EPTVGLDPITERQLLSLIFEV-LKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178

YbbA

COG4181

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...

352-548

4.14e-36

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: 134.87 E-value: 4.14e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 352 ILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN-----SALLRP-YIGFVEQT----PTLf 421
Cdd:COG4181   27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedaRARLRArHVGFVFQSfqllPTL- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 422 ekcTLLENITL-----GRSISKASLENIFERTNLDVLLRRFENgldtlvadiQLSGGERQLVALARALVSNPRLLILDEI 496
Cdd:COG4181  106 ---TALENVMLplelaGRRDARARARALLERVGLGHRLDHYPA---------QLSGGEQQRVALARAFATEPAILFADEP 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493533268 497 TANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVLLSDRVALISNGVIVA 548
Cdd:COG4181  174 TGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226

PRK11160

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

313-566

8.07e-36

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

Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 141.50 E-value: 8.07e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 313 RTIEVLEA-PEEERSNSSPKLEDVRSISLENIAFGYGNKQ--ILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKP 389
Cdd:PRK11160 313 RINEITEQkPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDP 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 390 QSGTIYINGDPVS--NSALLRPYIGFVEQTPTLFEKcTLLENITLGR-SISKASLENIFERTNLDVLLRRfENGLDTLVA 466
Cdd:PRK11160 393 QQGEILLNGQPIAdySEAALRQAISVVSQRVHLFSA-TLRDNLLLAApNASDEALIEVLQQVGLEKLLED-DKGLNAWLG 470

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 467 DI--QLSGGERQLVALARALVSNPRLLILDEITANIDSKTE-EIIQntLLGLRSEGIIVLMVAHRLSTVLLSDRVALISN 543
Cdd:PRK11160 471 EGgrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETErQILE--LLAEHAQNKTVLMITHRLTGLEQFDRICVMDN 548

                        250       260
                 ....*....|....*....|...
gi 493533268 544 GVIVASGTHNELLKTSSEYKKLY 566
Cdd:PRK11160 549 GQIIEQGTHQELLAQQGRYYQLK 571

ABC_PhnC_transporter

cd03256

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...

338-555

9.60e-36

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: 133.85 E-value: 9.60e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGN-KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN---SAL--LRPYI 411
Cdd:cd03256    1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgKALrqLRRQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 412 GFVEQTPTLFEKCTLLENITLGRSISKASLENIF------ERTNLDVLLRRFenGLDTLV---ADiQLSGGERQLVALAR 482
Cdd:cd03256   81 GMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFglfpkeEKQRALAALERV--GLLDKAyqrAD-QLSGGQQQRVAIAR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 483 ALVSNPRLLILDEITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNEL 555
Cdd:cd03256  158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPAEL 232

ABC_6TM_YwjA_like

cd18549

Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...

24-313

1.54e-35

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: 134.88 E-value: 1.54e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGvmiALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYF----GEVVfetTALMaKSDLRKQ 99
Cdd:cd18549    8 LFCAVLIA---ALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFvtywGHVM---GARI-ETDMRRD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 100 LLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIM 179
Cdd:cd18549   81 LFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 180 FFNIMVEKRSKVEREKFGElagVTSNIIDNMKLIRIAMPFA---WVMNFFDRFQGDHIYAGKRFIKSIKIAGTLKTSING 256
Cdd:cd18549  161 YFNKKMKKAFRRVREKIGE---INAQLEDSLSGIRVVKAFAneeYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTN 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268 257 LISFSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQSWGGLLR 313
Cdd:cd18549  238 LLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294

ABC_6TM_YknU_like

cd18542

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...

24-297

1.69e-35

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: 134.87 E-value: 1.69e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLEK 103
Cdd:cd18542    2 LLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 104 MFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIMFFNI 183
Cdd:cd18542   82 LQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 184 MVEKRSKVEREKFGELagvTSNIIDNMKLIRIAMPFA---WVMNFFDRFQGDhiYAGKRfIKSIKIAGTLKTSINGLISF 260
Cdd:cd18542  162 KVRPAFEEIREQEGEL---NTVLQENLTGVRVVKAFAredYEIEKFDKENEE--YRDLN-IKLAKLLAKYWPLMDFLSGL 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 493533268 261 SLLA---YGGYLVMKGEITVGILMTFWAYVQSLFNPIQLL 297
Cdd:cd18542  236 QIVLvlwVGGYLVINGEITLGELVAFISYLWMLIWPVRQL 275

YhaQ

COG4152

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

337-558

2.03e-35

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

Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.85 E-value: 2.03e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLRpyIGFVEQ 416
Cdd:COG4152    1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR--IGYLPE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 TPTLFEKCTLLENIT-LGR--SISKASLenifeRTNLDVLLRRFEngldtlVADI------QLSGGERQLVALARALVSN 487
Cdd:COG4152   79 ERGLYPKMKVGEQLVyLARlkGLSKAEA-----KRRADEWLERLG------LGDRankkveELSKGNQQKVQLIAALLHD 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268 488 PRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVIVASGTHNELLKT 558
Cdd:COG4152  148 PELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQ 219

ModC

COG4148

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...

357-556

3.13e-35

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: 136.00 E-value: 3.13e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 357 SLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL---LRPY---IGFVEQTPTLFEKCTLLENI 430
Cdd:COG4148   19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARgifLPPHrrrIGYVFQEARLFPHLSVRGNL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 431 TLG-----RSISKASLENIFERTNLDVLLRRFENgldtlvadiQLSGGERQLVALARALVSNPRLLILDEITANIDSKT- 504
Cdd:COG4148   99 LYGrkrapRAERRISFDEVVELLGIGHLLDRRPA---------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARk 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493533268 505 EEIIqNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELL 556
Cdd:COG4148  170 AEIL-PYLERLRDElDIPILYVSHSLDEVArLADHVVLLEQGRVVASGPLAEVL 222

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

338-549

3.14e-35

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 138.62 E-value: 3.14e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV---SNSALLRPYIGFV 414
Cdd:COG3845    6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirSPRDAIALGIGMV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQTPTLFEKCTLLENITLGRSISK----------ASLENIFERTNLDVllrrfenGLDTLVADiqLSGGERQLVALARAL 484
Cdd:COG3845   86 HQHFMLVPNLTVAENIVLGLEPTKggrldrkaarARIRELSERYGLDV-------DPDAKVED--LSVGEQQRVEILKAL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268 485 VSNPRLLILDEITANI-DSKTEEIIQnTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVAS 549
Cdd:COG3845  157 YRGARILILDEPTAVLtPQEADELFE-ILRRLAAEGKSIIFITHKLREVMaIADRVTVLRRGKVVGT 222

ABC_cobalt_CbiO_domain2

cd03226

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...

339-547

4.99e-35

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: 130.84 E-value: 4.99e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 339 SLENIAFGYG-NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLRPyIGFVEQT 417
Cdd:cd03226    1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS-IGYVMQD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PT--LFEkCTLLENITLGRSISKASLENIFErtnldvLLRRFEngLDTLVAD--IQLSGGERQLVALARALVSNPRLLIL 493
Cdd:cd03226   80 VDyqLFT-DSVREELLLGLKELDAGNEQAET------VLKDLD--LYALKERhpLSLSGGQKQRLAIAAALLSGKDLLIF 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 494 DEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLL-SDRVALISNGVIV 547
Cdd:cd03226  151 DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205

ABC_putative_ATPase

cd03269

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...

338-550

1.13e-34

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: 130.09 E-value: 1.13e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAllRPYIGFVEQT 417
Cdd:cd03269    1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA--RNRIGYLPEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PTLFEKCTLLENIT-------LGRSISKASLENIFERTNL-DVLLRRFEngldtlvadiQLSGGERQLVALARALVSNPR 489
Cdd:cd03269   79 RGLYPKMKVIDQLVylaqlkgLKKEEARRRIDEWLERLELsEYANKRVE----------ELSKGNQQKVQFIAAVIHDPE 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268 490 LLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVIVASG 550
Cdd:cd03269  149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210

ABC_OpuCA_Osmoprotection

cd03295

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...

338-556

1.89e-34

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: 130.50 E-value: 1.89e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGN-KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIGFV 414
Cdd:cd03295    1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqDPVELRRKIGYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQTPTLFEKCTLLENITLGRSISKASLENIFERtnLDVLLRRFenGLDTL-VAD---IQLSGGERQLVALARALVSNPRL 490
Cdd:cd03295   81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRER--ADELLALV--GLDPAeFADrypHELSGGQQQRVGVARALAADPPL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 491 LILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRL-STVLLSDRVALISNGVIVASGTHNELL 556
Cdd:cd03295  157 LLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224

ThiQ

COG3840

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

338-556

1.14e-33

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

Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 127.95 E-value: 1.14e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNkQILKgLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNsalLRPY-----IG 412
Cdd:COG3840    2 LRLDDLTYRYGD-FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA---LPPAerpvsML 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTptLFEKCTLLENITLGRSIS-------KASLENIFERTNLDVLLRRFENgldtlvadiQLSGGERQLVALARALV 485
Cdd:COG3840   77 FQENN--LFPHLTVAQNIGLGLRPGlkltaeqRAQVEQALERVGLAGLLDRLPG---------QLSGGQRQRVALARCLV 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 486 SNPRLLILDEITANID-SKTEEIIQ--NTLlgLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELL 556
Cdd:COG3840  146 RKRPILLLDEPFSALDpALRQEMLDlvDEL--CRERGLTVLMVTHDPEDAArIADRVLLVADGRIAADGPTAALL 218

PRK10789

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

111-569

1.48e-33

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

Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 134.84 E-value: 1.48e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 111 FFHKNKTGELVSRLISDLELVgtVIAQVFPILLL--GVVQITAILAIM-FAFNWKLTLLPLGFIVFSFLVIMFFNIMVEK 187
Cdd:PRK10789  86 FYLRHRTGDLMARATNDVDRV--VFAAGEGVLTLvdSLVMGCAVLIVMsTQISWQLTLLALLPMPVMAIMIKRYGDQLHE 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 188 RSKVEREKFGELAGVTSniiDNMKLIRIAMPFAWVMNFFDRFQGDHIYAGKRFIKSIKIAGTLKTSINGLISFS-LLAYG 266
Cdd:PRK10789 164 RFKLAQAAFSSLNDRTQ---ESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMAnLLAIG 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 267 G--YLVMKGEITVGILMTFWAYVQSLFNP-IQLLMQVNILLRQS--WGGLLRTIEvlEAPEEERSNSSpkLEDVRSISLE 341
Cdd:PRK10789 241 GgsWMVVNGSLTLGQLTSFVMYLGLMIWPmLALAWMFNIVERGSaaYSRIRAMLA--EAPVVKDGSEP--VPEGRGELDV 316

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 342 NI-AFGY--GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGFVEQ 416
Cdd:PRK10789 317 NIrQFTYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLdsWRSRLAVVSQ 396

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 TPTLFEKcTLLENITLGRSisKASLENIFERTNL-----DVLlrRFENGLDTLVAD--IQLSGGERQLVALARALVSNPR 489
Cdd:PRK10789 397 TPFLFSD-TVANNIALGRP--DATQQEIEHVARLasvhdDIL--RLPQGYDTEVGErgVMLSGGQKQRISIARALLLNAE 471

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 490 LLILDEITANIDSKTE-EIIQNtlLGLRSEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYKKLYSL 568
Cdd:PRK10789 472 ILILDDALSAVDGRTEhQILHN--LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRY 549


                 .
gi 493533268 569 Q 569
Cdd:PRK10789 550 Q 550

ABC_DrrA

cd03265

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...

338-555

1.98e-33

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: 127.10 E-value: 1.98e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING-DPVSNSALLRPYIGFVEQ 416
Cdd:cd03265    1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhDVVREPREVRRRIGIVFQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 TPTLFEKCTLLENITLGRSISKASLENIFERTnlDVLLRRFENG--LDTLVAdiQLSGGERQLVALARALVSNPRLLILD 494
Cdd:cd03265   81 DLSVDDELTGWENLYIHARLYGVPGAERRERI--DELLDFVGLLeaADRLVK--TYSGGMRRRLEIARSLVHRPEVLFLD 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 495 EITANIDSKTE----EIIQNTllgLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVIVASGTHNEL 555
Cdd:cd03265  157 EPTIGLDPQTRahvwEYIEKL---KEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219

potA

PRK09452

spermidine/putrescine ABC transporter ATP-binding protein PotA;

338-551

2.15e-33

spermidine/putrescine ABC transporter ATP-binding protein PotA;

Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 131.22 E-value: 2.15e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN-SALLRPyIGFVEQ 416
Cdd:PRK09452  15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvPAENRH-VNTVFQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 TPTLFEKCTLLENITLGRSISKASLENIFERTnLDVL-LRRFENGLDTLVAdiQLSGGERQLVALARALVSNPRLLILDE 495
Cdd:PRK09452  94 SYALFPHMTVFENVAFGLRMQKTPAAEITPRV-MEALrMVQLEEFAQRKPH--QLSGGQQQRVAIARAVVNKPKVLLLDE 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 496 ITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGT 551
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALtMSDRIVVMRDGRIEQDGT 228

COG4559

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

338-551

2.54e-33

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

Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 127.92 E-value: 2.54e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNS-----ALLRpyiG 412
Cdd:COG4559    2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWspwelARRR---A 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTPTL---FekcTLLENITLGRS---ISKASLENI----FERTNLDVLLRRFENgldtlvadiQLSGGERQLVALAR 482
Cdd:COG4559   79 VLPQHSSLafpF---TVEEVVALGRAphgSSAAQDRQIvreaLALVGLAHLAGRSYQ---------TLSGGEQQRVQLAR 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 483 ALV-------SNPRLLILDEITANIDskteeiI--QNTLL----GLRSEGIIVLMVAHRLS-TVLLSDRVALISNGVIVA 548
Cdd:COG4559  147 VLAqlwepvdGGPRWLFLDEPTSALD------LahQHAVLrlarQLARRGGGVVAVLHDLNlAAQYADRILLLHQGRLVA 220


                 ...
gi 493533268 549 SGT 551
Cdd:COG4559  221 QGT 223

ABC_6TM_Tm288_like

cd18547

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...

24-303

4.95e-33

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: 128.29 E-value: 4.95e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALAVVFPLLIRLLIDVVI------PSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLR 97
Cdd:cd18547    2 ILVIILAIISTLLSVLGPYLLGKAIDLIIeglgggGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  98 KQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLV 177
Cdd:cd18547   82 KDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 178 IMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRiampfawVMN----FFDRFQG--DHIYagKRFIKSIKIAGTLK 251
Cdd:cd18547  162 TKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVK-------AFNreeeAIEEFDEinEELY--KASFKAQFYSGLLM 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 252 TSINGL--ISFSLLA-YGGYLVMKGEITVGILMTFWAYVQSLFNPI-QLLMQVNIL 303
Cdd:cd18547  233 PIMNFInnLGYVLVAvVGGLLVINGALTVGVIQAFLQYSRQFSQPInQISQQINSL 288

ABC_FtsE

cd03292

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...

338-546

8.96e-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: 124.83 E-value: 8.96e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQI-LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN-----SALLRPYI 411
Cdd:cd03292    1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 412 GFVEQTPTLFEKCTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTLVAdiQLSGGERQLVALARALVSNPRLL 491
Cdd:cd03292   81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPA--ELSGGEQQRVAIARAIVNSPTIL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 492 ILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVI 546
Cdd:cd03292  159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVdTTRHRVIALERGKL 214

modC_ABC

TIGR02142

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...

356-559

1.19e-32

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: 128.69 E-value: 1.19e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  356 LSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSA---LLRPY---IGFVEQTPTLFEKCTLLEN 429
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiFLPPEkrrIGYVFQEARLFPHLSVRGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  430 ITLGRSISKASLENI-FERT----NLDVLLRRFENgldtlvadiQLSGGERQLVALARALVSNPRLLILDEITANIDSKT 504
Cdd:TIGR02142  96 LRYGMKRARPSERRIsFERViellGIGHLLGRLPG---------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268  505 EEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLKTS 559
Cdd:TIGR02142 167 KYEILPYLERLHAEfGIPILYVSHSLQEVLrLADRVVVLEDGRVAAAGPIAEVWASP 223

ABC_6TM_MsbA_like

cd18552

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...

24-307

2.87e-32

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: 126.00 E-value: 2.87e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLEK 103
Cdd:cd18552    2 ALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 104 MFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIMFFNI 183
Cdd:cd18552   82 LLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 184 MVEKRSKVEREKFGELAGVTSNIIDNMKLIRIampFA---WVMNFFDRFQGDHIyagKRFIKSIKIAGTLKTSINGLISF 260
Cdd:cd18552  162 RLRKISRRSQESMGDLTSVLQETLSGIRVVKA---FGaedYEIKRFRKANERLR---RLSMKIARARALSSPLMELLGAI 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 493533268 261 SL---LAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQS 307
Cdd:cd18552  236 AIalvLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRG 285

ABC_6TM_YknV_like

cd18545

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...

24-305

3.53e-32

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: 125.66 E-value: 3.53e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLEK 103
Cdd:cd18545    3 LLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 104 MFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIMFFNI 183
Cdd:cd18545   83 LQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 184 MVEKRSKVEREKfgeLAGVTSNIIDNMKLIRIAMPFA---WVMNFFDRFQGDHIYAgkrFIKSIKIAGTLKTS---INGL 257
Cdd:cd18545  163 RARKAWQRVRKK---ISNLNAYLHESISGIRVIQSFAredENEEIFDELNRENRKA---NMRAVRLNALFWPLvelISAL 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 493533268 258 ISFSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLL-MQVNILLR 305
Cdd:cd18545  237 GTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLsNFYNQLQS 285

ABC_ThiQ_thiamine_transporter

cd03298

ATP-binding cassette domain of the thiamine transport system; Part of the ...

338-550

5.01e-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: 122.99 E-value: 5.01e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQIlkGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLRPYIGFVEQT 417
Cdd:cd03298    1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PTLFEKCTLLENITLGRSiskASLE-NIFERTNLDVLLRRFenGLDTLVADI--QLSGGERQLVALARALVSNPRLLILD 494
Cdd:cd03298   79 NNLFAHLTVEQNVGLGLS---PGLKlTAEDRQAIEVALARV--GLAGLEKRLpgELSGGERQRVALARVLVRDKPVLLLD 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 495 EITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASG 550
Cdd:cd03298  154 EPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKrLAQRVVFLDNGRIAAQG 211

PLN03232

ABC transporter C family member; Provisional

72-567

5.94e-32

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 132.02 E-value: 5.94e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   72 FGSLIFTYFGEVVFETTALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDL--------ELVGTVIAQVFPIL- 142
Cdd:PLN03232  961 FGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIgdidrnvaNLMNMFMNQLWQLLs 1040

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  143 ---LLGVVQITAILAIMfafnwkltllPLgFIVFSFLVIMFFNIMVEKR--SKVERE----KFGE-LAGVTSniidnmkl 212
Cdd:PLN03232 1041 tfaLIGTVSTISLWAIM----------PL-LILFYAAYLYYQSTSREVRrlDSVTRSpiyaQFGEaLNGLSS-------- 1101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  213 IRIAMPFAWVMNFFDRFQGDHIYAGKRFIKSIKIAGTLKTSINGLI-----SFSLLAYGGYLVMKG-EITVGILMTFWAY 286
Cdd:PLN03232 1102 IRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMiwltaTFAVLRNGNAENQAGfASTMGLLLSYTLN 1181

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  287 VQSLFNPIqllmqvnilLRQSWGG--LLRTIEVL--------EAPEEERSNSSPKLEDVR-SISLENIAFGY--GNKQIL 353
Cdd:PLN03232 1182 ITTLLSGV---------LRQASKAenSLNSVERVgnyidlpsEATAIIENNRPVSGWPSRgSIKFEDVHLRYrpGLPPVL 1252

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  354 KGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGFVEQTPTLFEKcTLLENIT 431
Cdd:PLN03232 1253 HGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLtdLRRVLSIIPQSPVLFSG-TVRFNID 1331

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  432 LGRSISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQ 509
Cdd:PLN03232 1332 PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268  510 NTllgLRSE--GIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELL--KTSSEYKKLYS 567
Cdd:PLN03232 1412 RT---IREEfkSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLsrDTSAFFRMVHS 1470

ABC_NatA_sodium_exporter

cd03266

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...

338-550

8.34e-32

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: 122.48 E-value: 8.34e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNK----QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING-DPVSNSALLRPYIG 412
Cdd:cd03266    2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTPTLFEKCTLLENIT-------LGRSISKASLENIFERTNLDVLLRRFENGLDTlvadiqlsgGERQLVALARALV 485
Cdd:cd03266   82 FVSDSTGLYDRLTARENLEyfaglygLKGDELTARLEELADRLGMEELLDRRVGGFST---------GMRQKVAIARALV 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 486 SNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVIVASG 550
Cdd:cd03266  153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218

ABC_BcrA_bacitracin_resist

cd03268

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...

347-550

9.29e-32

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: 121.94 E-value: 9.29e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 347 YGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLRPYIGFVEQTPTLFEKCTL 426
Cdd:cd03268   10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGFYPNLTA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 427 LENI---TLGRSISKASLENIFERTNLDVLLRRfengldtLVAdiQLSGGERQLVALARALVSNPRLLILDEITANIDSK 503
Cdd:cd03268   90 RENLrllARLLGIRKKRIDEVLDVVGLKDSAKK-------KVK--GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 493533268 504 TEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVIVASG 550
Cdd:cd03268  161 GIKELRELILSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208

ABC_membrane

pfam00664

ABC transporter transmembrane region; This family represents a unit of six transmembrane ...

24-294

1.98e-31

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

Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 123.14 E-value: 1.98e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   24 LLAAVLVGVMialAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFG--SLIFTYFGEVVFETTALMAKSDLRKQLL 101
Cdd:pfam00664   5 ILLAILSGAI---SPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGlaQFILSFLQSYLLNHTGERLSRRLRRKLF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  102 EKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIMFF 181
Cdd:pfam00664  82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  182 NIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRIampFAWVMNFFDRFQGDHIYAGKRFIKSIKIAGTLKTSINGLISFS 261
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKA---FGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 493533268  262 LLA---YGGYLVMKGEITVGILMTFWAYVQSLFNPI 294
Cdd:pfam00664 239 YALalwFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274

ABC_6TM_TmrB_like

cd18541

Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...

24-305

2.63e-31

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: 123.29 E-value: 2.63e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALAVVFPLLIRLLID-VVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLE 102
Cdd:cd18541    2 LLGILFLILVDLLQLLIPRIIGRAIDaLTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 103 KMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIMFFN 182
Cdd:cd18541   82 HLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 183 IMVEKRSKVEREKFGELAGVTSNIIDNMKLIRIampFAWVMNFFDRFQG--DHIYagKRFIKSIKIAGTLKTSINGLISF 260
Cdd:cd18541  162 KKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKA---FVQEEAEIERFDKlnEEYV--EKNLRLARVDALFFPLIGLLIGL 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 493533268 261 S---LLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLL-MQVNILLR 305
Cdd:cd18541  237 SfliVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALgWVINLIQR 285

ABC_drug_resistance_like

cd03264

ABC-type multidrug transport system, ATPase component; The biological function of this family ...

338-550

2.65e-31

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: 120.76 E-value: 2.65e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGeITTLVGESGAGKTTTLNILMGLQKPQSGTIYING-DPVSNSALLRPYIGFVEQ 416
Cdd:cd03264    1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqDVLKQPQKLRRRIGYLPQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 TPTLFEKCT---LLENITLGRSIS----KASLENIFERTNL-DVLLRRFEngldtlvadiQLSGGERQLVALARALVSNP 488
Cdd:cd03264   80 EFGVYPNFTvreFLDYIAWLKGIPskevKARVDEVLELVNLgDRAKKKIG----------SLSGGMRRRVGIAQALVGDP 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493533268 489 RLLILDEITANIDSKtEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLS-DRVALISNGVIVASG 550
Cdd:cd03264  150 SILIVDEPTAGLDPE-ERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211

ABCC_MRP_domain1

cd03250

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...

338-544

8.05e-31

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: 119.11 E-value: 8.05e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQ-----ILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDpvsnsallrpyIG 412
Cdd:cd03250    1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTPTLFEKcTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPRL 490
Cdd:cd03250   70 YVSQEPWIQNG-TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEkgINLSGGQKQRISLARAVYSDADI 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 491 LILDEITANIDSKTEE-IIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRVALISNG 544
Cdd:cd03250  149 YLLDDPLSAVDAHVGRhIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203

ABC_6TM_exporter_like

cd18778

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

24-307

9.35e-31

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: 121.49 E-value: 9.35e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALAVVFPLLIRLLID-VVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLE 102
Cdd:cd18778    2 ILTLLCALLSTLLGLVPPWLIRELVDlVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 103 KMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIMFFN 182
Cdd:cd18778   82 KLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 183 IMVEKRSKVEREKFGELAGVTSNIIDNMKLIRIampFAWVMNFFDRFQG-DHIYAgKRFIKSIKIAGTLKTSINGLISFS 261
Cdd:cd18778  162 KKVRPRYRKVREALGELNALLQDNLSGIREIQA---FGREEEEAKRFEAlSRRYR-KAQLRAMKLWAIFHPLMEFLTSLG 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 493533268 262 ---LLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQS 307
Cdd:cd18778  238 tvlVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRA 286

hmuV

PRK13548

hemin importer ATP-binding subunit; Provisional

337-551

1.77e-30

hemin importer ATP-binding subunit; Provisional

Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 119.88 E-value: 1.77e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIGFV 414
Cdd:PRK13548   2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwSPAELARRRAVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQTPTLFEKCTLLENITLGRS---ISKASLENIF----ERTNLDVLLRRFENgldtlvadiQLSGGERQLVALARALV-- 485
Cdd:PRK13548  82 PQHSSLSFPFTVEEVVAMGRAphgLSRAEDDALVaaalAQVDLAHLAGRDYP---------QLSGGEQQRVQLARVLAql 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 486 ----SNPRLLILDEITANIDskteeiI--QNTLLGL-----RSEGIIVLMVAHRLS-TVLLSDRVALISNGVIVASGT 551
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALD------LahQHHVLRLarqlaHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224

ABCG_EPDR

cd03213

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...

337-550

3.01e-30

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: 117.27 E-value: 3.01e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAF------GYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQ--SGTIYINGDPVSNSAlLR 408
Cdd:cd03213    3 TLSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRS-FR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 409 PYIGFVEQTPTLFEKCTLLENItlgrSISkaslenifertnldVLLRrfengldtlvadiQLSGGERQLVALARALVSNP 488
Cdd:cd03213   82 KIIGYVPQDDILHPTLTVRETL----MFA--------------AKLR-------------GLSGGERKRVSIALELVSNP 130

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493533268 489 RLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLS--DRVALISNGVIVASG 550
Cdd:cd03213  131 SLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFElfDKLLLLSQGRVIYFG 194

ABC_6TM_LmrA_like

cd18551

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...

24-299

3.70e-30

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: 119.85 E-value: 3.70e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALAVVFPLLIRLLIDVVipsGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLEK 103
Cdd:cd18551    2 ILALLLSLLGTAASLAQPLLVKNLIDAL---SAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 104 MFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIMFFNI 183
Cdd:cd18551   79 LLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 184 MVEKRSKVEREKFGELAGVTSNIIDNMKLIRIAmpfawvmNFFDRFQ---GDHIYAGKRF-IKSIKIAGTLKTSINGLIS 259
Cdd:cd18551  159 RIRKASKRAQDALGELSAALERALSAIRTVKAS-------NAEERETkrgGEAAERLYRAgLKAAKIEALIGPLMGLAVQ 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 493533268 260 FSL---LAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQ 299
Cdd:cd18551  232 LALlvvLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSS 274

ABC_ModC_molybdenum_transporter

cd03297

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...

353-550

4.71e-30

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: 117.40 E-value: 4.71e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 353 LKGLSLELR---KGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL---LRPY---IGFVEQTPTLFEK 423
Cdd:cd03297   10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKkinLPPQqrkIGLVFQQYALFPH 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 424 CTLLENITLG-----RSISKASLENIFERTNLDVLLRRFENgldtlvadiQLSGGERQLVALARALVSNPRLLILDEITA 498
Cdd:cd03297   90 LNVRENLAFGlkrkrNREDRISVDELLDLLGLDHLLNRYPA---------QLSGGEKQRVALARALAAQPELLLLDEPFS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493533268 499 NIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTV-LLSDRVALISNGVIVASG 550
Cdd:cd03297  161 ALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214

PRK13537

nodulation factor ABC transporter ATP-binding protein NodI;

338-558

7.62e-30

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 119.52 E-value: 7.62e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSA-LLRPYIGFVEQ 416
Cdd:PRK13537   8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRArHARQRVGVVPQ 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 TPTLFEKCTLLENI-TLGRSISKASLEnIFERTNLDVLLRRFENGLDTLVADiqLSGGERQLVALARALVSNPRLLILDE 495
Cdd:PRK13537  88 FDNLDPDFTVRENLlVFGRYFGLSAAA-ARALVPPLLEFAKLENKADAKVGE--LSGGMKRRLTLARALVNDPDVLVLDE 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493533268 496 ITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVIVASGTHNELLKT 558
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIES 228

fbpC

PRK11432

ferric ABC transporter ATP-binding protein;

340-558

8.94e-30

ferric ABC transporter ATP-binding protein;

Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 120.21 E-value: 8.94e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 340 LENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLRPYIGFVEQTPT 419
Cdd:PRK11432   9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 420 LFEKCTLLENITLGRSISKASLENIFERTN--LD-VLLRRFEnglDTLVAdiQLSGGERQLVALARALVSNPRLLILDEI 496
Cdd:PRK11432  89 LFPHMSLGENVGYGLKMLGVPKEERKQRVKeaLElVDLAGFE---DRYVD--QISGGQQQRVALARALILKPKVLLFDEP 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493533268 497 TANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLKT 558
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFaVSDTVIVMNKGKIMQIGSPQELYRQ 227

ntrCD

TIGR01184

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...

353-544

9.14e-30

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: 117.18 E-value: 9.14e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAllrPYIGFVEQTPTLFEKCTLLENITL 432
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG---PDRMVVFQNYSLLPWLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  433 G-----RSISKASLENIFERTNLDVLLRRFENGLDTlvadiQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEI 507
Cdd:TIGR01184  78 AvdrvlPDLSKSERRAIVEEHIALVGLTEAADKRPG-----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 493533268  508 IQNTLLGLRSE-GIIVLMVAHRL-STVLLSDRVALISNG 544
Cdd:TIGR01184 153 LQEELMQIWEEhRVTVLMVTHDVdEALLLSDRVVMLTNG 191

AbcC

COG1135

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

338-551

1.53e-29

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

Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 119.41 E-value: 1.53e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENI--AFGYGNKQI--LKGLSLELRKGEITTLVGESGAGKTT---TLNilmGLQKPQSGTIYINGDPV---SNSAL- 406
Cdd:COG1135    2 IELENLskTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTlirCIN---LLERPTSGSVLVDGVDLtalSERELr 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 407 -LRPYIGFVEQTPTLFEKCTLLENITLGRSISKASLENIFERTN--LDvllrrfengldtLV-----ADI---QLSGGER 475
Cdd:COG1135   79 aARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAelLE------------LVglsdkADAypsQLSGGQK 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 476 QLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGT 551
Cdd:COG1135  147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRrICDRVAVLENGRIVEQGP 224

cbiO

PRK13632

cobalt transporter ATP-binding subunit; Provisional

338-557

1.63e-29

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.40 E-value: 1.63e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGN--KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGF 413
Cdd:PRK13632   8 IKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLkeIRKKIGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTP-TLFEKCTL-------LENITLGRSISKASLENIFERTNLDVLLRRfengldtlvADIQLSGGERQLVALARALV 485
Cdd:PRK13632  88 IFQNPdNQFIGATVeddiafgLENKKVPPKKMKDIIDDLAKKVGMEDYLDK---------EPQNLSGGQKQRVAIASVLA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493533268 486 SNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGI-IVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLK 557
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231

ABC_6TM_exporter_like

cd18564

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

24-295

1.93e-29

Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 118.38 E-value: 1.93e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSL---------------IFTYFGEVVFETT 88
Cdd:cd18564    2 ALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPGLLGLAPLLGPDPLALLllaaaalvgiallrgLASYAGTYLTALV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  89 ALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPL 168
Cdd:cd18564   82 GQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 169 GFIVFSFLVIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRiamPFAWVMNFFDRFQGDHIYAGKRFIKSIKIAG 248
Cdd:cd18564  162 AVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQ---AFGREEHEERRFARENRKSLRAGLRAARLQA 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 493533268 249 TLKTSINGLISFSL---LAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQ 295
Cdd:cd18564  239 LLSPVVDVLVAVGTalvLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVR 288

PRK13536

nodulation factor ABC transporter ATP-binding protein NodI;

319-557

3.82e-29

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 118.39 E-value: 3.82e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 319 EAPEEERSNSSPKLEDVRSISLENIAF-------GYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQS 391
Cdd:PRK13536  16 LSPIERKHQGISEAKASIPGSMSTVAIdlagvskSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 392 GTIYINGDPVSNSA-LLRPYIGFVEQTPTLFEKCTLLEN-ITLGR--SISKASLENIfertnLDVLLR--RFENGLDTLV 465
Cdd:PRK13536  96 GKITVLGVPVPARArLARARIGVVPQFDNLDLEFTVRENlLVFGRyfGMSTREIEAV-----IPSLLEfaRLESKADARV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 466 ADiqLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNG 544
Cdd:PRK13536 171 SD--LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAeRLCDRLCVLEAG 248

                        250
                 ....*....|...
gi 493533268 545 VIVASGTHNELLK 557
Cdd:PRK13536 249 RKIAEGRPHALID 261

ABC_6TM_TAP_ABCB8_10_like

cd18557

Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...

26-295

6.28e-29

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: 116.51 E-value: 6.28e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  26 AAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLEKMF 105
Cdd:cd18557    1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 106 VLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIMFFNIMV 185
Cdd:cd18557   81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 186 EKRSKVEREKFGELAGVTSNIIDNMKLIRIampFAWVMNFFDRFQG--DHIYA-GKRFIKSIKIAGTLKTSINGLISFSL 262
Cdd:cd18557  161 RKLSKEVQDALAKAGQVAEESLSNIRTVRS---FSAEEKEIRRYSEalDRSYRlARKKALANALFQGITSLLIYLSLLLV 237

                        250       260       270
                 ....*....|....*....|....*....|...
gi 493533268 263 LAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQ 295
Cdd:cd18557  238 LWYGGYLVLSGQLTVGELTSFILYTIMVASSVG 270

ABC_6TM_PCAT1_LagD_like

cd18570

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...

21-306

1.03e-28

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: 116.01 E-value: 1.03e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  21 KRELLAAVLVGVMIA-LAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQ 99
Cdd:cd18570    1 KKLLILILLLSLLITlLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 100 LLEKMFVLPFDFFHKNKTGELVSRLiSDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIM 179
Cdd:cd18570   81 YFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIIL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 180 FFNIMVEKRSKVEREKFGELagvTSNIIDNMKLIRIAMPFAWVMNFFDRFQ---GDHIYAGKRFIKSIKIAGTLKTSING 256
Cdd:cd18570  160 LFNKPFKKKNREVMESNAEL---NSYLIESLKGIETIKSLNAEEQFLKKIEkkfSKLLKKSFKLGKLSNLQSSIKGLISL 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 493533268 257 LISFSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQ 306
Cdd:cd18570  237 IGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQE 286

ABCC_NFT1

cd03369

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...

337-551

1.06e-28

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: 113.28 E-value: 1.06e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGNK--QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIG 412
Cdd:cd03369    6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLedLRSSLT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTPTLFEKcTLLENITLgrsISKASLENIFErtnldvLLRRFENGLDtlvadiqLSGGERQLVALARALVSNPRLLI 492
Cdd:cd03369   86 IIPQDPTLFSG-TIRSNLDP---FDEYSDEEIYG------ALRVSEGGLN-------LSQGQRQLLCLARALLKRPRVLV 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493533268 493 LDEITANIDSKTEEIIQNTllgLRSE--GIIVLMVAHRLSTVLLSDRVALISNGVIVASGT 551
Cdd:cd03369  149 LDEATASIDYATDALIQKT---IREEftNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206

artP

PRK11124

arginine transporter ATP-binding subunit; Provisional

337-552

1.36e-28

arginine transporter ATP-binding subunit; Provisional

Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 113.96 E-value: 1.36e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSA--------LLR 408
Cdd:PRK11124   2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKtpsdkairELR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 409 PYIGFVEQTPTLFEKCTLLENIT--------LGRSISKASLENIFERTNLDVLLRRFEngldtlvadIQLSGGERQLVAL 480
Cdd:PRK11124  82 RNVGMVFQQYNLWPHLTVQQNLIeapcrvlgLSKDQALARAEKLLERLRLKPYADRFP---------LHLSGGQQQRVAI 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493533268 481 ARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTH 552
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARkTASRVVYMENGHIVEQGDA 225

ABC_Pro_Gly_Betaine

cd03294

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...

339-556

1.44e-28

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: 114.66 E-value: 1.44e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 339 SLENIAFGYGNKQILKGL---------SLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN------ 403
Cdd:cd03294   17 AFKLLAKGKSKEEILKKTgqtvgvndvSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrkel 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 404 SALLRPYIGFVEQTPTLFEKCTLLENITLGRSISKASLENIFERTnLDVL----LRRFENGLDTlvadiQLSGGERQLVA 479
Cdd:cd03294   97 RELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERA-AEALelvgLEGWEHKYPD-----ELSGGMQQRVG 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493533268 480 LARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELL 556
Cdd:cd03294  171 LARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALrLGDRIAIMKDGRLVQVGTPEEIL 249

TauB

COG4525

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

338-527

1.56e-28

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

Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 114.57 E-value: 1.56e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGN----KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLRpyiGF 413
Cdd:COG4525    4 LTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---GV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPTLFEKCTLLENITLG---RSISKASLENIFERTNLDVLLRRFENgldtlvADI-QLSGGERQLVALARALVSNPR 489
Cdd:COG4525   81 VFQKDALLPWLNVLDNVAFGlrlRGVPKAERRARAEELLALVGLADFAR------RRIwQLSGGMRQRVGIARALAADPR 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 493533268 490 LLILDEITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAH 527
Cdd:COG4525  155 FLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITH 193

PLN03130

ABC transporter C family member; Provisional

72-556

1.73e-28

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 121.38 E-value: 1.73e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   72 FGSLIFTYFGEVVFETTALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLE--------LVGTVIAQVFPIL- 142
Cdd:PLN03130  964 FGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGdidrnvavFVNMFLGQIFQLLs 1043

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  143 ---LLGVVQITAILAIMfafnwkltllPLgFIVFSFLVIMFFNIMVE-------KRSKVeREKFGE-LAGVTSniidnmk 211
Cdd:PLN03130 1044 tfvLIGIVSTISLWAIM----------PL-LVLFYGAYLYYQSTAREvkrldsiTRSPV-YAQFGEaLNGLST------- 1104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  212 lIRIAMPFAWVMNFFDRFQGDHIyagkRFiksikiagTLKT-SINGLISFSLLAYGGYL--------VMKGE-------- 274
Cdd:PLN03130 1105 -IRAYKAYDRMAEINGRSMDNNI----RF--------TLVNmSSNRWLAIRLETLGGLMiwltasfaVMQNGraenqaaf 1171

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  275 -ITVGILMTFWAYVQSLFNPIQLLMQvniLLRQSWGGLLRTIEVLEAPEE-----ERSNSSPKLEDVRSISLENIAFGYG 348
Cdd:PLN03130 1172 aSTMGLLLSYALNITSLLTAVLRLAS---LAENSLNAVERVGTYIDLPSEaplviENNRPPPGWPSSGSIKFEDVVLRYR 1248

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  349 NK--QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGFVEQTPTLFEKc 424
Cdd:PLN03130 1249 PElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLmdLRKVLGIIPQAPVLFSG- 1327

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  425 TLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTLVADI--QLSGGERQLVALARALVSNPRLLILDEITANIDS 502
Cdd:PLN03130 1328 TVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAgeNFSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268  503 KTEEIIQNTllgLRSE--GIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELL 556
Cdd:PLN03130 1408 RTDALIQKT---IREEfkSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLL 1460

PhnK

COG1101

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

338-547

6.89e-28

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

Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.49 E-value: 6.89e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENI--AFGYG---NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLR--PY 410
Cdd:COG1101    2 LELKNLskTFNPGtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKraKY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 411 IGFVEQTPTL--FEKCTLLENI----------TLGRSISKASLENIFERtnldvlLRRFENGL----DTLVAdiQLSGGE 474
Cdd:COG1101   82 IGRVFQDPMMgtAPSMTIEENLalayrrgkrrGLRRGLTKKRRELFREL------LATLGLGLenrlDTKVG--LLSGGQ 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493533268 475 RQLVALARALVSNPRLLILDEITANIDSKTEEIIqntlLGL-----RSEGIIVLMVAHRLSTVL-LSDRVALISNGVIV 547
Cdd:COG1101  154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALV----LELtekivEENNLTTLMVTHNMEQALdYGNRLIMMHEGRII 228

PRK10851

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

337-555

1.64e-27

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 113.64 E-value: 1.64e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLRPYIGFVEQ 416
Cdd:PRK10851   2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 TPTLFEKCTLLENITLG-----------RSISKASLENIFERTNLDVLLRRFENgldtlvadiQLSGGERQLVALARALV 485
Cdd:PRK10851  82 HYALFRHMTVFDNIAFGltvlprrerpnAAAIKAKVTQLLEMVQLAHLADRYPA---------QLSGGQKQRVALARALA 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268 486 SNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNEL 555
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMeVADRVVVMSQGNIEQAGTPDQV 224

PRK10908

cell division ATP-binding protein FtsE;

338-554

2.46e-27

cell division ATP-binding protein FtsE;

Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 109.96 E-value: 2.46e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGY-GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS---NSAL--LRPYI 411
Cdd:PRK10908   2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlkNREVpfLRRQI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 412 GFVEQTPTLFEKCTLLENITLGRSISKASLENIFERTN--LDV--LLRRFENgldtlvADIQLSGGERQLVALARALVSN 487
Cdd:PRK10908  82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSaaLDKvgLLDKAKN------FPIQLSGGEQQRVGIARAVVNK 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 488 PRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSD-RVALISNGVIVAsGTHNE 554
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHLHG-GVGGE 222

ModF

COG1119

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...

338-556

2.48e-27

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: 110.56 E-value: 2.48e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSG-TIYINGDPVSNSAL--LRPYIGFV 414
Cdd:COG1119    4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVweLRKRIGLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 eqTPTLFEKCTLLEN------------ITLGRSISKAslenifERTNLDVLLRRFenGLDTLvADI---QLSGGERQLVA 479
Cdd:COG1119   84 --SPALQLRFPRDETvldvvlsgffdsIGLYREPTDE------QRERARELLELL--GLAHL-ADRpfgTLSQGEQRRVL 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493533268 480 LARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGII-VLMVAHRLSTVLLS-DRVALISNGVIVASGTHNELL 556
Cdd:COG1119  153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPtLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231

livF

PRK11614

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

338-556

2.71e-27

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

Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 110.35 E-value: 2.71e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN---SALLRPYIGFV 414
Cdd:PRK11614   6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtAKIMREAVAIV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQTPTLFEKCTLLENITLG-----RSISKASLENIFertnlDVLLRRFENGLDTLVAdiqLSGGERQLVALARALVSNPR 489
Cdd:PRK11614  86 PEGRRVFSRMTVEENLAMGgffaeRDQFQERIKWVY-----ELFPRLHERRIQRAGT---MSGGEQQMLAIGRALMSQPR 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 490 LLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELL 556
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALkLADRGYVLENGHVVLEDTGDALL 225

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

346-541

3.80e-27

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 108.48 E-value: 3.80e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 346 GYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTiyingdpVSNSALLRPyiGFVEQTPTLFEK-- 423
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT-------VRRAGGARV--AYVPQRSEVPDSlp 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 424 CTLLENITLGR-----------SISKASLENIFERTNLDVLLRRfenGLDTLvadiqlSGGERQLVALARALVSNPRLLI 492
Cdd:NF040873  72 LTVRDLVAMGRwarrglwrrltRDDRAAVDDALERVGLADLAGR---QLGEL------SGGQRQRALLAQGLAQEADLLL 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 493533268 493 LDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRVALI 541
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191

DppD

COG0444

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...

355-557

4.89e-27

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: 111.68 E-value: 4.89e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 355 GLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQ---SGTIYINGDPVSN--SALLRPY----IGFVEQTP------- 418
Cdd:COG0444   23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKlsEKELRKIrgreIQMIFQDPmtslnpv 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 419 -TLFEkcTLLENITLGRSISKASLENIFERtnldvLLRRFenGLDTLVADI-----QLSGGERQLVALARALVSNPRLLI 492
Cdd:COG0444  103 mTVGD--QIAEPLRIHGGLSKAEARERAIE-----LLERV--GLPDPERRLdryphELSGGMRQRVMIARALALEPKLLI 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493533268 493 LDEITANIDSkteeIIQ----NTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLK 557
Cdd:COG0444  174 ADEPTTALDV----TIQaqilNLLKDLQRElGLAILFITHDLGVVAeIADRVAVMYAGRIVEEGPVEELFE 240

fecE

PRK11231

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

337-569

6.46e-27

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

Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 109.72 E-value: 6.46e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSA--LLRPYIGFV 414
Cdd:PRK11231   2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSsrQLARRLALL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQTPTLFEKCTLLENITLGRS--------IS---KASLENIFERTNLDVLLRRfengldtLVADiqLSGGERQLVALARA 483
Cdd:PRK11231  82 PQHHLTPEGITVRELVAYGRSpwlslwgrLSaedNARVNQAMEQTRINHLADR-------RLTD--LSGGQRQRAFLAMV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 484 LVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLkTSSEY 562
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASrYCDHLVVLANGHVMAQGTPEEVM-TPGLL 231


                 ....*..
gi 493533268 563 KKLYSLQ 569
Cdd:PRK11231 232 RTVFDVE 238

ABC_6TM_bac_exporter_ABCB8_10_like

cd18576

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...

26-286

7.90e-27

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: 110.27 E-value: 7.90e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  26 AAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLEKMF 105
Cdd:cd18576    1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 106 VLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIMFFNIMV 185
Cdd:cd18576   81 RLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 186 EKRSKVEREkfgELAGVTSNIIDNMKLIRIAMPFA---WVMNffdRFQG--DHIYagKRFIKSIKIAGTLKTSINGLISF 260
Cdd:cd18576  161 RKLSKKVQD---ELAEANTIVEETLQGIRVVKAFTredYEIE---RYRKalERVV--KLALKRARIRALFSSFIIFLLFG 232

                        250       260
                 ....*....|....*....|....*....
gi 493533268 261 SLLA---YGGYLVMKGEITVGILMTFWAY 286
Cdd:cd18576  233 AIVAvlwYGGRLVLAGELTAGDLVAFLLY 261

ABCG_White

cd03234

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...

350-550

1.10e-26

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: 108.13 E-value: 1.10e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 350 KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQ---KPQSGTIYINGDPVSnSALLRPYIGFVEQTPTLFEKCTL 426
Cdd:cd03234   20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRK-PDQFQKCVAYVRQDDILLPGLTV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 427 LENIT------LGRSISKASLENIFErtnlDVLLRRFEnglDTLVADI---QLSGGERQLVALARALVSNPRLLILDEIT 497
Cdd:cd03234   99 RETLTytailrLPRKSSDAIRKKRVE----DVLLRDLA---LTRIGGNlvkGISGGERRRVSIAVQLLWDPKVLILDEPT 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 498 ANIDSKTEEIIQNTLLGLRSEGIIVLMVAH--RLSTVLLSDRVALISNGVIVASG 550
Cdd:cd03234  172 SGLDSFTALNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226

ABC_Carb_Monos_II

cd03215

Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...

353-544

1.67e-26

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: 106.36 E-value: 1.67e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV---SNSALLRPYIGFV---EQTPTLFEKCTL 426
Cdd:cd03215   16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrrSPRDAIRAGIAYVpedRKREGLVLDLSV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 427 LENITLGRsiskaslenifertnldvllrrfengldtlvadiQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEE 506
Cdd:cd03215   96 AENIALSS----------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 493533268 507 IIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNG 544
Cdd:cd03215  142 EIYRLIRELADAGKAVLLISSELDELLgLCDRILVMYEG 180

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

313-556

1.70e-26

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: 113.36 E-value: 1.70e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  313 RTIEVLEAPEEERS----NSSPKLEDV--RSISLENiafgyGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGL 386
Cdd:TIGR03269 259 VFMEGVSEVEKECEvevgEPIIKVRNVskRYISVDR-----GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGV 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  387 QKPQSGTIYIN-GDP--------VSNSALLRPYIGFVEQTPTLFEKCTLLENITlgRSIskaSLENIFE---RTNLDVLL 454
Cdd:TIGR03269 334 LEPTSGEVNVRvGDEwvdmtkpgPDGRGRAKRYIGILHQEYDLYPHRTVLDNLT--EAI---GLELPDElarMKAVITLK 408

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  455 ------RRFENGLDTLVAdiQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAH 527
Cdd:TIGR03269 409 mvgfdeEKAEEILDKYPD--ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSH 486

                         250       260       270
                  ....*....|....*....|....*....|
gi 493533268  528 RLSTVL-LSDRVALISNGVIVASGTHNELL 556
Cdd:TIGR03269 487 DMDFVLdVCDRAALMRDGKIVKIGDPEEIV 516

PTZ00265

multidrug resistance protein (mdr1); Provisional

321-543

1.95e-26

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 114.74 E-value: 1.95e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  321 PEEERSNSSPKLEDVRSISLENIAFGYGNK---QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYIN 397
Cdd:PTZ00265  366 PLVENNDDGKKLKDIKKIQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  398 GD---PVSNSALLRPYIGFVEQTPTLFE-------------------------------------------KCTLLENIT 431
Cdd:PTZ00265  446 DShnlKDINLKWWRSKIGVVSQDPLLFSnsiknnikyslyslkdlealsnyynedgndsqenknkrnscraKCAGDLNDM 525

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  432 LGRSISKASLE-----NIFERTNL-----DVLLRRFENGL----DTLVAD--IQLSGGERQLVALARALVSNPRLLILDE 495
Cdd:PTZ00265  526 SNTTDSNELIEmrknyQTIKDSEVvdvskKVLIHDFVSALpdkyETLVGSnaSKLSGGQKQRISIARAIIRNPKILILDE 605

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 493533268  496 ITANIDSKTEEIIQNTLLGLR-SEGIIVLMVAHRLSTVLLSDRVALISN 543
Cdd:PTZ00265  606 ATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTIRYANTIFVLSN 654

znuC

PRK09544

high-affinity zinc transporter ATPase; Reviewed

338-551

2.55e-26

high-affinity zinc transporter ATPase; Reviewed

Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 107.89 E-value: 2.55e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIyingdpvSNSALLRpyIGFVEQT 417
Cdd:PRK09544   5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------KRNGKLR--IGYVPQK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 ----PTLfeKCTLLENITLGRSISKASLENIFERTNLDVLLRrfengldtlvADIQ-LSGGERQLVALARALVSNPRLLI 492
Cdd:PRK09544  76 lyldTTL--PLTVNRFLRLRPGTKKEDILPALKRVQAGHLID----------APMQkLSGGETQRVLLARALLNRPQLLV 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 493 LDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVLLSDRVALISNGVIVASGT 551
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGT 203

PRK10895

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

341-566

6.67e-26

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 106.52 E-value: 6.67e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 341 ENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL---LRPYIGFVEQT 417
Cdd:PRK10895   7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLharARRGIGYLPQE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PTLFEKCTLLENITLGRSISK-ASLENIFERTNldVLLRRF--ENGLDTLVAdiQLSGGERQLVALARALVSNPRLLILD 494
Cdd:PRK10895  87 ASIFRRLSVYDNLMAVLQIRDdLSAEQREDRAN--ELMEEFhiEHLRDSMGQ--SLSGGERRRVEIARALAANPKFILLD 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493533268 495 EITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRL-STVLLSDRVALISNGVIVASGTHNELLkTSSEYKKLY 566
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL-QDEHVKRVY 234

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

312-547

8.11e-26

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.31 E-value: 8.11e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 312 LRTIEVLEAPEEERSNSSPKL---EDVRS----ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILM 384
Cdd:COG0488  283 IKALEKLEREEPPRRDKTVEIrfpPPERLgkkvLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 385 GLQKPQSGTIYInGDPVSnsallrpyIGFVEQ-TPTLFEKCTLLENITLGRSiskaslenifERTNLDV--LLRRF---E 458
Cdd:COG0488  363 GELEPDSGTVKL-GETVK--------IGYFDQhQEELDPDKTVLDELRDGAP----------GGTEQEVrgYLGRFlfsG 423

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 459 NGLDTLVADiqLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLrsEGIIVLmVAH-R--LSTVllS 535
Cdd:COG0488  424 DDAFKPVGV--LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PGTVLL-VSHdRyfLDRV--A 496

                        250
                 ....*....|..
gi 493533268 536 DRVALISNGVIV 547
Cdd:COG0488  497 TRILEFEDGGVR 508

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

325-555

1.41e-25

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 110.53 E-value: 1.41e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 325 RSNSSPK-LEDVRSISLEniafgYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN 403
Cdd:PRK15439   3 TSDTTAPpLLCARSISKQ-----YSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 404 salLRPY------IGFVEQTPTLFEKCTLLENITLGRSISKASLEnifertNLDVLLRRFENGLDTLVADIQLSGGERQL 477
Cdd:PRK15439  78 ---LTPAkahqlgIYLVPQEPLLFPNLSVKENILFGLPKRQASMQ------KMKQLLAALGCQLDLDSSAGSLEVADRQI 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493533268 478 VALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNEL 555
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRqLADRISVMRDGTIALSGKTADL 227

ssuB

PRK11247

aliphatic sulfonates transport ATP-binding subunit; Provisional

338-546

1.54e-25

aliphatic sulfonates transport ATP-binding subunit; Provisional

Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 105.92 E-value: 1.54e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAllrpyigfvEQT 417
Cdd:PRK11247  13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR---------EDT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PTLFEKCTLL------ENITLG-----RSISKASLENIfertnldvllrrfenGLDTLVAD--IQLSGGERQLVALARAL 484
Cdd:PRK11247  84 RLMFQDARLLpwkkviDNVGLGlkgqwRDAALQALAAV---------------GLADRANEwpAALSGGQKQRVALARAL 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493533268 485 VSNPRLLILDEITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAHRLS-TVLLSDRVALISNGVI 546
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212

cbiO

PRK13635

energy-coupling factor ABC transporter ATP-binding protein;

338-565

3.05e-25

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.48 E-value: 3.05e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGN--KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGF 413
Cdd:PRK13635   6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwdVRRQVGM 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTP-TLFEKCTL-------LENITLGRsiskaslENIFERTNLDVLLRRFENGLDTLVAdiQLSGGERQLVALARALV 485
Cdd:PRK13635  86 VFQNPdNQFVGATVqddvafgLENIGVPR-------EEMVERVDQALRQVGMEDFLNREPH--RLSGGQKQRVAIAGVLA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 486 SNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYKK 564
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHMLQE 236


                 .
gi 493533268 565 L 565
Cdd:PRK13635 237 I 237

cbiO

PRK13650

energy-coupling factor transporter ATPase;

338-565

3.25e-25

energy-coupling factor transporter ATPase;

Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.58 E-value: 3.25e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQ---ILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIG 412
Cdd:PRK13650   5 IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRHKIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTP-TLFEKCTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTLVAdiQLSGGERQLVALARALVSNPRLL 491
Cdd:PRK13650  85 MVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPA--RLSGGQKQRVAIAGAVAMRPKII 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 492 ILDEITANIDSKTE-EIIQnTLLGLRSE-GIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYKKL 565
Cdd:PRK13650 163 ILDEATSMLDPEGRlELIK-TIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLLQL 237

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

338-550

3.71e-25

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 109.10 E-value: 3.71e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING---DPVSNSALLRPYIGFV 414
Cdd:PRK09700   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinyNKLDHKLAAQLGIGII 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQTPTLFEKCTLLENITLGRSISKASLE-NI----FERTNLDVLLRR--FENGLDTLVADIQLSggERQLVALARALVSN 487
Cdd:PRK09700  86 YQELSVIDELTVLENLYIGRHLTKKVCGvNIidwrEMRVRAAMMLLRvgLKVDLDEKVANLSIS--HKQMLEIAKTLMLD 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493533268 488 PRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASG 550
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRrICDRYTVMKDGSSVCSG 227

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

73-557

3.85e-25

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

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 110.81 E-value: 3.85e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268    73 GSLIFTYfgEVVFETTALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQ-ITA 151
Cdd:TIGR00957 1019 GFAVFGY--SMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNvIGA 1096

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   152 ILAIMFAFN-WKLTLLPLGFIVFsfLVIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRIampfawvmnfFDRfQ 230
Cdd:TIGR00957 1097 LIVILLATPiAAVIIPPLGLLYF--FVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRA----------FEE-Q 1163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   231 GDHIYagkrfIKSIKIAGTLKTSINGLISFSLLAYGGYLVmkGEITVGILMTFWAYVQSLFNP----------IQLLMQV 300
Cdd:TIGR00957 1164 ERFIH-----QSDLKVDENQKAYYPSIVANRWLAVRLECV--GNCIVLFAALFAVISRHSLSAglvglsvsysLQVTFYL 1236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   301 NILLRQSWGGLLRTIEV----------LEAPEEERSNSSPK-LEDVRSISLENIAFGY--GNKQILKGLSLELRKGEITT 367
Cdd:TIGR00957 1237 NWLVRMSSEMETNIVAVerlkeyseteKEAPWQIQETAPPSgWPPRGRVEFRNYCLRYreDLDLVLRHINVTIHGGEKVG 1316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   368 LVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGFVEQTPTLFEKcTLLENITLGRSISKASLENIF 445
Cdd:TIGR00957 1317 IVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLhdLRFKITIIPQDPVLFSG-SLRMNLDPFSQYSDEEVWWAL 1395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   446 ERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLgLRSEGIIVL 523
Cdd:TIGR00957 1396 ELAHLKTFVSALPDKLDHECAEggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR-TQFEDCTVL 1474

                          490       500       510
                   ....*....|....*....|....*....|....
gi 493533268   524 MVAHRLSTVLLSDRVALISNGVIVASGTHNELLK 557
Cdd:TIGR00957 1475 TIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQ 1508

PRK11264

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

338-556

4.32e-25

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

Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.45 E-value: 4.32e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYInGDPVSNSAL----------- 406
Cdd:PRK11264   4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTARslsqqkglirq 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 407 LRPYIGFVEQTPTLFEKCTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTLVADiQLSGGERQLVALARALVS 486
Cdd:PRK11264  83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPR-RLSGGQQQRVAIARALAM 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493533268 487 NPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELL 556
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALF 232

PRK10247

putative ABC transporter ATP-binding protein YbbL; Provisional

340-527

5.14e-25

putative ABC transporter ATP-binding protein YbbL; Provisional

Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 103.26 E-value: 5.14e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 340 LENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIGFVEQT 417
Cdd:PRK10247  10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlKPEIYRQQVSYCAQT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PTLFEKcTLLENITLGRSI-SKASLENIFERTnldvlLRRFENGLDTLVADI-QLSGGERQLVALARALVSNPRLLILDE 495
Cdd:PRK10247  90 PTLFGD-TVYDNLIFPWQIrNQQPDPAIFLDD-----LERFALPDTILTKNIaELSGGEKQRISLIRNLQFMPKVLLLDE 163

                        170       180       190
                 ....*....|....*....|....*....|...
gi 493533268 496 ITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAH 527
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYvREQNIAVLWVTH 196

lolD

PRK11629

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

352-530

5.24e-25

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 103.74 E-value: 5.24e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 352 ILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS-----NSALLRPY-IGFVEQTPTLFEKCT 425
Cdd:PRK11629  24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssaAKAELRNQkLGFIYQFHHLLPDFT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 426 LLENITLGRSISKASLENIFERTnLDVLLrrfENGLDTLVA--DIQLSGGERQLVALARALVSNPRLLILDEITANIDSK 503
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRA-LEMLA---AVGLEHRANhrPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179

                        170       180
                 ....*....|....*....|....*...
gi 493533268 504 TEEIIQNTLLGL-RSEGIIVLMVAHRLS 530
Cdd:PRK11629 180 NADSIFQLLGELnRLQGTAFLVVTHDLQ 207

ABC_6TM_exporter_like

cd18563

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

24-301

6.31e-25

Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 104.90 E-value: 6.31e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETtaLMAK------SDLR 97
Cdd:cd18563    2 ILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGR--LLARlgeritADLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  98 KQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLV 177
Cdd:cd18563   80 RDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 178 IMFFNIMVEKRSKVEREKFGELAGVTSNIIDNmklIRIAMPFAWVMNFFDRFQGDHIYAGKRFIKSIKIAGTLKTSINGL 257
Cdd:cd18563  160 SYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPG---IRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFL 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 493533268 258 ISFSLL---AYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVN 301
Cdd:cd18563  237 TSLGTLivwYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLN 283

MglA

COG1129

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

346-548

1.01e-24

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.80 E-value: 1.01e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 346 GYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV---SNSALLRPYIGFV-E--QTPT 419
Cdd:COG1129  261 GLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrirSPRDAIRAGIAYVpEdrKGEG 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 420 LFEKCTLLENITL--------GRSISKASLENIFERtnldvLLRRFE---NGLDTLVAdiQLSGGERQLVALARALVSNP 488
Cdd:COG1129  341 LVLDLSIRENITLasldrlsrGGLLDRRRERALAEE-----YIKRLRiktPSPEQPVG--NLSGGNQQKVVLAKWLATDP 413

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493533268 489 RLLILDEITANID--SKTEeiIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVA 548
Cdd:COG1129  414 KVLILDEPTRGIDvgAKAE--IYRLIRELAAEGKAVIVISSELPELLgLSDRILVMREGRIVG 474

tauB

PRK11248

taurine ABC transporter ATP-binding subunit;

338-544

1.04e-24

taurine ABC transporter ATP-binding subunit;

Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 103.24 E-value: 1.04e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLRpyiGFVEQT 417
Cdd:PRK11248   2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---GVVFQN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PTLFEKCTLLENITLG---RSISKASLENIFERTNLDVLLRRFENGLdtlvadI-QLSGGERQLVALARALVSNPRLLIL 493
Cdd:PRK11248  79 EGLLPWRNVQDNVAFGlqlAGVEKMQRLEIAHQMLKKVGLEGAEKRY------IwQLSGGQRQRVGIARALAANPQLLLL 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493533268 494 DEITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAHRL-STVLLSDRVALISNG 544
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIeEAVFMATELVLLSPG 205

AppF

COG4608

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

355-555

1.08e-24

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

Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 105.20 E-value: 1.08e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 355 GLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPY---IGFVEQTP--------TLF 421
Cdd:COG4608   36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITglSGRELRPLrrrMQMVFQDPyaslnprmTVG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 422 EkcTLLENITLGRSISKASLEnifERTNldVLLRRFenGLDTLVAD---IQLSGGERQLVALARALVSNPRLLILDEITA 498
Cdd:COG4608  116 D--IIAEPLRIHGLASKAERR---ERVA--ELLELV--GLRPEHADrypHEFSGGQRQRIGIARALALNPKLIVCDEPVS 186

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493533268 499 NID-SkteeiIQ----NTLLGLRSE-GIIVLMVAHRLSTV-LLSDRVALISNGVIVASGTHNEL 555
Cdd:COG4608  187 ALDvS-----IQaqvlNLLEDLQDElGLTYLFISHDLSVVrHISDRVAVMYLGKIVEIAPRDEL 245

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

338-549

1.18e-24

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: 107.60 E-value: 1.18e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGL--QKPQSGTIYINGDPVSNSALL---RPYIG 412
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRdteRAGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  413 FVEQTPTLFEKCTLLENITLGRSISKASlenifERTNLDVLLRRFENGLDTLVADI--------QLSGGERQLVALARAL 484
Cdd:TIGR02633  82 IIHQELTLVPELSVAENIFLGNEITLPG-----GRMAYNAMYLRAKNLLRELQLDAdnvtrpvgDYGGGQQQLVEIAKAL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268  485 VSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVIVAS 549
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVkAVCDTICVIRDGQHVAT 222

thiQ

PRK10771

thiamine ABC transporter ATP-binding protein ThiQ;

338-556

2.33e-24

thiamine ABC transporter ATP-binding protein ThiQ;

Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.58 E-value: 2.33e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILkgLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLRPYIGFVEQT 417
Cdd:PRK10771   2 LKLTDITWLYHHLPMR--FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PTLFEKCTLLENITLG-------RSISKASLENIFERTNLDVLLRRFENgldtlvadiQLSGGERQLVALARALVSNPRL 490
Cdd:PRK10771  80 NNLFSHLTVAQNIGLGlnpglklNAAQREKLHAIARQMGIEDLLARLPG---------QLSGGQRQRVALARCLVREQPI 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268 491 LILDEITANIDSKteeiIQNTLLGL-----RSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELL 556
Cdd:PRK10771 151 LLLDEPFSALDPA----LRQEMLTLvsqvcQERQLTLLMVSHSLEDAArIAPRSLVVADGRIAWDGPTDELL 218

YnjD

COG4136

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...

337-527

2.45e-24

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

Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.02 E-value: 2.45e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQ---SGTIYINGDPVSNSALLRPYIGF 413
Cdd:COG4136    1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPTLFEKCTLLENI------TLGRSISKASLENIFERTNLDVLLRRFengldtlVAdiQLSGGERQLVALARALVSN 487
Cdd:COG4136   81 LFQDDLLFPHLSVGENLafalppTIGRAQRRARVEQALEEAGLAGFADRD-------PA--TLSGGQRARVALLRALLAE 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 493533268 488 PRLLILDEITANIDSK-TEEIIQNTLLGLRSEGIIVLMVAH 527
Cdd:COG4136  152 PRALLLDEPFSKLDAAlRAQFREFVFEQIRQRGIPALLVTH 192

PRK10584

putative ABC transporter ATP-binding protein YbbA; Provisional

346-527

2.93e-24

putative ABC transporter ATP-binding protein YbbA; Provisional

Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 101.39 E-value: 2.93e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 346 GYGNKQ--ILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN-----SALLRP-YIGFVEQT 417
Cdd:PRK10584  17 GQGEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeaRAKLRAkHVGFVFQS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PTLFEKCTLLENITL-----GRSISKAslenifeRTNLDVLLRRFENG--LDTLVAdiQLSGGERQLVALARALVSNPRL 490
Cdd:PRK10584  97 FMLIPTLNALENVELpallrGESSRQS-------RNGAKALLEQLGLGkrLDHLPA--QLSGGEQQRVALARAFNGRPDV 167

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 493533268 491 LILDEITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAH 527
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTH 205

PstB

COG1117

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

338-550

3.02e-24

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

Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 102.04 E-value: 3.02e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTT---TLNILMGLQkPQ---SGTIYING----DPVSNSALL 407
Cdd:COG1117   12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLI-PGarvEGEILLDGediyDPDVDVVEL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 408 RPYIGFVEQTPTLFEKcTLLENITLGRSI----SKASLENIFERTnldvlLRR-----------FENGLDtlvadiqLSG 472
Cdd:COG1117   91 RRRVGMVFQKPNPFPK-SIYDNVAYGLRLhgikSKSELDEIVEES-----LRKaalwdevkdrlKKSALG-------LSG 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493533268 473 GERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVlMVAHRLS-TVLLSDRVALISNGVIVASG 550
Cdd:COG1117  158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIV-IVTHNMQqAARVSDYTAFFYLGELVEFG 235

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

339-561

3.08e-24

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 106.15 E-value: 3.08e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 339 SLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV---SNSALLRPYIGFVE 415
Cdd:PRK11288   6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGVAIIY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 416 QTPTLFEKCTLLENITLGRSISKASLENifERTnldvLLRRFENGLDTLVADI-------QLSGGERQLVALARALVSNP 488
Cdd:PRK11288  86 QELHLVPEMTVAENLYLGQLPHKGGIVN--RRL----LNYEAREQLEHLGVDIdpdtplkYLSIGQRQMVEIAKALARNA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493533268 489 RLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVAsgTHNELLKTSSE 561
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFaLCDAITVFKDGRYVA--TFDDMAQVDRD 231

PRK14247

phosphate ABC transporter ATP-binding protein; Provisional

338-556

3.41e-24

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 101.91 E-value: 3.41e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGL----QKPQ-SGTIYINGDPV--SNSALLRPY 410
Cdd:PRK14247   4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielyPEARvSGEVYLDGQDIfkMDVIELRRR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 411 IGFVEQTPTLFEKCTLLENITLGRSISK--ASLENIFERTNLDV----LLRRFENGLDTLVAdiQLSGGERQLVALARAL 484
Cdd:PRK14247  84 VQMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALekaqLWDEVKDRLDAPAG--KLSGGQQQRLCIARAL 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268 485 VSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELL 556
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233

nickel_nikE

TIGR02769

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...

348-547

4.31e-24

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: 101.81 E-value: 4.31e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  348 GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRpyiGFVEQTPTLFEKCT 425
Cdd:TIGR02769  22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqlDRKQRR---AFRRDVQLVFQDSP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  426 LLEN--ITLGRSISK-----ASLENIFERTNLDVLLRrfENGLDTLVAD---IQLSGGERQLVALARALVSNPRLLILDE 495
Cdd:TIGR02769  99 SAVNprMTVRQIIGEplrhlTSLDESEQKARIAELLD--MVGLRSEDADklpRQLSGGQLQRINIARALAVKPKLIVLDE 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 493533268  496 ITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIV 547
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQsFCQRVAVMDKGQIV 230

PRK13549

xylose transporter ATP-binding subunit; Provisional

342-544

4.45e-24

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 105.78 E-value: 4.45e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 342 NIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQkPQ---SGTIYINGDPVSNSALL---RPYIGFVE 415
Cdd:PRK13549  10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRdteRAGIAIIH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 416 QTPTLFEKCTLLENITLGRSISKasleniFERTNLDVLLRRFENGLDTLVADI-------QLSGGERQLVALARALVSNP 488
Cdd:PRK13549  89 QELALVKELSVLENIFLGNEITP------GGIMDYDAMYLRAQKLLAQLKLDInpatpvgNLGLGQQQLVEIAKALNKQA 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268 489 RLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNG 544
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKaISDTICVIRDG 219

metN

PRK11153

DL-methionine transporter ATP-binding subunit; Provisional

338-551

4.83e-24

DL-methionine transporter ATP-binding subunit; Provisional

Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 103.34 E-value: 4.83e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIA--FGYGNKQI--LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV---SNSAL--LR 408
Cdd:PRK11153   2 IELKNISkvFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKELrkAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 409 PYIGFVEQTPTLFEKCTLLENITLGRSISKASLENIFERTN--LDVLlrrfenGL----DTLVAdiQLSGGERQLVALAR 482
Cdd:PRK11153  82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTelLELV------GLsdkaDRYPA--QLSGGQKQRVAIAR 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493533268 483 ALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTV-LLSDRVALISNGVIVASGT 551
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

356-551

5.37e-24

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: 107.41 E-value: 5.37e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   356 LSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING-DPVSNSALLRPYIGFVEQTPTLFEKCTLLENITL-- 432
Cdd:TIGR01257  949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFya 1028

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   433 ---GRSISKASLE--NIFERTNLDvlLRRFENGLDtlvadiqLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEI 507
Cdd:TIGR01257 1029 qlkGRSWEEAQLEmeAMLEDTGLH--HKRNEEAQD-------LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 493533268   508 IQNTLLGLRSEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGT 551
Cdd:TIGR01257 1100 IWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143

glnQ

PRK09493

glutamine ABC transporter ATP-binding protein GlnQ;

338-559

5.70e-24

glutamine ABC transporter ATP-binding protein GlnQ;

Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 100.94 E-value: 5.70e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING----DPVSNSALLRPYIGF 413
Cdd:PRK09493   2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvnDPKVDERLIRQEAGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPTLFEKCTLLENITLG----RSISKASLENIFERtnldvLLRRFenGLDTLVADI--QLSGGERQLVALARALVSN 487
Cdd:PRK09493  82 VFQQFYLFPHLTALENVMFGplrvRGASKEEAEKQARE-----LLAKV--GLAERAHHYpsELSGGQQQRVAIARALAVK 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493533268 488 PRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLKTS 559
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEkVASRLIFIDKGRIAEDGDPQVLIKNP 227

ABC_6TM_Rv0194_D1_like

cd18543

Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...

24-297

5.87e-24

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: 102.18 E-value: 5.87e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLEK 103
Cdd:cd18543    2 ILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 104 MFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVfPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIMFFNI 183
Cdd:cd18543   82 LQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFG-PFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 184 MVEKRSKVEREKFGELAGVtsnIIDNMKLIRIAMPFA---WVMNFFDRfQGDHIYAGKrfIKSIKIAGTLKTSINGLISF 260
Cdd:cd18543  161 RYFPASRRAQDQAGDLATV---VEESVTGIRVVKAFGrerRELDRFEA-AARRLRATR--LRAARLRARFWPLLEALPEL 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 493533268 261 SL---LAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLL 297
Cdd:cd18543  235 GLaavLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRML 274

ccmA

TIGR01189

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...

338-527

6.31e-24

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: 99.36 E-value: 6.31e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLRP----YIGf 413
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHenilYLG- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  414 veQTPTLFEKCTLLENITLGRSISKASLENIFERTNlDVLLRRFEnglDTLVAdiQLSGGERQLVALARALVSNPRLLIL 493
Cdd:TIGR01189  80 --HLPGLKPELSALENLHFWAAIHGGAQRTIEDALA-AVGLTGFE---DLPAA--QLSAGQQRRLALARLWLSRRPLWIL 151

                         170       180       190
                  ....*....|....*....|....*....|....
gi 493533268  494 DEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAH 527
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185

cbiO

PRK13637

energy-coupling factor transporter ATPase;

337-570

7.06e-24

energy-coupling factor transporter ATPase;

Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 101.66 E-value: 7.06e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYG-----NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING----DPVSNSALL 407
Cdd:PRK13637   2 SIKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditDKKVKLSDI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 408 RPYIGFVEQTP--TLFEKcTLLENITLGRSISKASLENIFERT--NLDVLLRRFENGLDTlvADIQLSGGERQLVALARA 483
Cdd:PRK13637  82 RKKVGLVFQYPeyQLFEE-TIEKDIAFGPINLGLSEEEIENRVkrAMNIVGLDYEDYKDK--SPFELSGGQKRRVAIAGV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 484 LVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLKtssE 561
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAkLADRIIVMNKGKCELQGTPREVFK---E 235


                 ....*....
gi 493533268 562 YKKLYSLQL 570
Cdd:PRK13637 236 VETLESIGL 244

cbiO

PRK13639

cobalt transporter ATP-binding subunit; Provisional

338-555

5.05e-23

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.00 E-value: 5.05e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGN-KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV--SNSALL--RPYIG 412
Cdd:PRK13639   2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLevRKTVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTP--TLFEKcTLLENITLGRSISKASLENIFERTN---LDVLLRRFENGldtlvADIQLSGGERQLVALARALVSN 487
Cdd:PRK13639  82 IVFQNPddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKealKAVGMEGFENK-----PPHHLSGGQKKRVAIAGILAMK 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493533268 488 PRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVIVASGTHNEL 555
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

340-495

5.09e-23

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.84 E-value: 5.09e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 340 LENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDpvsnsalLRpyIGFVEQTPT 419
Cdd:COG0488    1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-------LR--IGYLPQEPP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 420 LFEKCTLLENITLG-----------RSISKASLENIFERTNLDVLLRRFE---------------NGL-------DTLVA 466
Cdd:COG0488   72 LDDDLTVLDTVLDGdaelraleaelEELEAKLAEPDEDLERLAELQEEFEalggweaearaeeilSGLgfpeedlDRPVS 151

                        170       180
                 ....*....|....*....|....*....
gi 493533268 467 DiqLSGGERQLVALARALVSNPRLLILDE 495
Cdd:COG0488  152 E--LSGGWRRRVALARALLSEPDLLLLDE 178

nikE

PRK10419

nickel ABC transporter ATP-binding protein NikE;

348-560

6.06e-23

nickel ABC transporter ATP-binding protein NikE;

Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.61 E-value: 6.06e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 348 GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSnsALLRPYIG-FVEQTPTLFEKCTL 426
Cdd:PRK10419  23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLA--KLNRAQRKaFRRDIQMVFQDSIS 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 427 LEN--ITLGRSISK-----ASLENIFERTNLDVLLRrfENGLDTLVAD---IQLSGGERQLVALARALVSNPRLLILDEI 496
Cdd:PRK10419 101 AVNprKTVREIIREplrhlLSLDKAERLARASEMLR--AVDLDDSVLDkrpPQLSGGQLQRVCLARALAVEPKLLILDEA 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 497 TANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTV-LLSDRVALISNGVIVASGTHNELLKTSS 560
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVeRFCQRVMVMDNGQIVETQPVGDKLTFSS 244

PLN03232

ABC transporter C family member; Provisional

175-565

8.52e-23

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 103.52 E-value: 8.52e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  175 FLVIMFFNIMVEKRSKVEREKF---GELAGVTSNIIDNMKLIRIampFAWVMNFFDRFQGDHIYAGKRFIKSIKIAGTLK 251
Cdd:PLN03232  451 FLLIPLQTLIVRKMRKLTKEGLqwtDKRVGIINEILASMDTVKC---YAWEKSFESRIQGIRNEELSWFRKAQLLSAFNS 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  252 TSINGL-ISFSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQvniLLRQSWGG--LLRTIEVLEAPEEERSNS 328
Cdd:PLN03232  528 FILNSIpVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPN---LLSQVVNAnvSLQRIEELLLSEERILAQ 604

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  329 SPKLE-DVRSISLENIAFGYGNKQ---ILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTiyingdpvsnS 404
Cdd:PLN03232  605 NPPLQpGAPAISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS----------S 674

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  405 ALLRPYIGFVEQTPTLFeKCTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALAR 482
Cdd:PLN03232  675 VVIRGSVAYVPQVSWIF-NATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGErgVNISGGQKQRVSMAR 753

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  483 ALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEY 562
Cdd:PLN03232  754 AVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLF 833


                  ...
gi 493533268  563 KKL 565
Cdd:PLN03232  834 KKL 836

YddA

COG4178

ABC-type uncharacterized transport system, permease and ATPase components [General function ...

310-538

8.71e-23

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

Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.19 E-value: 8.71e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 310 GLLRTIEVLEAPEEERSNssPKLEDVRSISLENIA-FGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQK 388
Cdd:COG4178  337 GFEEALEAADALPEAASR--IETSEDGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWP 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 389 PQSGTIYIngdPVSNSALL---RPYI--GfveqtptlfekcTLLENIT---LGRSISKASLENIFERTNLDVLLRRFENG 460
Cdd:COG4178  415 YGSGRIAR---PAGARVLFlpqRPYLplG------------TLREALLypaTAEAFSDAELREALEAVGLGHLAERLDEE 479

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 461 LDTlvaDIQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEE----IIQNTLlglrsEGIIVLMVAHRLSTVLLSD 536
Cdd:COG4178  480 ADW---DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAalyqLLREEL-----PGTTVISVGHRSTLAAFHD 551


                 ..
gi 493533268 537 RV 538
Cdd:COG4178  552 RV 553

ABC_6TM_Sav1866_like

cd18554

Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...

24-313

1.03e-22

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: 98.65 E-value: 1.03e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVG-VMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFT-------YFGEVVFETTALMAKSD 95
Cdd:cd18554    1 IIITIVIGlVRFGIPLLLPLILKYIVDDVIQGSSLTLDEKVYKLFTIIGIMFFIFLilrppveYYRQYFAQWIANKILYD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  96 LRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSF 175
Cdd:cd18554   81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 176 LVIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIR-IAMPFAWVMNFFDRFQGDHIYAgkrfIKSIKIAGTLKTSI 254
Cdd:cd18554  161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKsFALEKHEQKQFDKRNGHFLTRA----LKHTRWNAKTFSAV 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268 255 NGLISFSLL---AYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQSWGGLLR 313
Cdd:cd18554  237 NTITDLAPLlviGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDR 298

PRK14239

phosphate transporter ATP-binding protein; Provisional

338-544

1.27e-22

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.15 E-value: 1.27e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNIL--MGLQKPQ---SGTIYING----DPVSNSALLR 408
Cdd:PRK14239   6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGhniySPRTDTVDLR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 409 PYIGFVEQTPTLFeKCTLLENITLGRSIS----KASLENIFERTNLDVLLrrFENGLDTLVAD-IQLSGGERQLVALARA 483
Cdd:PRK14239  86 KEIGMVFQQPNPF-PMSIYENVVYGLRLKgikdKQVLDEAVEKSLKGASI--WDEVKDRLHDSaLGLSGGQQQRVCIARV 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493533268 484 LVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRVALISNG 544
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDG 223

btuD

PRK09536

corrinoid ABC transporter ATPase; Reviewed

338-558

1.32e-22

corrinoid ABC transporter ATPase; Reviewed

Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 100.30 E-value: 1.32e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN--SALLRPYIGFVE 415
Cdd:PRK09536   4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlsARAASRRVASVP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 416 QTPTLFEKCTLLENITLGR-----------SISKASLENIFERTNLDVLLRRfengldtlvADIQLSGGERQLVALARAL 484
Cdd:PRK09536  84 QDTSLSFEFDVRQVVEMGRtphrsrfdtwtETDRAAVERAMERTGVAQFADR---------PVTSLSGGERQRVLLARAL 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493533268 485 VSNPRLLILDEITANID----SKTEEIIQNtllgLRSEGIIVLMVAHRLS-TVLLSDRVALISNGVIVASGTHNELLKT 558
Cdd:PRK09536 155 AQATPVLLLDEPTASLDinhqVRTLELVRR----LVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTA 229

PTZ00265

multidrug resistance protein (mdr1); Provisional

338-568

1.65e-22

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 102.41 E-value: 1.65e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  338 ISLENIAFGY---GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGL----------------------QKPQ-- 390
Cdd:PTZ00265 1166 IEIMDVNFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneQDYQgd 1245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  391 ------------------------------SGTIYINGDPVSNSAL--LRPYIGFVEQTPTLFEKcTLLENITLGRSisK 438
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLkdLRNLFSIVSQEPMLFNM-SIYENIKFGKE--D 1322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  439 ASLENIFERTN---LDVLLRRFENGLDTLVADI--QLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLL 513
Cdd:PTZ00265 1323 ATREDVKRACKfaaIDEFIESLPNKYDTNVGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268  514 GLRSEG-IIVLMVAHRLSTVLLSDRVALISN----GVIV-ASGTHNELLKTSSE-YKKLYSL 568
Cdd:PTZ00265 1403 DIKDKAdKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVqAHGTHEELLSVQDGvYKKYVKL 1464

ABC_6TM_exporter_like

cd18550

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

24-307

2.64e-22

Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 97.17 E-value: 2.64e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVmiALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTyfgevVFET--TALMAKS---DLRK 98
Cdd:cd18550    4 VLLLILLSA--LLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLG-----VVQTylSARIGQGvmyDLRV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  99 QLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVI 178
Cdd:cd18550   77 QLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 179 MFFNimvEKRSKVEREKFGELAGVTSNI-----IDNMKLIRIampFAWVMNFFDRFQGDhiyAGKrfIKSIKI----AGT 249
Cdd:cd18550  157 RRVG---RRRRKLTREQQEKLAELNSIMqetlsVSGALLVKL---FGREDDEAARFARR---SRE--LRDLGVrqalAGR 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268 250 LKTSINGLISFSLLA----YGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQS 307
Cdd:cd18550  226 WFFAALGLFTAIGPAlvywVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTS 287

ABC_6TM_Pgp_ABCB1_D1_like

cd18577

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...

24-303

2.78e-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: 97.55 E-value: 2.78e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGV-MIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGlWF-----GSLIFTYFGEVVFETTALMAKSDLR 97
Cdd:cd18577    5 LLAAIAAGAaLPLMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYAL-YFvylgiGSFVLSYIQTACWTITGERQARRIR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  98 KQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLV 177
Cdd:cd18577   84 KRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 178 IMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRIampFAWVMNFFDRFQGDHIYAGKRFIKSIKIAGTLKTSINGL 257
Cdd:cd18577  164 GGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKA---FGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFI 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 493533268 258 I--SFSL-LAYGGYLVMKGEITVGILMT-FWAYVQSLFNPIQLLMQVNIL 303
Cdd:cd18577  241 IfaMYALaFWYGSRLVRDGEISPGDVLTvFFAVLIGAFSLGQIAPNLQAF 290

ABC_NatA_like

cd03267

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...

347-550

3.59e-22

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: 95.48 E-value: 3.59e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 347 YGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING-DPVSNSALLRPYIGFV-EQTPTLFEKC 424
Cdd:cd03267   31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWKRRKKFLRRIGVVfGQKTQLWWDL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 425 TLLENITLGRSISKasLENIFERTNLDVL--LRRFENGLDTLVAdiQLSGGERQLVALARALVSNPRLLILDEITANIDS 502
Cdd:cd03267  111 PVIDSFYLLAAIYD--LPPARFKKRLDELseLLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 493533268 503 KTEEIIQNTLLGL-RSEGIIVLMVAHRLSTV-LLSDRVALISNGVIVASG 550
Cdd:cd03267  187 VAQENIRNFLKEYnRERGTTVLLTSHYMKDIeALARRVLVIDKGRLLYDG 236

cbiO

PRK13636

cobalt transporter ATP-binding subunit; Provisional

338-556

5.37e-22

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 96.07 E-value: 5.37e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGN-KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL----LRPYIG 412
Cdd:PRK13636   6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmkLRESVG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTP--TLFEKCTLLE------NITLGRSISKASLENIFERTNLDVLLRRFENGldtlvadiqLSGGERQLVALARAL 484
Cdd:PRK13636  86 MVFQDPdnQLFSASVYQDvsfgavNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHC---------LSFGQKKRVAIAGVL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493533268 485 VSNPRLLILDEITANIDSK-TEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVIVASGTHNELL 556
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMgVSEIMKLLVEMQKELGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVF 230

potG

PRK11607

putrescine ABC transporter ATP-binding subunit PotG;

316-555

5.56e-22

putrescine ABC transporter ATP-binding subunit PotG;

Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.98 E-value: 5.56e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 316 EVLEAPEEERSNSSPKLEDVRsisleNIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIY 395
Cdd:PRK11607   3 DAIPRPQAKTRKALTPLLEIR-----NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 396 INGDPVSNSA-LLRPyIGFVEQTPTLFEKCTLLENITLGRSISKASLENIFERTN--LD-VLLRRFENGldtlvADIQLS 471
Cdd:PRK11607  78 LDGVDLSHVPpYQRP-INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNemLGlVHMQEFAKR-----KPHQLS 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 472 GGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLG-LRSEGIIVLMVAH-RLSTVLLSDRVALISNGVIVAS 549
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQI 231


                 ....*.
gi 493533268 550 GTHNEL 555
Cdd:PRK11607 232 GEPEEI 237

ABC_6TM_exporter_like

cd18540

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

21-300

5.58e-22

Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 96.39 E-value: 5.58e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  21 KRELLAAVLVGVMIALA-VVFPLLIRLLIDVVIPSGDMDLlvkyvllvvglwFGSLIFTYFGEVVFETTA---------- 89
Cdd:cd18540    1 KKLLILLIILMLLVALLdAVFPLLTKYAIDHFITPGTLDG------------LTGFILLYLGLILIQALSvflfirlagk 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  90 ---LMAKsDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLL 166
Cdd:cd18540   69 iemGVSY-DLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALI 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 167 PLGFIVFSFLVIMFF--NIMVEKRsKVERE------KFGE-LAGV----TSNIIDNMkliriampfawvmnfFDRFQGDh 233
Cdd:cd18540  148 VLAVVPVLAVVSIYFqkKILKAYR-KVRKInsritgAFNEgITGAkttkTLVREEKN---------------LREFKEL- 210

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493533268 234 iyAGKRFIKSIK---IAGTLKTSINGLISFSL---LAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQV 300
Cdd:cd18540  211 --TEEMRRASVRaarLSALFLPIVLFLGSIATalvLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARV 281

cbiO

PRK13644

energy-coupling factor transporter ATPase;

338-560

8.44e-22

energy-coupling factor transporter ATPase;

Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.44 E-value: 8.44e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGN-KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING-DPVSNSAL--LRPYIGF 413
Cdd:PRK13644   2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKLqgIRKLVGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTP-TLFEKCTLLENITLGRSisKASLENIFERTNLDVLLRrfENGLDTLV--ADIQLSGGERQLVALARALVSNPRL 490
Cdd:PRK13644  82 VFQNPeTQFVGRTVEEDLAFGPE--NLCLPPIEIRKRVDRALA--EIGLEKYRhrSPKTLSGGQGQCVALAGILTMEPEC 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 491 LILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSS 560
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227

PRK11000

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

337-502

1.86e-21

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 96.25 E-value: 1.86e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLRPYIGFVEQ 416
Cdd:PRK11000   3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 TPTLFEKCTLLENITLGRSISKASLENIFERTN-------LDVLLRRFENGldtlvadiqLSGGERQLVALARALVSNPR 489
Cdd:PRK11000  83 SYALYPHLSVAENMSFGLKLAGAKKEEINQRVNqvaevlqLAHLLDRKPKA---------LSGGQRQRVAIGRTLVAEPS 153

                        170
                 ....*....|...
gi 493533268 490 LLILDEITANIDS 502
Cdd:PRK11000 154 VFLLDEPLSNLDA 166

PRK13539

cytochrome c biogenesis protein CcmA; Provisional

348-527

2.00e-21

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.63 E-value: 2.00e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 348 GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV--SNSALLRPYIG---FVeqTPTLfe 422
Cdd:PRK13539  13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIddPDVAEACHYLGhrnAM--KPAL-- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 423 kcTLLENITLGRsiskasleNIFERTNLDVL--LRRFenGLDtLVADIQ---LSGGERQLVALARALVSNPRLLILDEIT 497
Cdd:PRK13539  89 --TVAENLEFWA--------AFLGGEELDIAaaLEAV--GLA-PLAHLPfgyLSAGQKRRVALARLLVSNRPIWILDEPT 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 493533268 498 ANIDSKTEEIIQNTLLGLRSEGIIVLMVAH 527
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGGIVIAATH 185

PRK03695

vitamin B12-transporter ATPase; Provisional

356-557

2.34e-21

vitamin B12-transporter ATPase; Provisional

Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 93.46 E-value: 2.34e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 356 LSLELRKGEITTLVGESGAGKTTTLNILMGLQkPQSGTIYINGDPVSNS-----ALLRPYigFVEQTPTLF--------- 421
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWsaaelARHRAY--LSQQQTPPFampvfqylt 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 422 ----EKCTLlenitlgrSISKASLENIFERTNLDVLLRRFENgldtlvadiQLSGGERQLVALARAL-----VSNP--RL 490
Cdd:PRK03695  92 lhqpDKTRT--------EAVASALNEVAEALGLDDKLGRSVN---------QLSGGEWQRVRLAAVVlqvwpDINPagQL 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 491 LILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLL-SDRVALISNGVIVASGTHNELLK 557
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRhADRVWLLKQGKLLASGRRDEVLT 222

cbiO

PRK13647

cobalt transporter ATP-binding subunit; Provisional

338-556

2.83e-21

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.03 E-value: 2.83e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGY--GNKQiLKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIGF 413
Cdd:PRK13647   5 IEVEDLHFRYkdGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaeNEKWVRSKVGL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTP--TLFEKcTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTlvADIQLSGGERQLVALARALVSNPRLL 491
Cdd:PRK13647  84 VFQDPddQVFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDK--PPYHLSYGQKKRVAIAGVLAMDPDVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 492 ILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGThNELL 556
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAeWADQVIVLKEGRVLAEGD-KSLL 225

ABC_6TM_Rv0194_D2_like

cd18546

Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...

24-300

2.84e-21

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: 94.09 E-value: 2.84e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDllvkYVLLVVGLWFGSLIFTYFGEVVFetTALMAKS------DLR 97
Cdd:cd18546    2 ALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLG----VLLLAAAAYLAVVLAGWVAQRAQ--TRLTGRTgerllyDLR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  98 KQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLV 177
Cdd:cd18546   76 LRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 178 IMFFNIMVEKRSKVEREkfgELAGVTSNIIDNMKLIRIAMPF---AWVMNFFDRFQGDHIYAGKRFIKSIKIAGTLKTSI 254
Cdd:cd18546  156 TRWFRRRSSRAYRRARE---RIAAVNADLQETLAGIRVVQAFrreRRNAERFAELSDDYRDARLRAQRLVAIYFPGVELL 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 493533268 255 NGLISFSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQV 300
Cdd:cd18546  233 GNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQV 278

PRK10535

macrolide ABC transporter ATP-binding protein/permease MacB;

340-554

3.08e-21

macrolide ABC transporter ATP-binding protein/permease MacB;

Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.87 E-value: 3.08e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 340 LENIAFGY--GNKQI--LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN------SALLRP 409
Cdd:PRK10535   7 LKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadalAQLRRE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 410 YIGFVEQTPTLFEKCTLLENITLGRSISKASLENIFERTNldVLLRRFENGLDTLVADIQLSGGERQLVALARALVSNPR 489
Cdd:PRK10535  87 HFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQ--ELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 490 LLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRVALISNGVIVA-SGTHNE 554
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRnPPAQEK 230

ABC_6TM_TAP

cd18572

Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...

24-315

3.52e-21

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: 93.76 E-value: 3.52e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIalavvfPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLEK 103
Cdd:cd18572    5 LVVAALSELAI------PHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 104 MFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIMFFNI 183
Cdd:cd18572   79 LLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 184 MVEKRSKVEREKFGELAGVTSNIIDNMKLIRIampFAWVMNFFDRFqGDHIYAGKRFIKSIKIAGTLKTSING----LIS 259
Cdd:cd18572  159 YYRKLSKEIQDALAEANQVAEEALSNIRTVRS---FATEEREARRY-ERALDKALKLSVRQALAYAGYVAVNTllqnGTQ 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 260 FSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVnillrqsWGGLLRTI 315
Cdd:cd18572  235 VLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDV-------FSSLMQAV 283

BtuD

COG4138

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

353-556

6.31e-21

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

Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 92.21 E-value: 6.31e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQkPQSGTIYINGDPVSNS-----ALLRPYigFVEQTPTLFEkCTLL 427
Cdd:COG4138   12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWsaaelARHRAY--LSQQQSPPFA-MPVF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 428 ENITLGRSiSKASLENIFERtnLDVLLRRFenGLDTLVA-DI-QLSGGERQLVALARALV-----SNP--RLLILDEITA 498
Cdd:COG4138   88 QYLALHQP-AGASSEAVEQL--LAQLAEAL--GLEDKLSrPLtQLSGGEWQRVRLAAVLLqvwptINPegQLLLLDEPMN 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493533268 499 NIDskteeIIQ----NTLLG-LRSEGIIVLMVAHRLS-TVLLSDRVALISNGVIVASGTHNELL 556
Cdd:COG4138  163 SLD-----VAQqaalDRLLReLCQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221

PvdE

COG4615

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...

10-527

7.70e-21

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: 96.02 E-value: 7.70e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  10 RFVFKLFKVYWkRELLAAVLVGVMIALAVVfpLLIRLLIDVVIPSGDMDLLVKYvllvvglWFGSLIFTYF-GEVVFE-- 86
Cdd:COG4615    2 NLLRLLLRESR-WLLLLALLLGLLSGLANA--GLIALINQALNATGAALARLLL-------LFAGLLVLLLlSRLASQll 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  87 TTALM--AKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVgTVIAQVFPILLLGVVQITAILAIMFAFNWKLT 164
Cdd:COG4615   72 LTRLGqhAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAYLAWLSPPLF 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 165 LLPLGFIVFSFLVIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRiampfawvMN------FFDR-FQG------ 231
Cdd:COG4615  151 LLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELK--------LNrrrrraFFDEdLQPtaeryr 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 232 DHIYAGKRFIKSIKIAGTlkTSINGLISFSLLAYGGYLVMKGEITVGILMTF---WAYVQSLFNPIQLLMQVNILLRQsw 308
Cdd:COG4615  223 DLRIRADTIFALANNWGN--LLFFALIGLILFLLPALGWADPAVLSGFVLVLlflRGPLSQLVGALPTLSRANVALRK-- 298

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 309 gglLRTIEVLEAPEEERSNSSPKLEDVR---SISLENIAFGYGNKQILKG-----LSLELRKGEITTLVGESGAGKTTTL 380
Cdd:COG4615  299 ---IEELELALAAAEPAAADAAAPPAPAdfqTLELRGVTYRYPGEDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLA 375

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 381 NILMGLQKPQSGTIYINGDPVS--NSALLRPYIGFVEQTPTLFEKctlleniTLGrsiskasLENIFERTNLDVLLRRFE 458
Cdd:COG4615  376 KLLTGLYRPESGEILLDGQPVTadNREAYRQLFSAVFSDFHLFDR-------LLG-------LDGEADPARARELLERLE 441

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268 459 ngLDTLVA-------DIQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLG-LRSEGIIVLMVAH 527
Cdd:COG4615  442 --LDHKVSvedgrfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYTELLPeLKARGKTVIAISH 516

3a01204

TIGR00955

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

350-557

7.92e-21

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

Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 96.27 E-value: 7.92e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  350 KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKP---QSGTIYINGDPVsNSALLRPYIGFVEQTPTLFEKCTL 426
Cdd:TIGR00955  38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI-DAKEMRAISAYVQQDDLFIPTLTV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  427 LENIT------LGRSISK----ASLENIFERTNLdvllrrfENGLDTLVADIQ----LSGGERQLVALARALVSNPRLLI 492
Cdd:TIGR00955 117 REHLMfqahlrMPRRVTKkekrERVDEVLQALGL-------RKCANTRIGVPGrvkgLSGGERKRLAFASELLTDPPLLF 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268  493 LDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL--LSDRVALISNGVIVASGTHNELLK 557
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELfeLFDKIILMAEGRVAYLGSPDQAVP 256

ABC_CcmA_heme_exporter

cd03231

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...

341-527

1.11e-20

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: 90.24 E-value: 1.11e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 341 ENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS------NSALLrpYIGfv 414
Cdd:cd03231    4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDfqrdsiARGLL--YLG-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 eQTPTLFEKCTLLENITLGRSISkaSLENIFERTNlDVLLRRFEnglDTLVAdiQLSGGERQLVALARALVSNPRLLILD 494
Cdd:cd03231   80 -HAPGIKTTLSVLENLRFWHADH--SDEQVEEALA-RVGLNGFE---DRPVA--QLSAGQQRRVALARLLLSGRPLWILD 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 493533268 495 EITANIDSKTEEIIQNTLLGLRSEGIIVLMVAH 527
Cdd:cd03231  151 EPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183

modC

PRK11144

molybdenum ABC transporter ATP-binding protein ModC;

365-550

1.62e-20

molybdenum ABC transporter ATP-binding protein ModC;

Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 93.02 E-value: 1.62e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 365 ITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL---LRPY---IGFVEQTPTLFEKCTLLENITLG-RSIS 437
Cdd:PRK11144  26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgicLPPEkrrIGYVFQDARLFPHYKVRGNLRYGmAKSM 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 438 KASLENIFERTNLDVLLRRFEngldtlvadIQLSGGERQLVALARALVSNPRLLILDEITANID--SKTEeiIQNTLLGL 515
Cdd:PRK11144 106 VAQFDKIVALLGIEPLLDRYP---------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlpRKRE--LLPYLERL 174

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 493533268 516 RSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASG 550
Cdd:PRK11144 175 AREiNIPILYVSHSLDEILrLADRVVVLEQGKVKAFG 211

cbiO

PRK13648

cobalt transporter ATP-binding subunit; Provisional

338-561

1.89e-20

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 91.35 E-value: 1.89e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQ--ILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGF 413
Cdd:PRK13648   8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFekLRKHIGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTP-TLFEKCTLLENITLGRSISKASLENIFER-----TNLDVLLRrfengldtlvADIQ---LSGGERQLVALARAL 484
Cdd:PRK13648  88 VFQNPdNQFVGSIVKYDVAFGLENHAVPYDEMHRRvsealKQVDMLER----------ADYEpnaLSGGQKQRVAIAGVL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 485 VSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSE 561
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

317-548

4.00e-20

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.55 E-value: 4.00e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 317 VLEAPEEERSNSSPKLEdVRSISLENiafgYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYI 396
Cdd:COG3845  243 LLRVEKAPAEPGEVVLE-VENLSVRD----DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 397 NGDPVSN---SALLRPYIGFVeqtPT------LFEKCTLLENITLGRSISKASLENIFE-----RTNLDVLLRRFE---N 459
Cdd:COG3845  318 DGEDITGlspRERRRLGVAYI---PEdrlgrgLVPDMSVAENLILGRYRRPPFSRGGFLdrkaiRAFAEELIEEFDvrtP 394

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 460 GLDTLVAdiQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRV 538
Cdd:COG3845  395 GPDTPAR--SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILaLSDRI 472

                        250
                 ....*....|
gi 493533268 539 ALISNGVIVA 548
Cdd:COG3845  473 AVMYEGRIVG 482

ABC_6TM_PrtD_LapB_HlyB_like

cd18782

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...

21-283

4.73e-20

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: 90.73 E-value: 4.73e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  21 KRELLAAVLVGVMIA-LAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQ 99
Cdd:cd18782    1 RRALIEVLALSFVVQlLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 100 LLEKMFVLPFDFFHKNKTGELVSRlISDLE-----LVGTVIAqvfpiLLLGVVQITAILAIMFAFNWKLTLLPLGFIVFS 174
Cdd:cd18782   81 IIDHLLRLPLGFFDKRPVGELSTR-ISELDtirgfLTGTALT-----TLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 175 FLVIMFFNIMVEKRSkveREKFGELAGVTSNIIDNMKLIR------IAMPFAWVMNffDRFqGDHIYAGKRFIKSIKIAG 248
Cdd:cd18782  155 LLLTFLFGPILRRQI---RRRAEASAKTQSYLVESLTGIQtvkaqnAELKARWRWQ--NRY-ARSLGEGFKLTVLGTTSG 228

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 493533268 249 TLKTSINGLISFSLLAYGGYLVMKGEITVGILMTF 283
Cdd:cd18782  229 SLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAF 263

ABCC_SUR2

cd03288

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...

338-556

6.58e-20

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: 89.58 E-value: 6.58e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGN--KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGF 413
Cdd:cd03288   20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLhtLRSRLSI 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPTLFEKcTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPRLL 491
Cdd:cd03288  100 ILQDPILFSG-SIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEggENFSVGQRQLFCLARAFVRKSSIL 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 492 ILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMvAHRLSTVLLSDRVALISNGVIVASGTHNELL 556
Cdd:cd03288  179 IMDEATASIDMATENILQKVVMTAFADRTVVTI-AHRVSTILDADLVLVLSRGILVECDTPENLL 242

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

353-556

6.77e-20

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: 93.21 E-value: 6.77e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQkPQSGTIYINGDPVS--NSALLRPY---IGFVEQTP--TLFEKCT 425
Cdd:COG4172  302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDglSRRALRPLrrrMQVVFQDPfgSLSPRMT 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 426 LLENIT-----LGRSISKASLEN----IFERTNLD-VLLRRFENgldtlvadiQLSGGERQLVALARALVSNPRLLILDE 495
Cdd:COG4172  381 VGQIIAeglrvHGPGLSAAERRArvaeALEEVGLDpAARHRYPH---------EFSGGQRQRIAIARALILEPKLLVLDE 451

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 496 ITANID-SkteeiIQNTLLGL-----RSEGIIVLMVAHRLSTV-LLSDRVALISNGVIVASGTHNELL 556
Cdd:COG4172  452 PTSALDvS-----VQAQILDLlrdlqREHGLAYLFISHDLAVVrALAHRVMVMKDGKVVEQGPTEQVF 514

livG

PRK11300

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

355-555

8.05e-20

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

Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 89.28 E-value: 8.05e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 355 GLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDP--------VSNSALLRPYigfveQTPTLFEKCTL 426
Cdd:PRK11300  23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpghqIARMGVVRTF-----QHVRLFREMTV 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 427 LENITLG--RSISKASLENIF--------ERTNLD---VLLRRFenGLdTLVADIQ---LSGGERQLVALARALVSNPRL 490
Cdd:PRK11300  98 IENLLVAqhQQLKTGLFSGLLktpafrraESEALDraaTWLERV--GL-LEHANRQagnLAYGQQRRLEIARCMVTQPEI 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268 491 LILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNEL 555
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMgISDRIYVVNQGTPLANGTPEEI 241

phnK

PRK11701

phosphonate C-P lyase system protein PhnK; Provisional

339-550

1.08e-19

phosphonate C-P lyase system protein PhnK; Provisional

Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 88.83 E-value: 1.08e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 339 SLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTI-YINGDPVSNS----------ALL 407
Cdd:PRK11701   8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDlyalseaerrRLL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 408 RPYIGFVEQTPTlfekctllenITLGRSISKASleNIFER--------------TNLDvLLRRFE---NGLDTLVAdiQL 470
Cdd:PRK11701  88 RTEWGFVHQHPR----------DGLRMQVSAGG--NIGERlmavgarhygdiraTAGD-WLERVEidaARIDDLPT--TF 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 471 SGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTV-LLSDRVALISNGVIVA 548
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVArLLAHRLLVMKQGRVVE 232


                 ..
gi 493533268 549 SG 550
Cdd:PRK11701 233 SG 234

PRK10619

histidine ABC transporter ATP-binding protein HisP;

347-556

1.18e-19

histidine ABC transporter ATP-binding protein HisP;

Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.87 E-value: 1.18e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 347 YGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS---------------NSALLRPYI 411
Cdd:PRK10619  15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadknQLRLLRTRL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 412 GFVEQTPTLFEKCTLLENI------TLGRSISKASLENIFERTNLdvllrrfenGLDTLVAD---IQLSGGERQLVALAR 482
Cdd:PRK10619  95 TMVFQHFNLWSHMTVLENVmeapiqVLGLSKQEARERAVKYLAKV---------GIDERAQGkypVHLSGGQQQRVSIAR 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 483 ALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELL 556
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEGAPEQLF 240

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

338-564

1.54e-19

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 91.79 E-value: 1.54e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQ--KPQSGTI-----------YIN-----GD 399
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgYVErpskvGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  400 --PVSNSALLRPYIGFVEQTPTLFEKCTLLENITLGRSIS----KASLENIFERTN-------------LDVL-LRRFEN 459
Cdd:TIGR03269  81 pcPVCGGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFAlygdDTVLDNVLEALEeigyegkeavgraVDLIeMVQLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  460 GLDTLVADiqLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLL-GLRSEGIIVLMVAHrLSTVL--LSD 536
Cdd:TIGR03269 161 RITHIARD--LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeAVKASGISMVLTSH-WPEVIedLSD 237

                         250       260       270
                  ....*....|....*....|....*....|..
gi 493533268  537 RVALISNGVIVASGTHNEL----LKTSSEYKK 564
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVvavfMEGVSEVEK 269

cbiO

PRK13643

energy-coupling factor transporter ATPase;

356-557

1.67e-19

energy-coupling factor transporter ATPase;

Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.02 E-value: 1.67e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 356 LSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYInGDPVSNSAL-------LRPYIGFVEQTP--TLFEKcTL 426
Cdd:PRK13643  25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSkqkeikpVRKKVGVVFQFPesQLFEE-TV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 427 LENITLGRS---ISKASLENI-FERTNLDVLLRRFENGldtlvADIQLSGGERQLVALARALVSNPRLLILDEITANIDS 502
Cdd:PRK13643 103 LKDVAFGPQnfgIPKEKAEKIaAEKLEMVGLADEFWEK-----SPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 503 KTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLK 557
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDVFQ 233

PRK14267

phosphate ABC transporter ATP-binding protein; Provisional

337-550

2.41e-19

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.98 E-value: 2.41e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTT---TLNILMGLQKPQ--SGTIYINGDPVSNSAL----L 407
Cdd:PRK14267   4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTllrTFNRLLELNEEArvEGEVRLFGRNIYSPDVdpieV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 408 RPYIGFVEQTPTLFEKCTLLENITLGRSISK--ASLENIFERTNLDV----LLRRFENGLDTLVAdiQLSGGERQLVALA 481
Cdd:PRK14267  84 RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALkkaaLWDEVKDRLNDYPS--NLSGGQRQRLVIA 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493533268 482 RALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRVALISNGVIVASG 550
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230

ABC_FeS_Assembly

cd03217

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...

348-550

2.76e-19

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

Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 86.04 E-value: 2.76e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 348 GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQ--KPQSGTIYINGD-----PVSNSALLRPYIGFveQTPTL 420
Cdd:cd03217   11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEditdlPPEERARLGIFLAF--QYPPE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 421 FEKCTLLEnitlgrsiskaslenifertnldvLLRRFENGLdtlvadiqlSGGERQLVALARALVSNPRLLILDEITANI 500
Cdd:cd03217   89 IPGVKNAD------------------------FLRYVNEGF---------SGGEKKRNEILQLLLLEPDLAILDEPDSGL 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493533268 501 DSKTEEIIQNTLLGLRSEGIIVLMVAH--RLSTVLLSDRVALISNGVIVASG 550
Cdd:cd03217  136 DIDALRLVAEVINKLREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187

ABCF_EF-3

cd03221

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...

338-527

2.83e-19

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: 84.42 E-value: 2.83e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGdpvsnsallRPYIGFVEqt 417
Cdd:cd03221    1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------TVKIGYFE-- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 ptlfekctllenitlgrsiskaslenifertnldvllrrfengldtlvadiQLSGGERQLVALARALVSNPRLLILDEIT 497
Cdd:cd03221   70 ---------------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPT 98

                        170       180       190
                 ....*....|....*....|....*....|
gi 493533268 498 ANIDSKTEEIIQNTLLGLRSegiIVLMVAH 527
Cdd:cd03221   99 NHLDLESIEALEEALKEYPG---TVILVSH 125

PRK10070

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

336-556

4.48e-19

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

Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 89.71 E-value: 4.48e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 336 RSISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING---DPVSNSALL---RP 409
Cdd:PRK10070  27 QGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELRevrRK 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 410 YIGFVEQTPTLFEKCTLLENITLGRSISKASLENIFERTnLDVL----LRRFENGLDTlvadiQLSGGERQLVALARALV 485
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKA-LDALrqvgLENYAHSYPD-----ELSGGMRQRVGLARALA 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493533268 486 SNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELL 556
Cdd:PRK10070 181 INPDILLMDEAFSALDPLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMrIGDRIAIMQNGEVVQVGTPDEIL 253

cbiO

PRK13642

energy-coupling factor transporter ATPase;

338-573

4.89e-19

energy-coupling factor transporter ATPase;

Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.46 E-value: 4.89e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGY---GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIG 412
Cdd:PRK13642   5 LEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTP-TLFEKCTLLENITLGRSISKASLENIFERTNLDVLLrrfENGLDTLVAD-IQLSGGERQLVALARALVSNPRL 490
Cdd:PRK13642  85 MVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLA---VNMLDFKTREpARLSGGQKQRVAVAGIIALRPEI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 491 LILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYKKL---- 565
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEIgldv 241


                 ....*....
gi 493533268 566 -YSLQLIKD 573
Cdd:PRK13642 242 pFSSNLMKD 250

ABC_KpsT_Wzt

cd03220

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...

344-550

6.78e-19

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: 85.66 E-value: 6.78e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 344 AFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPvsnSALLRPYIGFVeqtPTLfek 423
Cdd:cd03220   29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV---SSLLGLGGGFN---PEL--- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 424 cTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTLVAdiQLSGGERQLVALARALVSNPRLLILDEITANIDSK 503
Cdd:cd03220  100 -TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVK--TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 493533268 504 TEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASG 550
Cdd:cd03220  177 FQEKCQRRLRELLKQGKTVILVSHDPSSIKrLCDRALVLEKGKIRFDG 224

PRK13538

cytochrome c biogenesis heme-transporting ATPase CcmA;

338-527

7.75e-19

cytochrome c biogenesis heme-transporting ATPase CcmA;

Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.86 E-value: 7.75e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS------NSALLrpYI 411
Cdd:PRK13538   2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdeyHQDLL--YL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 412 GFV-----EQTPtlfekctlLENIT----LGRSISKASLENIFERTNldvlLRRFEnglDTLVAdiQLSGGERQLVALAR 482
Cdd:PRK13538  80 GHQpgiktELTA--------LENLRfyqrLHGPGDDEALWEALAQVG----LAGFE---DVPVR--QLSAGQQRRVALAR 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 493533268 483 ALVSNPRLLILDE-ITAnIDSKTEEIIQNTLLGLRSEGIIVLMVAH 527
Cdd:PRK13538 143 LWLTRAPLWILDEpFTA-IDKQGVARLEALLAQHAEQGGMVILTTH 187

PRK14258

phosphate ABC transporter ATP-binding protein; Provisional

335-558

8.21e-19

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 86.63 E-value: 8.21e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 335 VRSISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQS-----GTIYINGDPV----SNSA 405
Cdd:PRK14258   5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNLN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 406 LLRPYIGFVEQTPTLFeKCTLLENITLGRSI----SKASLENIFERTNLDV-LLRRFENGLDTlvADIQLSGGERQLVAL 480
Cdd:PRK14258  85 RLRRQVSMVHPKPNLF-PMSVYDNVAYGVKIvgwrPKLEIDDIVESALKDAdLWDEIKHKIHK--SALDLSGGQQQRLCI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 481 ARALVSNPRLLILDEITANIDS----KTEEIIQNtlLGLRSEGIIVLmVAHRLSTVL-LSDRVALISN-----GVIVASG 550
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPiasmKVESLIQS--LRLRSELTMVI-VSHNLHQVSrLSDFTAFFKGnenriGQLVEFG 238


                 ....*...
gi 493533268 551 THNELLKT 558
Cdd:PRK14258 239 LTKKIFNS 246

cbiO

PRK13641

energy-coupling factor transporter ATPase;

337-566

1.18e-18

energy-coupling factor transporter ATPase;

Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.42 E-value: 1.18e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYG-----NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV----SNSAL- 406
Cdd:PRK13641   2 SIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLk 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 407 -LRPYIGFVEQTP--TLFEKcTLLENITLGRSISKASLENIFERTNldVLLRRFenGLDTLVAD---IQLSGGERQLVAL 480
Cdd:PRK13641  82 kLRKKVSLVFQFPeaQLFEN-TVLKDVEFGPKNFGFSEDEAKEKAL--KWLKKV--GLSEDLISkspFELSGGQMRRVAI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 481 ARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLKTS 559
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAeYADDVLVLEHGKLIKHASPKEIFSDK 236


                 ....*..
gi 493533268 560 SEYKKLY 566
Cdd:PRK13641 237 EWLKKHY 243

ABC_6TM_ABCB10_like

cd18573

Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...

25-283

1.21e-18

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: 86.41 E-value: 1.21e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  25 LAAVLVGVMIALAvvFPLLIRLLIDVvIPSGDMDLLVKYVLLVVGLWFGSLIFT-----YFGEVVFETTA---LMAKsdL 96
Cdd:cd18573    2 LALLLVSSAVTMS--VPFAIGKLIDV-ASKESGDIEIFGLSLKTFALALLGVFVvgaaaNFGRVYLLRIAgerIVAR--L 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  97 RKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFL 176
Cdd:cd18573   77 RKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 177 VIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRIampFAWVMNFFDRF--QGDHIYA-GKR--FIKSIkIAGTLK 251
Cdd:cd18573  157 GAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRA---FAAERKEVERYakKVDEVFDlAKKeaLASGL-FFGSTG 232

                        250       260       270
                 ....*....|....*....|....*....|..
gi 493533268 252 TSINGLISfSLLAYGGYLVMKGEITVGILMTF 283
Cdd:cd18573  233 FSGNLSLL-SVLYYGGSLVASGELTVGDLTSF 263

ABCG_PDR_domain2

cd03232

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...

348-544

1.54e-18

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: 83.83 E-value: 1.54e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 348 GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGlQKPQ---SGTIYINGDPVSNSalLRPYIGFVEQTPTLFEKC 424
Cdd:cd03232   18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG-RKTAgviTGEILINGRPLDKN--FQRSTGYVEQQDVHSPNL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 425 TLLEnitlgrsiskaSLEnifertnLDVLLRrfengldtlvadiQLSGGERQLVALARALVSNPRLLILDEITANIDSKT 504
Cdd:cd03232   95 TVRE-----------ALR-------FSALLR-------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 493533268 505 EEIIQNTLLGLRSEGIIVLMVAHRLSTVLLS--DRVALISNG 544
Cdd:cd03232  144 AYNIVRFLKKLADSGQAILCTIHQPSASIFEkfDRLLLLKRG 185

PRK14271

phosphate ABC transporter ATP-binding protein; Provisional

342-558

2.77e-18

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.15 E-value: 2.77e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 342 NIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIY-----INGDPVSNSA---LLRPYIGF 413
Cdd:PRK14271  26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIFNYRdvlEFRRRVGM 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPTLFeKCTLLENITLGRSISKASLENIFERTnldVLLRRFENGLDTLVAD------IQLSGGERQLVALARALVSN 487
Cdd:PRK14271 106 LFQRPNPF-PMSIMDNVLAGVRAHKLVPRKEFRGV---AQARLTEVGLWDAVKDrlsdspFRLSGGQQQLLCLARTLAVN 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268 488 PRLLILDEITANIDSKTEEIIQNTLLGLrSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLKT 558
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAArISDRAALFFDGRLVEEGPTEQLFSS 252

cbiO

PRK13638

energy-coupling factor ABC transporter ATP-binding protein;

338-556

3.21e-18

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.06 E-value: 3.21e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAllRPYIGFVEQT 417
Cdd:PRK13638   2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK--RGLLALRQQV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PTLFEKCTllenitlgRSISKASLEN--IFERTNLDV----LLRRFENGLdTLVaDIQ---------LSGGERQLVALAR 482
Cdd:PRK13638  80 ATVFQDPE--------QQIFYTDIDSdiAFSLRNLGVpeaeITRRVDEAL-TLV-DAQhfrhqpiqcLSHGQKKRVAIAG 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 483 ALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELL 556
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYeISDAVYVLRQGQILTHGAPGEVF 224

cbiO

PRK13631

cobalt transporter ATP-binding subunit; Provisional

332-573

4.67e-18

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.29 E-value: 4.67e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 332 LEDVRSISLENIAFGYGNKQ-----ILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTI-----YINGDP- 400
Cdd:PRK13631  16 LSDDIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiYIGDKKn 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 401 ------------VSNSALLRPYIGFVEQTP--TLF----EKCTLLENITLGRSISKASLENIF--ERTNLDvllrrfENG 460
Cdd:PRK13631  96 nhelitnpyskkIKNFKELRRRVSMVFQFPeyQLFkdtiEKDIMFGPVALGVKKSEAKKLAKFylNKMGLD------DSY 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 461 LDtlVADIQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVA 539
Cdd:PRK13631 170 LE--RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLeVADEVI 247

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 493533268 540 LISNGVIVASGT-----HNELLKTSSEYKKLYSLQLIKD 573
Cdd:PRK13631 248 VMDKGKILKTGTpyeifTDQHIINSTSIQVPRVIQVIND 286

PRK10261

glutathione transporter ATP-binding protein; Provisional

356-550

8.45e-18

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.83 E-value: 8.45e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 356 LSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING---DPVSNSAL--LRPYIGFVEQTPTlfekCTLLENI 430
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqriDTLSPGKLqaLRRDIQFIFQDPY----ASLDPRQ 418

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 431 TLGRSISK-----ASLENIFERTNLDVLLRRFenGLDTLVA---DIQLSGGERQLVALARALVSNPRLLILDEITANIDS 502
Cdd:PRK10261 419 TVGDSIMEplrvhGLLPGKAAAARVAWLLERV--GLLPEHAwryPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 493533268 503 KTEEIIQNTLLGLRSE-GIIVLMVAHRLSTV-LLSDRVALISNGVIVASG 550
Cdd:PRK10261 497 SIRGQIINLLLDLQRDfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546

ABC_6TM_bac_exporter_ABCB8_10_like

cd18575

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...

94-283

8.67e-18

Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 84.07 E-value: 8.67e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  94 SDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVF 173
Cdd:cd18575   69 ADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 174 SFLVIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRIAMPFAWVMNFFDRFQGDHIYAGKRfikSIKIAGTLKTS 253
Cdd:cd18575  149 VVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALR---RIRARALLTAL 225

                        170       180       190
                 ....*....|....*....|....*....|...
gi 493533268 254 INGLISFSL---LAYGGYLVMKGEITVGILMTF 283
Cdd:cd18575  226 VIFLVFGAIvfvLWLGAHDVLAGRMSAGELSQF 258

nikD

PRK10418

nickel transporter ATP-binding protein NikD; Provisional

336-558

1.26e-17

nickel transporter ATP-binding protein NikD; Provisional

Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.83 E-value: 1.26e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 336 RSISLENIAFgYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKP----QSGTIYINGDPVSNSALLRPYI 411
Cdd:PRK10418   3 QQIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 412 GFVEQTP-TLFE---------KCTLLeniTLGRSISKASLENIFERTNLD---VLLRRFEngldtlvadIQLSGGERQLV 478
Cdd:PRK10418  82 ATIMQNPrSAFNplhtmhthaRETCL---ALGKPADDATLTAALEAVGLEnaaRVLKLYP---------FEMSGGMLQRM 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 479 ALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELL 556
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVArLADDVAVMSHGRIVEQGDVETLF 229


                 ..
gi 493533268 557 KT 558
Cdd:PRK10418 230 NA 231

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

356-555

1.50e-17

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 85.65 E-value: 1.50e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  356 LSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQ-SGTIYINGDPVSNSALLRPYIGFVEQTPTLFEKCTLLENITLGR 434
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGK 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  435 SISKASLENIFERTNLDVllrrfENGLDTLVADIQ---------------LSGGERQLVALARALVSNPRLLILDEITAN 499
Cdd:TIGR02633 359 NITLSVLKSFCFKMRIDA-----AAELQIIGSAIQrlkvktaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268  500 IDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNEL 555
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLgLSDRVLVIGEGKLKGDFVNHAL 490

ABC_6TM_T1SS_like

cd18555

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...

21-299

2.11e-17

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

Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 82.94 E-value: 2.11e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  21 KRELLAAVLVGVMI-ALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYF-GEVVFETTALMAKSdLRK 98
Cdd:cd18555    1 KKLLISILLLSLLLqLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLrGYIIIKLQTKLDKS-LMS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  99 QLLEKMFVLPFDFFHKNKTGELVSRL-----ISDLeLVGTVIAQVFPILLLGVvqitaILAIMFAFNWKLTLLPLGFIVF 173
Cdd:cd18555   80 DFFEHLLKLPYSFFENRSSGDLLFRAnsnvyIRQI-LSNQVISLIIDLLLLVI-----YLIYMLYYSPLLTLIVLLLGLL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 174 SFLVIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRIAMPFAWVMNFFDRFQGDHIYAGKRFIKSIKIAGTLKTS 253
Cdd:cd18555  154 IVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSS 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 493533268 254 INGLISFSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQ 299
Cdd:cd18555  234 IQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLIN 279

ugpC

PRK11650

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

337-503

2.33e-17

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

Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.74 E-value: 2.33e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGNK-QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNsalLRPY---IG 412
Cdd:PRK11650   3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE---LEPAdrdIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 413 FVEQTPTLFEKCTLLENITLGRSISKASLENIFERT-------NLDVLLRRFENgldtlvadiQLSGGERQLVALARALV 485
Cdd:PRK11650  80 MVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVaeaarilELEPLLDRKPR---------ELSGGQRQRVAMGRAIV 150

                        170
                 ....*....|....*...
gi 493533268 486 SNPRLLILDEITANIDSK 503
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAK 168

SufC

COG0396

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...

339-557

2.88e-17

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

Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 81.65 E-value: 2.88e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 339 SLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGL--QKPQSGTIYINGDPVSNsalLRPY------ 410
Cdd:COG0396    2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILE---LSPDerarag 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 411 IGFVEQTPTLFEKCTlleNITLGRSISKAslenifeRTNLDVLLRRFENGLDTLVADIQL-------------SGGERQL 477
Cdd:COG0396   79 IFLAFQYPVEIPGVS---VSNFLRTALNA-------RRGEELSAREFLKLLKEKMKELGLdedfldryvnegfSGGEKKR 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 478 VALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAH--RLSTVLLSDRVALISNGVIVASGTHnEL 555
Cdd:COG0396  149 NEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGK-EL 227


                 ..
gi 493533268 556 LK 557
Cdd:COG0396  228 AL 229

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

348-535

2.94e-17

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.76 E-value: 2.94e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 348 GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQsGTIYINGDPVSN---SALL--RPYIGFVEQTP--TL 420
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNlnrRQLLpvRHRIQVVFQDPnsSL 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 421 FEKCTLLENITLGRSISKASLeNIFERTNlDVLLRRFENGLDTLVAD---IQLSGGERQLVALARALVSNPRLLILDEIT 497
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVHQPTL-SAAQREQ-QVIAVMEEVGLDPETRHrypAEFSGGQRQRIAIARALILKPSLIILDEPT 453

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 493533268 498 ANIDSKTEEIIQNTLLGLRSEgiivlmvaHRLSTVLLS 535
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQK--------HQLAYLFIS 483

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

152-556

3.06e-17

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 85.77 E-value: 3.06e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   152 ILAIMFAfnWkLTLLP--LGFIVFSFLVIMFFNIMVEK---------RSKVEREKfgelagVTSNIIDNMKLIRIampFA 220
Cdd:TIGR00957  446 ILALYFL--W-LNLGPsvLAGVAVMVLMVPLNAVMAMKtktyqvahmKSKDNRIK------LMNEILNGIKVLKL---YA 513

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   221 WVMNFFDRFQGdhIYAGKrfIKSIKIAGTLKTsingLISFSLLAyGGYLVMkgeitvgiLMTFWAYVQ------------ 288
Cdd:TIGR00957  514 WELAFLDKVEG--IRQEE--LKVLKKSAYLHA----VGTFTWVC-TPFLVA--------LITFAVYVTvdennildaeka 576

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   289 ----SLFN----PIQLLMQVNILLRQSWGGLLR-----TIEVLEAPEEERSNSSPKleDVRSISLENIAFGY--GNKQIL 353
Cdd:TIGR00957  577 fvslALFNilrfPLNILPMVISSIVQASVSLKRlriflSHEELEPDSIERRTIKPG--EGNSITVHNATFTWarDLPPTL 654

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   354 KGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDpvsnsallrpyIGFVEQTPTLfEKCTLLENITLG 433
Cdd:TIGR00957  655 NGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------VAYVPQQAWI-QNDSLRENILFG 722

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   434 RSISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNT 511
Cdd:TIGR00957  723 KALNEKYYQQVLEACALLPDLEILPSGDRTEIGEkgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 493533268   512 LLGlrSEGIIV----LMVAHRLSTVLLSDRVALISNGVIVASGTHNELL 556
Cdd:TIGR00957  803 VIG--PEGVLKnktrILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 849

ABC_6TM_Pgp_ABCB1_D2_like

cd18578

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...

72-292

3.62e-17

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: 82.50 E-value: 3.62e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  72 FGSLIFTYFGEVVFETTALMAKSDLRKQLLEKMFVLPFDFF--HKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQI 149
Cdd:cd18578   63 IVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTL 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 150 TAILAIMFAFNWKLTLLPLGFIVFSFLVIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRIampfawvMN----F 225
Cdd:cd18578  143 VAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVAS-------LTledyF 215

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493533268 226 FDRFQGDHIYAGKRFIKSIKIAGTLkTSINGLISFSLLA----YGGYLVMKGEITVG-ILMTFWAYVQSLFN 292
Cdd:cd18578  216 LEKYEEALEEPLKKGLRRALISGLG-FGLSQSLTFFAYAlafwYGGRLVANGEYTFEqFFIVFMALIFGAQS 286

PRK14246

phosphate ABC transporter ATP-binding protein; Provisional

333-558

3.76e-17

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.63 E-value: 3.76e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 333 EDVRSISleNIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--------NS 404
Cdd:PRK14246   8 EDVFNIS--RLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqiDA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 405 ALLRPYIGFVEQTPTLFEKCTLLENITLGRSI----SKASLENIFERTNLDV-LLRRFENGLDTLVAdiQLSGGERQLVA 479
Cdd:PRK14246  86 IKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKShgikEKREIKKIVEECLRKVgLWKEVYDRLNSPAS--QLSGGQQQRLT 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493533268 480 LARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKT 558
Cdd:PRK14246 164 IARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242

PRK13633

energy-coupling factor transporter ATPase;

338-565

4.75e-17

energy-coupling factor transporter ATPase;

Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 81.67 E-value: 4.75e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGN------KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALL---R 408
Cdd:PRK13633   5 IKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwdiR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 409 PYIGFVEQTP------TLFEKCTLL--ENITLGRSISKASLENIFERTNLdVLLRRFENGLdtlvadiqLSGGERQLVAL 480
Cdd:PRK13633  85 NKAGMVFQNPdnqivaTIVEEDVAFgpENLGIPPEEIRERVDESLKKVGM-YEYRRHAPHL--------LSGGQKQRVAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 481 ARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTS 559
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKEV 235


                 ....*.
gi 493533268 560 SEYKKL 565
Cdd:PRK13633 236 EMMKKI 241

GguA

NF040905

sugar ABC transporter ATP-binding protein;

353-544

5.38e-17

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.07 E-value: 5.38e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQkPQ---SGTIYINGDPVSNSALL---RPYIGFVEQTPTLFEKCTL 426
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRdseALGIVIIHQELALIPYLSI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 427 LENITLGRSISKASLENiFERTNL--DVLLRRFenGL----DTLVADIQLsgGERQLVALARALVSNPRLLILDEITANI 500
Cdd:NF040905  96 AENIFLGNERAKRGVID-WNETNRraRELLAKV--GLdespDTLVTDIGV--GKQQLVEIAKALSKDVKLLILDEPTAAL 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 493533268 501 DSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNG 544
Cdd:NF040905 171 NEEDSAALLDLLLELKAQGITSIIISHKLNEIRrVADSITVLRDG 215

TagH

COG1134

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...

346-551

6.57e-17

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

Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.51 E-value: 6.57e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 346 GYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGdpvSNSALLRPYIGFVeqtPTLfekcT 425
Cdd:COG1134   35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RVSALLELGAGFH---PEL----T 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 426 LLENITLGRSI---SKASLENIFErtnlDVL----LRRFengLDTLVAdiQLSGGERQLVALARALVSNPRLLILDEITA 498
Cdd:COG1134  105 GRENIYLNGRLlglSRKEIDEKFD----EIVefaeLGDF---IDQPVK--TYSSGMRARLAFAVATAVDPDILLVDEVLA 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 499 NIDS----KTEEIIQNtllgLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGT 551
Cdd:COG1134  176 VGDAafqkKCLARIRE----LRESGRTVIFVSHSMGAVRrLCDRAIWLEKGRLVMDGD 229

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

327-574

8.06e-17

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.60 E-value: 8.06e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 327 NSSPKLeDVRSISlenIAFGYGN--KQILKGLSLELRKGEITTLVGESGAGKT-TTLNILMGLQKPQ----SGTIYINGD 399
Cdd:PRK15134   1 MTQPLL-AIENLS---VAFRQQQtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 400 PV--SNSALLRPY----IGFVEQTPTL-------FEKcTLLENITLGRSISK--ASLENI--FERTNLDVLLRRfengld 462
Cdd:PRK15134  77 SLlhASEQTLRGVrgnkIAMIFQEPMVslnplhtLEK-QLYEVLSLHRGMRReaARGEILncLDRVGIRQAAKR------ 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 463 tlVADI--QLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRV 538
Cdd:PRK15134 150 --LTDYphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRkLADRV 227

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 493533268 539 ALISNGVIVASGTHNELLKTSSEykkLYSLQLIKDE 574
Cdd:PRK15134 228 AVMQNGRCVEQNRAATLFSAPTH---PYTQKLLNSE 260

PRK11831

phospholipid ABC transporter ATP-binding protein MlaF;

326-555

8.20e-17

phospholipid ABC transporter ATP-binding protein MlaF;

Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.58 E-value: 8.20e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 326 SNSSPKLEDVRSISleniaFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV---S 402
Cdd:PRK11831   1 EQSVANLVDMRGVS-----FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 403 NSAL--LRPYIGFVEQTPTLFEKCTLLENITLgrsiskasleNIFERTNL-DVLLR-----RFE----NGLDTLVADiQL 470
Cdd:PRK11831  76 RSRLytVRKRMSMLFQSGALFTDMNVFDNVAY----------PLREHTQLpAPLLHstvmmKLEavglRGAAKLMPS-EL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 471 SGGERQLVALARALVSNPRLLILDEITANIDSkteeIIQNTLLGLRSE-----GIIVLMVAHRLSTVL-LSDRVALISNG 544
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDEPFVGQDP----ITMGVLVKLISElnsalGVTCVVVSHDVPEVLsIADHAYIVADK 220

                        250
                 ....*....|.
gi 493533268 545 VIVASGTHNEL 555
Cdd:PRK11831 221 KIVAHGSAQAL 231

PhnL

COG4778

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...

348-538

9.29e-17

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: 79.79 E-value: 9.29e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 348 GNKQI--LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYIN----------GDPVSNSALLRPYIGFVE 415
Cdd:COG4778   20 GGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqASPREILALRRRTIGYVS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 416 Q-------TPTL---FEKctLLENiTLGRSISKASLENIFERTNLDVLLRRfengldtlVADIQLSGGERQLVALARALV 485
Cdd:COG4778  100 QflrviprVSALdvvAEP--LLER-GVDREEARARARELLARLNLPERLWD--------LPPATFSGGEQQRVNIARGFI 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493533268 486 SNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRV 538
Cdd:COG4778  169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVReAVADRV 222

COG4586

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

353-565

9.34e-17

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

Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 81.29 E-value: 9.34e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING-DPVSNSALLRPYIGFV-EQTPTLFEKCTLLENI 430
Cdd:COG4586   38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPFKRRKEFARRIGVVfGQRSQLWWDLPAIDSF 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 431 TLGRSISKASlENIFERtNLDVLLRRFENG--LDTLVAdiQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEII 508
Cdd:COG4586  118 RLLKAIYRIP-DAEYKK-RLDELVELLDLGelLDTPVR--QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAI 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493533268 509 QNTLLGL-RSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLKTSSEYKKL 565
Cdd:COG4586  194 REFLKEYnRERGTTILLTSHDMDDIEaLCDRVIVIDHGRIIYDGSLEELKERFGPYKTI 252

PTZ00243

ABC transporter; Provisional

352-555

1.01e-16

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 84.06 E-value: 1.01e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  352 ILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGFVEQTPTLFEKcTLLEN 429
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLreLRRQFSMIPQDPVLFDG-TVRQN 1403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  430 ITlgrSISKASLENIFERTNLDVLLRRF---ENGLDTLVAD--IQLSGGERQLVALARALVSNPRLLIL-DEITANIDSK 503
Cdd:PTZ00243 1404 VD---PFLEASSAEVWAALELVGLRERVaseSEGIDSRVLEggSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPA 1480

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 493533268  504 TEEIIQNTLLGLRSeGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNEL 555
Cdd:PTZ00243 1481 LDRQIQATVMSAFS-AYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531

PRK10575

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

337-557

1.68e-16

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

Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.83 E-value: 1.68e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVS--NSALLRPYIGFV 414
Cdd:PRK10575  11 TFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAYL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQTPTLFEKCTLLENITLGR--------SISKASLENIFERTNLdVLLRRFENGL-DTlvadiqLSGGERQLVALARALV 485
Cdd:PRK10575  91 PQQLPAAEGMTVRELVAIGRypwhgalgRFGAADREKVEEAISL-VGLKPLAHRLvDS------LSGGERQRAWIAMLVA 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 486 SNPRLLILDEITANIDSKTeeiiQNTLLGL-----RSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLK 557
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAH----QVDVLALvhrlsQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAELMR 237

cbiO

PRK13645

energy-coupling factor transporter ATPase;

336-568

1.92e-16

energy-coupling factor transporter ATPase;

Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.05 E-value: 1.92e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 336 RSISLENIAFGYGNK-----QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIyINGD--------PVS 402
Cdd:PRK13645   5 KDIILDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGDyaipanlkKIK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 403 NSALLRPYIGFVEQTP--TLFEKcTLLENITLGRSISKASLENIFERT----NLDVLLRRFENGldtlvADIQLSGGERQ 476
Cdd:PRK13645  84 EVKRLRKEIGLVFQFPeyQLFQE-TIEKDIAFGPVNLGENKQEAYKKVpellKLVQLPEDYVKR-----SPFELSGGQKR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 477 LVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASG---- 550
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLrIADEVIVMHEGKVISIGspfe 237

                        250       260
                 ....*....|....*....|.
gi 493533268 551 --THNELL-KTSSEYKKLYSL 568
Cdd:PRK13645 238 ifSNQELLtKIEIDPPKLYQL 258

cbiO

PRK13640

energy-coupling factor transporter ATPase;

338-565

2.27e-16

energy-coupling factor transporter ATPase;

Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.84 E-value: 2.27e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGN--KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQS---GTIYINGDPVSNSAL--LRPY 410
Cdd:PRK13640   6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVwdIREK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 411 IGFVEQTP-TLFEKCTLLENITLG---RSISKASLENIFERTNLDVLLrrfengLDTLVADIQ-LSGGERQLVALARALV 485
Cdd:PRK13640  86 VGIVFQNPdNQFVGATVGDDVAFGlenRAVPRPEMIKIVRDVLADVGM------LDYIDSEPAnLSGGQKQRVAIAGILA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 486 SNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYKK 564
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKE 239


                 .
gi 493533268 565 L 565
Cdd:PRK13640 240 I 240

PRK13540

cytochrome c biogenesis protein CcmA; Provisional

342-528

4.36e-16

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 76.91 E-value: 4.36e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 342 NIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV-SNSALLRPYIGFVEQTPTL 420
Cdd:PRK13540   6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQLCFVGHRSGI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 421 FEKCTLLENITLGRSISKASLEnifertnLDVLLRRFENG--LDTLVAdiQLSGGERQLVALARALVSNPRLLILDEITA 498
Cdd:PRK13540  86 NPYLTLRENCLYDIHFSPGAVG-------ITELCRLFSLEhlIDYPCG--LLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 493533268 499 NIDSKTEEIIQNTLLGLRSEGIIVLMVAHR 528
Cdd:PRK13540 157 ALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186

cbiO

PRK13634

cobalt transporter ATP-binding subunit; Provisional

353-565

4.90e-16

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.91 E-value: 4.90e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYInGDPV-----SNSAL--LRPYIGFVEQTP--TLFEK 423
Cdd:PRK13634  23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkKNKKLkpLRKKVGIVFQFPehQLFEE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 424 cTLLENITLGRSISKASLENIFERTNLDVLLRrfenGLDTLVAD---IQLSGGERQLVALARALVSNPRLLILDEITANI 500
Cdd:PRK13634 102 -TVEKDICFGPMNFGVSEEDAKQKAREMIELV----GLPEELLArspFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268 501 DSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLKTSSEYKKL 565
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAArYADQIVVMHKGTVFLQGTPREIFADPDELEAI 243

cbiO

PRK13649

energy-coupling factor transporter ATPase;

337-551

7.23e-16

energy-coupling factor transporter ATPase;

Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 78.25 E-value: 7.23e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 337 SISLENIAFGYG-----NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL----- 406
Cdd:PRK13649   2 GINLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdik 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 407 -LRPYIGFVEQTP--TLFEKcTLLENITLGRS---ISKASLENIfERTNLDVLlrrfenGLDTLVAD---IQLSGGERQL 477
Cdd:PRK13649  82 qIRKKVGLVFQFPesQLFEE-TVLKDVAFGPQnfgVSQEEAEAL-AREKLALV------GISESLFEknpFELSGGQMRR 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 478 VALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGT 551
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGK 228

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

328-551

8.75e-16

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

Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 80.11 E-value: 8.75e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 328 SSPKLEDVRSISlenIAFG--YGNKQILKGLSLELRKGEITTLVGESGAGKT-TTLNILMGLQKPQ---SGTIYINGDPV 401
Cdd:COG4172    2 MSMPLLSVEDLS---VAFGqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 402 SN--SALLRPY----IGFVEQTPTlfekcTLL-----------ENITLGRSISKASLEnifERTnLDvLLRRFenGLDTL 464
Cdd:COG4172   79 LGlsERELRRIrgnrIAMIFQEPM-----TSLnplhtigkqiaEVLRLHRGLSGAAAR---ARA-LE-LLERV--GIPDP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 465 VADI-----QLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTV-LLSDR 537
Cdd:COG4172  147 ERRLdayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVrRFADR 226

                        250
                 ....*....|....
gi 493533268 538 VALISNGVIVASGT 551
Cdd:COG4172  227 VAVMRQGEIVEQGP 240

PRK10522

multidrug transporter membrane component/ATP-binding component; Provisional

312-546

8.88e-16

multidrug transporter membrane component/ATP-binding component; Provisional

Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 80.40 E-value: 8.88e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 312 LRTIEVLE-APEEERSNSSPKLEDVRSISLENIAFGYGNKQI-LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKP 389
Cdd:PRK10522 296 FNKLNKLAlAPYKAEFPRPQAFPDWQTLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQP 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 390 QSGTIYINGDPVS--NSALLRPYIGFVEQTPTLFEKctLLENitLGRSISKASLENIFERTNLDVLLrRFENGldtLVAD 467
Cdd:PRK10522 376 QSGEILLDGKPVTaeQPEDYRKLFSAVFTDFHLFDQ--LLGP--EGKPANPALVEKWLERLKMAHKL-ELEDG---RISN 447

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 468 IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLG-LRSEGIIVLMVAHRLSTVLLSDRVALISNGVI 546
Cdd:PRK10522 448 LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPlLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

316-510

9.14e-16

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 80.36 E-value: 9.14e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  316 EVLEAPEEERSNSS-------PKLEDVrSISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQK 388
Cdd:TIGR03719 295 ELLSQEFQKRNETAeiyippgPRLGDK-VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQ 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  389 PQSGTIYInGDPVSnsallrpyIGFVEQT-PTLFEKCTLLENITLGRSISKASLENIFERTnldvLLRRFE-NGLD--TL 464
Cdd:TIGR03719 374 PDSGTIEI-GETVK--------LAYVDQSrDALDPNKTVWEEISGGLDIIKLGKREIPSRA----YVGRFNfKGSDqqKK 440

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 493533268  465 VAdiQLSGGERQLVALARALVSNPRLLILDEITANIDSKT----EEIIQN 510
Cdd:TIGR03719 441 VG--QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETlralEEALLN 488

PLN03211

ABC transporter G-25; Provisional

350-544

1.59e-15

ABC transporter G-25; Provisional

Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.92 E-value: 1.59e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 350 KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQS--GTIYINGDPVSNSALLRpyIGFVEQTPTLFEKCTLL 427
Cdd:PLN03211  81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKR--TGFVTQDDILYPHLTVR 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 428 ENIT------LGRSISKASLENIFERTNLDVLLRRFENGL--DTLVADIqlSGGERQLVALARALVSNPRLLILDEITAN 499
Cdd:PLN03211 159 ETLVfcsllrLPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGI--SGGERKRVSIAHEMLINPSLLILDEPTSG 236

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 493533268 500 IDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL--LSDRVALISNG 544
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVyqMFDSVLVLSEG 283

PRK10762

D-ribose transporter ATP binding protein; Provisional

353-544

2.57e-15

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.51 E-value: 2.57e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAllrPY------IGFVEQTPTLFEKCTL 426
Cdd:PRK10762  20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNG---PKssqeagIGIIHQELNLIPQLTI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 427 LENITLGRSISkasleNIFERTN-------LDVLLRRF--ENGLDTLVADiqLSGGERQLVALARALVSNPRLLILDEIT 497
Cdd:PRK10762  97 AENIFLGREFV-----NRFGRIDwkkmyaeADKLLARLnlRFSSDKLVGE--LSIGEQQMVEIAKVLSFESKVIIMDEPT 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 493533268 498 -ANIDSKTEEIIqNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNG 544
Cdd:PRK10762 170 dALTDTETESLF-RVIRELKSQGRGIVYISHRLKEIFeICDDVTVFRDG 217

cbiO

PRK13652

cobalt transporter ATP-binding subunit; Provisional

338-555

2.65e-15

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 76.38 E-value: 2.65e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGY-GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAL--LRPYIGFV 414
Cdd:PRK13652   4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIreVRKFVGLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQTP--TLFEKcTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTlvADIQLSGGERQLVALARALVSNPRLLI 492
Cdd:PRK13652  84 FQNPddQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDR--VPHHLSGGEKKRVAIAGVIAMEPQVLV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 493 LDEITANIDSK-TEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNEL 555
Cdd:PRK13652 161 LDEPTAGLDPQgVKELIDFLNDLPETYGMTVIFSTHQLDLVPeMADYIYVMDKGRIVAYGTVEEI 225

PRK15056

manganese/iron ABC transporter ATP-binding protein;

353-550

2.66e-15

manganese/iron ABC transporter ATP-binding protein;

Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.46 E-value: 2.66e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVsNSALLRPYIGFVEQT-------PTLFEKCT 425
Cdd:PRK15056  23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-RQALQKNLVAYVPQSeevdwsfPVLVEDVV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 426 LLEN------ITLGRSISKASLENIFERTNLdVLLRRFENGldtlvadiQLSGGERQLVALARALVSNPRLLILDEITAN 499
Cdd:PRK15056 102 MMGRyghmgwLRRAKKRDRQIVTAALARVDM-VEFRHRQIG--------ELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 493533268 500 IDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRVALISNGVIVASG 550
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223

dppF

PRK11308

dipeptide transporter ATP-binding subunit; Provisional

351-532

3.03e-15

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.93 E-value: 3.03e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 351 QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING-DPVSNS----ALLRPYIGFVEQTP------- 418
Cdd:PRK11308  29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqDLLKADpeaqKLLRQKIQIVFQNPygslnpr 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 419 -----TLFEKctLLENITLGRSISKASLENIFERtnldVLLR-----RFENgldtlvadiQLSGGERQLVALARALVSNP 488
Cdd:PRK11308 109 kkvgqILEEP--LLINTSLSAAERREKALAMMAK----VGLRpehydRYPH---------MFSGGQRQRIAIARALMLDP 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 493533268 489 RLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTV 532
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVV 218

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

346-546

3.07e-15

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.67 E-value: 3.07e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 346 GYGNKQIlKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING---DPVSNSALLRPYIGFVEQT---PT 419
Cdd:PRK09700 273 SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdiSPRSPLDAVKKGMAYITESrrdNG 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 420 LFEKCTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTL---VADI-----QLSGGERQLVALARALVSNPRLL 491
Cdd:PRK09700 352 FFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLalkCHSVnqnitELSGGNQQKVLISKWLCCCPEVI 431

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 492 ILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVI 546
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIItVCDRIAVFCEGRL 487

PRK09984

phosphonate ABC transporter ATP-binding protein;

338-551

3.28e-15

phosphonate ABC transporter ATP-binding protein;

Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.82 E-value: 3.28e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGL---QKPQSGTIYINGDPVSNSALL------- 407
Cdd:PRK09984   5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLardirks 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 408 RPYIGFVEQTPTLFEKCTLLENITLGrsiskASLENIFERTNLDVLLR-RFENGLDTL----VADI------QLSGGERQ 476
Cdd:PRK09984  85 RANTGYIFQQFNLVNRLSVLENVLIG-----ALGSTPFWRTCFSWFTReQKQRALQALtrvgMVHFahqrvsTLSGGQQQ 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268 477 LVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGT 551
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALrYCERIVALRQGHVFYDGS 236

ABCD_peroxisomal_ALDP

cd03223

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...

338-543

3.80e-15

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: 73.34 E-value: 3.80e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGN-KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDpvSNSALL--RPYIGFV 414
Cdd:cd03223    1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG--EDLLFLpqRPYLPLG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 eqtptlfekctlleniTLGRSISKASlenifertnldvllrrfengldtlvaDIQLSGGERQLVALARALVSNPRLLILD 494
Cdd:cd03223   79 ----------------TLREQLIYPW--------------------------DDVLSGGEQQRLAFARLLLHKPKFVFLD 116

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 493533268 495 EITANIDSKTEEIIQNTllgLRSEGIIVLMVAHRLSTVLLSDRVALISN 543
Cdd:cd03223  117 EATSALDEESEDRLYQL---LKELGITVISVGHRPSLWKFHDRVLDLDG 162

PRK13549

xylose transporter ATP-binding subunit; Provisional

349-555

4.43e-15

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.05 E-value: 4.43e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 349 NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQS-GTIYINGDPVSNSA---LLRPYIGFVEQTPTLFEKC 424
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIRNpqqAIAQGIAMVPEDRKRDGIV 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 425 TLL---ENITLG--RSISKAS-LENIFERTNLDVLLRRFENGLDTLVADI-QLSGGERQLVALARALVSNPRLLILDEIT 497
Cdd:PRK13549 354 PVMgvgKNITLAalDRFTGGSrIDDAAELKTILESIQRLKVKTASPELAIaRLSGGNQQKAVLAKCLLLNPKILILDEPT 433

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493533268 498 ANID--SKTEeiIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNEL 555
Cdd:PRK13549 434 RGIDvgAKYE--IYKLINQLVQQGVAIIVISSELPEVLgLSDRVLVMHEGKLKGDLINHNL 492

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

348-504

5.94e-15

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 77.67 E-value: 5.94e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  348 GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGtiyingdpvsnSALLRP--YIGFVEQTPTLFEKCT 425
Cdd:TIGR03719  16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-----------EARPQPgiKVGYLPQEPQLDPTKT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  426 LLENITLGRSISK---------------------------ASLENIFERTNLDVLLRRFENGLDTLV-----ADIQ-LSG 472
Cdd:TIGR03719  85 VRENVEEGVAEIKdaldrfneisakyaepdadfdklaaeqAELQEIIDAADAWDLDSQLEIAMDALRcppwdADVTkLSG 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 493533268  473 GERQLVALARALVSNPRLLILDEITANIDSKT 504
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

352-555

8.95e-15

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: 78.03 E-value: 8.95e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   352 ILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDpvsnsallrpyIGFVEQTPTLFEKcTLLENIT 431
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNII 508

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   432 LGRSISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTE-EII 508
Cdd:TIGR01271  509 FGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEkEIF 588

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 493533268   509 QNTLLGLRSEGIIVLmVAHRLSTVLLSDRVALISNGVIVASGTHNEL 555
Cdd:TIGR01271  589 ESCLCKLMSNKTRIL-VTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634

sufC

TIGR01978

FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...

348-550

9.05e-15

FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]

Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 74.22 E-value: 9.05e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  348 GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQ--SGTIYINGD-----PVSNSALLRPYIGFveQTPTL 420
Cdd:TIGR01978  11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEvtSGTILFKGQdllelEPDERARAGLFLAF--QYPEE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  421 FEKCTLLENItlgrsisKASLENIFERTNLDVL-LRRFENGLDTLVADIQL-------------SGGERQLVALARALVS 486
Cdd:TIGR01978  89 IPGVSNLEFL-------RSALNARRSARGEEPLdLLDFEKLLKEKLALLDMdeeflnrsvnegfSGGEKKRNEILQMALL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268  487 NPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAH--RLSTVLLSDRVALISNGVIVASG 550
Cdd:TIGR01978 162 EPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227

ABC_6TM_HetC_like

cd18568

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...

24-300

9.52e-15

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: 74.90 E-value: 9.52e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVmiaLAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLEK 103
Cdd:cd18568    8 LLASLLLQL---LGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 104 MFVLPFDFFHKNKTGELVSRL-----ISDLeLVGTVIAqvfpiLLLGVVQITAILAIMFAFNWKLTLLPLGFIV-FSFLV 177
Cdd:cd18568   85 LLSLPLSFFASRKVGDIITRFqenqkIRRF-LTRSALT-----TILDLLMVFIYLGLMFYYNLQLTLIVLAFIPlYVLLT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 178 IMFFNIMvekrSKVEREKFGELAGVTSNIIDNMKLIRIAMPFAWVMNFFDRFQGDHIYAGKRFIKSIKIA---GTLKTSI 254
Cdd:cd18568  159 LLSSPKL----KRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSivlQLISSLI 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 493533268 255 NGLISFSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQV 300
Cdd:cd18568  235 NHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGL 280

PRK10253

iron-enterobactin ABC transporter ATP-binding protein;

333-569

1.16e-14

iron-enterobactin ABC transporter ATP-binding protein;

Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 74.25 E-value: 1.16e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 333 EDVRSISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN--SALLRPY 410
Cdd:PRK10253   3 ESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaSKEVARR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 411 IGFVEQTPTLFEKCTLLENITLGRsISKASLENIFERTNLDVLLRRFE-NGLDTLVADI--QLSGGERQLVALARALVSN 487
Cdd:PRK10253  83 IGLLAQNATTPGDITVQELVARGR-YPHQPLFTRWRKEDEEAVTKAMQaTGITHLADQSvdTLSGGQRQRAWIAMVLAQE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 488 PRLLILDEITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAH------RLSTVLLSDRvalisNGVIVASGTHNELLkTSS 560
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHdlnqacRYASHLIALR-----EGKIVAQGAPKEIV-TAE 235


                 ....*....
gi 493533268 561 EYKKLYSLQ 569
Cdd:PRK10253 236 LIERIYGLR 244

cbiO

PRK13646

energy-coupling factor transporter ATPase;

350-566

1.57e-14

energy-coupling factor transporter ATPase;

Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.43 E-value: 1.57e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 350 KQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSA---LLRPY---IGFVEQTP--TLF 421
Cdd:PRK13646  20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkYIRPVrkrIGMVFQFPesQLF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 422 EKcTLLENITLGRSISKASLENIFERTnLDVLLRR-FENGLDTLvADIQLSGGERQLVALARALVSNPRLLILDEITANI 500
Cdd:PRK13646 100 ED-TVEREIIFGPKNFKMNLDEVKNYA-HRLLMDLgFSRDVMSQ-SPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 501 DSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLKTSSEYKKLY 566
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKELFKDKKKLADWH 244

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

88-567

1.78e-14

Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 76.87 E-value: 1.78e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268    88 TALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLelvgTVIAQVFPILLLGVVQIT-------AILAIMFAFN 160
Cdd:TIGR01271  952 TLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDM----AIIDDMLPLTLFDFIQLTlivlgaiFVVSVLQPYI 1027

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   161 WkLTLLPLGFIvfsFLVI-MFFNIMVEKRSKVEREKfgeLAGVTSNIIDNMKLIriampfaWVMNFFDRfqgdHIYAGKR 239
Cdd:TIGR01271 1028 F-IAAIPVAVI---FIMLrAYFLRTSQQLKQLESEA---RSPIFSHLITSLKGL-------WTIRAFGR----QSYFETL 1089

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   240 FIKSIkiagTLKTSIngliSFSLLAYGGYLVMKGEITVGIL---MTFWAYVQSLFNP----IQLLMQVNILLRQSWG--- 309
Cdd:TIGR01271 1090 FHKAL----NLHTAN----WFLYLSTLRWFQMRIDIIFVFFfiaVTFIAIGTNQDGEgevgIILTLAMNILSTLQWAvns 1161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   310 -----GLLRTIEVL--------EAPEEERSNSSPKLEDVRSI---------------SLENIAFGY--GNKQILKGLSLE 359
Cdd:TIGR01271 1162 sidvdGLMRSVSRVfkfidlpqEEPRPSGGGGKYQLSTVLVIenphaqkcwpsggqmDVQGLTAKYteAGRAVLQDLSFS 1241

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   360 LRKGEITTLVGESGAGKTTTLNILMGLQKPQsGTIYINGdpVS-NSALL---RPYIGFVEQTPTLFEKcTLLENITLGRS 435
Cdd:TIGR01271 1242 VEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDG--VSwNSVTLqtwRKAFGVIPQKVFIFSG-TFRKNLDPYEQ 1317

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   436 ISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLL 513
Cdd:TIGR01271 1318 WSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDggYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLK 1397

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 493533268   514 GLRSEgIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYKKLYS 567
Cdd:TIGR01271 1398 QSFSN-CTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMS 1450

ABC_6TM_AtABCB27_like

cd18780

Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...

27-286

2.29e-14

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: 73.82 E-value: 2.29e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  27 AVLVGVMIALAVvfPLLIRLLIDVVI------PSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQL 100
Cdd:cd18780    4 ALLVSSGTNLAL--PYFFGQVIDAVTnhsgsgGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 101 LEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGfiVFSFLVIMF 180
Cdd:cd18780   82 FSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLS--VVPPLSIGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 181 fnIMVEKRSKVEREKFGELAGVTSNI----IDNMKLIRiamPFAWVMNFFDRFQGDhIYAGKRFIKSIKIAGTLKTSING 256
Cdd:cd18780  160 --VIYGKYVRKLSKKFQDALAAASTVaeesISNIRTVR---SFAKETKEVSRYSEK-INESYLLGKKLARASGGFNGFMG 233

                        250       260       270
                 ....*....|....*....|....*....|....
gi 493533268 257 LISF----SLLAYGGYLVMKGEITVGILMTFWAY 286
Cdd:cd18780  234 AAAQlaivLVLWYGGRLVIDGELTTGLLTSFLLY 267

PRK13543

heme ABC exporter ATP-binding protein CcmA;

343-501

3.37e-14

heme ABC exporter ATP-binding protein CcmA;

Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 71.80 E-value: 3.37e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 343 IAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLRpYIGFVEQTPTLFE 422
Cdd:PRK13543  17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSR-FMAYLGHLPGLKA 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493533268 423 KCTLLENITLGRSISKASLENIFERTNLDVLLRRFEnglDTLVAdiQLSGGERQLVALARALVSNPRLLILDEITANID 501
Cdd:PRK13543  96 DLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYE---DTLVR--QLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169

MK0520

COG2401

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...

291-528

5.64e-14

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

Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.53 E-value: 5.64e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 291 FNPIQLLMQVNILLRQswggllrtievleapeeeRSNSSPKLEDVrsISLENIAFGYGNKQILKGLSLELRKGEITTLVG 370
Cdd:COG2401    4 YNPFFVLMRVTKVYSS------------------VLDLSERVAIV--LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 371 ESGAGKTTTLNILMGLQK--PQSGTIYINGDPVSnsallrpyigfveqtptlfEKCTLLENITLGRSIsKASLEnIFERT 448
Cdd:COG2401   64 ASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFG-------------------REASLIDAIGRKGDF-KDAVE-LLNAV 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 449 NL-DV--LLRRFENgldtlvadiqLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGL-RSEGIIVLM 524
Cdd:COG2401  123 GLsDAvlWLRRFKE----------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVV 192


                 ....
gi 493533268 525 VAHR 528
Cdd:COG2401  193 ATHH 196

ABC_6TM_NHLM_bacteriocin

cd18569

Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ...

21-300

6.20e-14

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

Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 72.51 E-value: 6.20e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  21 KRELLAAVLVGV-MIALAVVFPLLIRLLIDVVIPSGDMDllvkyvllvvglWFGSLIFTYFGEVVFET--TALMAKSDLR 97
Cdd:cd18569    1 RSALLFVVLAGLlLVIPGLVIPVFSRIFIDDILVGGLPD------------WLRPLLLGMALTALLQGllTWLQQYYLLR 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  98 ----------KQLLEKMFVLPFDFFHKNKTGELVSRLISDlELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLP 167
Cdd:cd18569   69 letklalsssSRFFWHVLRLPVEFFSQRYAGDIASRVQSN-DRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 168 LGFIVFSFLVIMFF-NIMVEKRSKVEREKfGELAGVTSNIIDNMKLIRIAmpfAWVMNFFDR---FQGDHIYAGKRFIKS 243
Cdd:cd18569  148 IAIALLNLLVLRLVsRKRVDLNRRLLQDS-GKLTGTTMSGLQMIETLKAS---GAESDFFSRwagYQAKVLNAQQELGRT 223

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268 244 IKIAGTLKTSINGLISFSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQV 300
Cdd:cd18569  224 NQLLGALPTLLSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGL 280

ABC_6TM_exporter_like

cd18565

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

24-300

6.83e-14

Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 72.60 E-value: 6.83e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVmiALAVVF---PLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQL 100
Cdd:cd18565   16 LAPPLLIGV--AIDAVFngeASFLPLVPASLGPADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 101 LEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIMF 180
Cdd:cd18565   94 YDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYW 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 181 FNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRiampfAWVMnffDRFQGDHIYAGKR-----FIKSIKIAGTLKTSIN 255
Cdd:cd18565  174 FQRRIEPRYRAVREAVGDLNARLENNLSGIAVIK-----AFTA---EDFERERVADASEeyrdaNWRAIRLRAAFFPVIR 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493533268 256 GLISFSLLA---YGGYLVMKG------EITVGILMTFWAYVQSLFNPIQLLMQV 300
Cdd:cd18565  246 LVAGAGFVAtfvVGGYWVLDGpplftgTLTVGTLVTFLFYTQRLLWPLTRLGDL 299

ABCC_CFTR1

cd03291

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...

316-555

7.18e-14

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: 72.20 E-value: 7.18e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 316 EVLEAPEEERSNSSPKLEDvRSISLENIAFgYGNKqILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIY 395
Cdd:cd03291   19 ELLEKAKQENNDRKHSSDD-NNLFFSNLCL-VGAP-VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 396 INGDpvsnsallrpyIGFVEQTPTLFEKcTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGG 473
Cdd:cd03291   96 HSGR-----------ISFSSQFSWIMPG-TIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEggITLSGG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 474 ERQLVALARALVSNPRLLILDEITANIDSKTE-EIIQNTLLGLRSEGIIVLmVAHRLSTVLLSDRVALISNGVIVASGTH 552
Cdd:cd03291  164 QRARISLARAVYKDADLYLLDSPFGYLDVFTEkEIFESCVCKLMANKTRIL-VTSKMEHLKKADKILILHEGSSYFYGTF 242


                 ...
gi 493533268 553 NEL 555
Cdd:cd03291  243 SEL 245

ABCC_SUR1_N

cd03290

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...

353-544

7.89e-14

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: 70.82 E-value: 7.89e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALL------RPYIGFVEQTPTLFeKCTL 426
Cdd:cd03290   17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEatrsrnRYSVAYAAQKPWLL-NATV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 427 LENITLGRSISKASLENIFERTNL--DVLLRRFENGLDTLVADIQLSGGERQLVALARALVSNPRLLILDEITANIDSK- 503
Cdd:cd03290   96 EENITFGSPFNKQRYKAVTDACSLqpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 493533268 504 TEEIIQNTLLG-LRSEGIIVLMVAHRLSTVLLSDRVALISNG 544
Cdd:cd03290  176 SDHLMQEGILKfLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217

hmuV

PRK13547

heme ABC transporter ATP-binding protein;

352-557

9.51e-14

heme ABC transporter ATP-binding protein;

Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.78 E-value: 9.51e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 352 ILKGLSLELRKGEITTLVGESGAGKTTTLNILMG-LQKPQ-------SGTIYINGDPVS-----NSALLRPYIGFVEQTP 418
Cdd:PRK13547  16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAaidapRLARLRAVLPQAAQPA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 419 TLFekcTLLENITLGR--SISKASLENIFERTNLDVLLRRfeNGLDTLVA-DIQ-LSGGERQLVALARAL---------V 485
Cdd:PRK13547  96 FAF---SAREIVLLGRypHARRAGALTHRDGEIAWQALAL--AGATALVGrDVTtLSGGELARVQFARVLaqlwpphdaA 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493533268 486 SNPRLLILDEITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAHRLS-TVLLSDRVALISNGVIVASGTHNELLK 557
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVLT 244

ABCC_CFTR2

cd03289

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...

348-567

1.62e-13

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: 71.04 E-value: 1.62e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 348 GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQsGTIYINGdpVS-NSALL---RPYIGFVEQTPTLFEK 423
Cdd:cd03289   15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDG--VSwNSVPLqkwRKAFGVIPQKVFIFSG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 424 cTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQLVALARALVSNPRLLILDEITANID 501
Cdd:cd03289   92 -TFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDggCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 502 SKTEEIIQNTLLGLRSeGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNELLKTSSEYKKLYS 567
Cdd:cd03289  171 PITYQVIRKTLKQAFA-DCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAIS 235

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

357-554

1.67e-13

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 1.67e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 357 SLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSnsalLRPYIGFVEQTPTLfekC------------ 424
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID----IRSPRDAIRAGIML---Cpedrkaegiipv 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 425 -TLLENITLG--RSISKAS--LENIFERTNLDVLLRRFE---NGLDTLVadIQLSGGERQLVALARALVSNPRLLILDEI 496
Cdd:PRK11288 346 hSVADNINISarRHHLRAGclINNRWEAENADRFIRSLNiktPSREQLI--MNLSGGNQQKAILGRWLSEDMKVILLDEP 423

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493533268 497 TANID--SKTEeiIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNE 554
Cdd:PRK11288 424 TRGIDvgAKHE--IYNVIYELAAQGVAVLFVSSDLPEVLgVADRIVVMREGRIAGELAREQ 482

PRK13651

cobalt transporter ATP-binding subunit; Provisional

338-557

1.71e-13

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.27 E-value: 1.71e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNK-----QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTI-YINGDPVSNSAL----- 406
Cdd:PRK13651   3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDEKNKKKTkekek 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 407 --------------------LRPYIGFVEQTP--TLFEKcTLLENITLG-RS--ISKASLE----NIFERTNLDV-LLRR 456
Cdd:PRK13651  83 vleklviqktrfkkikkikeIRRRVGVVFQFAeyQLFEQ-TIEKDIIFGpVSmgVSKEEAKkraaKYIELVGLDEsYLQR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 457 --FEngldtlvadiqLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL- 533
Cdd:PRK13651 162 spFE-----------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLe 230

                        250       260
                 ....*....|....*....|....
gi 493533268 534 LSDRVALISNGVIVASGTHNELLK 557
Cdd:PRK13651 231 WTKRTIFFKDGKIIKDGDTYDILS 254

PRK13541

cytochrome c biogenesis protein CcmA; Provisional

338-532

2.06e-13

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 69.13 E-value: 2.06e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKgLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAllRPYIGFVEQT 417
Cdd:PRK13541   2 LSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--KPYCTYIGHN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PTLFEKCTLLENITLGRSISKASlenifERTNLDVLLRRFENGLDTLVAdiQLSGGERQLVALARALVSNPRLLILDEIT 497
Cdd:PRK13541  79 LGLKLEMTVFENLKFWSEIYNSA-----ETLYAAIHYFKLHDLLDEKCY--SLSSGMQKIVAIARLIACQSDLWLLDEVE 151

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 493533268 498 ANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV 532
Cdd:PRK13541 152 TNLSKENRDLLNNLIVMKANSGGIVLLSSHLESSI 186

ABC_6TM_ABCB9_like

cd18784

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...

111-309

2.37e-13

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

Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 70.80 E-value: 2.37e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 111 FFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIMFFNIMVEKRSK 190
Cdd:cd18784   86 FFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSK 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 191 VEREKFGELAGVTSNIIDNMKLIRiamPFAWVMNFFDRFQgDHIYAGKRFIKSIKIAGTLKTSINGLISFSL----LAYG 266
Cdd:cd18784  166 AVQDSLAKANEVAEETISSIRTVR---SFANEDGEANRYS-EKLKDTYKLKIKEALAYGGYVWSNELTELALtvstLYYG 241

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 493533268 267 GYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQVNILLRQSWG 309
Cdd:cd18784  242 GHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVG 284

PRK14243

phosphate transporter ATP-binding protein; Provisional

341-522

2.45e-13

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.20 E-value: 2.45e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 341 ENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTL------NILMGLQKPQsGTIYING--------DPVSnsal 406
Cdd:PRK14243  14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIPGFRVE-GKVTFHGknlyapdvDPVE---- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 407 LRPYIGFVEQTPTLFEKcTLLENITLGRSIS--KASLENIFERTnldvlLRR---FENGLDTL-VADIQLSGGERQLVAL 480
Cdd:PRK14243  89 VRRRIGMVFQKPNPFPK-SIYDNIAYGARINgyKGDMDELVERS-----LRQaalWDEVKDKLkQSGLSLSGGQQQRLCI 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 493533268 481 ARALVSNPRLLILDEITANIDS----KTEEIIQNtlLGLRSEGIIV 522
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPistlRIEELMHE--LKEQYTIIIV 206

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

356-546

2.82e-13

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 2.82e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 356 LSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN-SALLRPYIGFV-----EQTPTLF-------E 422
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAlSTAQRLARGLVylpedRQSSGLYldaplawN 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 423 KCTLLENiTLGRSISKASLENIFErtnldvllrRFENGLDTLVADIQ-----LSGGERQLVALARALVSNPRLLILDEIT 497
Cdd:PRK15439 362 VCALTHN-RRGFWIKPARENAVLE---------RYRRALNIKFNHAEqaartLSGGNQQKVLIAKCLEASPQLLIVDEPT 431

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 493533268 498 ANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVI 546
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIeQMADRVLVMHQGEI 481

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

340-549

2.93e-13

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.07 E-value: 2.93e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 340 LENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV---SNSALLRPYIGFVEQ 416
Cdd:PRK10982   1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 417 TPTLFEKCTLLENITLGRSISKA----------SLENIFERTNLDVllrrfenglDTLVADIQLSGGERQLVALARALVS 486
Cdd:PRK10982  81 ELNLVLQRSVMDNMWLGRYPTKGmfvdqdkmyrDTKAIFDELDIDI---------DPRAKVATLSVSQMQMIEIAKAFSY 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493533268 487 NPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVAS 549
Cdd:PRK10982 152 NAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFqLCDEITILRDGQWIAT 215

ABC_6TM_CvaB_RaxB_like

cd18567

Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...

21-303

3.94e-13

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: 70.18 E-value: 3.94e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  21 KRELLAAVLVGVMI-ALAVVFPLLIRLLIDVVIPSGDMDLLVKyvllvvglwfgsLIFTYFGEVVFETTALMAKS----- 94
Cdd:cd18567    1 KRALLQILLLSLALeLFALASPLYLQLVIDEVIVSGDRDLLTV------------LAIGFGLLLLLQALLSALRSwlvly 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  95 -------DLRKQLLEKMFVLPFDFFHKNKTGELVSRLISdLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLP 167
Cdd:cd18567   69 lstslnlQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 168 LGFIVFSFLV-IMFFNIMvekrSKVEREKFGELAGVTSNIIDNMKLIRIAMPFAWVMNFFDRFQG---DHIYAGKRfIKS 243
Cdd:cd18567  148 LAAVALYALLrLALYPPL----RRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNllvDAINADIR-LQR 222

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 244 IKIA-GTLKTSINGLISFSLLAYGGYLVMKGEITVGILMTFWAY----VQSLFNPIQLLMQVNIL 303
Cdd:cd18567  223 LQILfSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYkdqfSSRASSLIDKLFELRML 287

PTZ00243

ABC transporter; Provisional

319-559

4.75e-13

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.50 E-value: 4.75e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  319 EAPEEERSNSSPKLEDVRSISLENiafgygnKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING 398
Cdd:PTZ00243  649 ATPTSERSAKTPKMKTDDFFELEP-------KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER 721

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  399 DpvsnsallrpyIGFVEQTPTLFeKCTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTLVAD--IQLSGGERQ 476
Cdd:PTZ00243  722 S-----------IAYVPQQAWIM-NATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEkgVNLSGGQKA 789

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  477 LVALARALVSNPRLLILDEITANIDSKT-EEIIQNTLLGlRSEGIIVLMVAHRLSTVLLSDRVALISNGVIVASGTHNEL 555
Cdd:PTZ00243  790 RVSLARAVYANRDVYLLDDPLSALDAHVgERVVEECFLG-ALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADF 868


                  ....
gi 493533268  556 LKTS 559
Cdd:PTZ00243  869 MRTS 872

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

348-501

1.57e-12

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.15 E-value: 1.57e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 348 GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPqsgtiyINGDpvsnsALLRP--YIGFVEQTPTLFEKCT 425
Cdd:PRK11819  18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE------FEGE-----ARPAPgiKVGYLPQEPQLDPEKT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 426 LLENITLGRS-----------IS----------------KASLENIFERTNLDVLLRRFENGLDTLV-----ADI-QLSG 472
Cdd:PRK11819  87 VRENVEEGVAevkaaldrfneIYaayaepdadfdalaaeQGELQEIIDAADAWDLDSQLEIAMDALRcppwdAKVtKLSG 166

                        170       180
                 ....*....|....*....|....*....
gi 493533268 473 GERQLVALARALVSNPRLLILDEITANID 501
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLD 195

oppD

PRK09473

oligopeptide transporter ATP-binding component; Provisional

321-555

2.54e-12

oligopeptide transporter ATP-binding component; Provisional

Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.21 E-value: 2.54e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 321 PEEERSNSSPKLEDVRSIsleNIAFGY--GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQ---SGTIY 395
Cdd:PRK09473   1 TVPLAQQQADALLDVKDL---RVTFSTpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSAT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 396 ING------------------------DPVSNsalLRPYIGFVEQtptlfekctLLENITLGRSISKASlenIFERT--N 449
Cdd:PRK09473  78 FNGreilnlpekelnklraeqismifqDPMTS---LNPYMRVGEQ---------LMEVLMLHKGMSKAE---AFEESvrM 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 450 LDVL--------LRRFENgldtlvadiQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GI 520
Cdd:PRK09473 143 LDAVkmpearkrMKMYPH---------EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNT 213

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 493533268 521 IVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNEL 555
Cdd:PRK09473 214 AIIMITHDLGVVAgICDKVLVMYAGRTMEYGNARDV 249

3a01205

TIGR00956

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

348-544

3.06e-12

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

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.75 E-value: 3.06e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   348 GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNIL-----MGLQkpQSGTIYINGDPVSNSALLRpyIGFVEQTPTLFE 422
Cdd:TIGR00956  774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSSFQRS--IGYVQQQDLHLP 849

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   423 KCTLLENITLG---RSISKASLENIFERTNLDVLLRRFENGLDTLV--ADIQLSGGERQLVALARALVSNPRLLI-LDEI 496
Cdd:TIGR00956  850 TSTVRESLRFSaylRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVgvPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 493533268   497 TANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLS--DRVALISNG 544
Cdd:TIGR00956  930 TSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEefDRLLLLQKG 979

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

356-555

3.12e-12

Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.04 E-value: 3.12e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   356 LSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV-SNSALLRPYIGFVEQTPTLFEKCTLLENITLGR 434
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYA 2037

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   435 SISKASLENIFERTNLDVLlrrfENGLdTLVADI---QLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNT 511
Cdd:TIGR01257 2038 RLRGVPAEEIEKVANWSIQ----SLGL-SLYADRlagTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 493533268   512 LLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVIVASGTHNEL 555
Cdd:TIGR01257 2113 IVSIIREGRAVVLTSHSMEECeALCTRLAIMVKGAFQCLGTIQHL 2157

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

338-510

3.19e-12

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.99 E-value: 3.19e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYInGDPVSnsallrpyIGFVEQT 417
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK--------LAYVDQS 395

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 -PTLFEKCTLLENITLGrsiskasLENI----FErTNLDVLLRRFE-NGldtlvADIQ-----LSGGERQLVALARALVS 486
Cdd:PRK11819 396 rDALDPNKTVWEEISGG-------LDIIkvgnRE-IPSRAYVGRFNfKG-----GDQQkkvgvLSGGERNRLHLAKTLKQ 462

                        170       180
                 ....*....|....*....|....*...
gi 493533268 487 NPRLLILDEITANIDSKT----EEIIQN 510
Cdd:PRK11819 463 GGNVLLLDEPTNDLDVETlralEEALLE 490

ABC_6TM_Tm287_like

cd18548

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...

24-298

3.51e-12

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: 67.42 E-value: 3.51e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIF----TYFGEVVfetTALMAKsDLRKQ 99
Cdd:cd18548    2 ILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAgilaGYFAAKA---SQGFGR-DLRKD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 100 LLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVvqITAILAIMFAF--NWKLTLLPLGFIVFSFLV 177
Cdd:cd18548   78 LFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAP--IMLIGAIIMAFriNPKLALILLVAIPILALV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 178 IMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRiampfAWVMNFF--DRFQGDHIYAGKRFIKSIKIAGTLKTSIN 255
Cdd:cd18548  156 VFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIR-----AFNREDYeeERFDKANDDLTDTSLKAGRLMALLNPLMM 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 493533268 256 GLISFSLLA---YGGYLVMKGEITVGILMTFWAYVqslfnpIQLLM 298
Cdd:cd18548  231 LIMNLAIVAilwFGGHLINAGSLQVGDLVAFINYL------MQILM 270

SapD

COG4170

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

332-558

4.56e-12

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

Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 67.24 E-value: 4.56e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 332 LEDVRSISLEnIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQsgtIYINGD------------ 399
Cdd:COG4170    3 LLDIRNLTIE-IDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN---WHVTADrfrwngidllkl 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 400 -PVSNSALLRPYIGFVEQTPTlfeKCtLLENITLGRSISkaslENIFERTNLDVLLRRFENGLDTLVA-----------D 467
Cdd:COG4170   79 sPRERRKIIGREIAMIFQEPS---SC-LDPSAKIGDQLI----EAIPSWTFKGKWWQRFKWRKKRAIEllhrvgikdhkD 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 468 I------QLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAHRLSTVL-LSDRVA 539
Cdd:COG4170  151 ImnsyphELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISqWADTIT 230

                        250
                 ....*....|....*....
gi 493533268 540 LISNGVIVASGTHNELLKT 558
Cdd:COG4170  231 VLYCGQTVESGPTEQILKS 249

ABC_6TM_PrtD_LapB_HlyB_like

cd18566

Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...

22-300

6.90e-12

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

Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 66.45 E-value: 6.90e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  22 RELLAAVLVGVMIALAVvfPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLL 101
Cdd:cd18566    5 PQVLLASLFINILALAT--PLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 102 EKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILL-LGVVQItaILAIMFAFNWKLTLLPLGFIVFSFLVIMF 180
Cdd:cd18566   83 EHLLSLPLSFFEREPSGAHLERLNSLEQIREFLTGQALLALLdLPFVLI--FLGLIWYLGGKLVLVPLVLLGLFVLVAIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 181 FNIMVEKRSKverEKFGELAGVTSNIIDNMKLIR----IAMPFAWvMNFFDRFQGDHIYAGKRFIKSIKIAGTLKTSING 256
Cdd:cd18566  161 LGPILRRALK---ERSRADERRQNFLIETLTGIHtikaMAMEPQM-LRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQ 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 493533268 257 LISFSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQV 300
Cdd:cd18566  237 VSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGL 280

PLN03130

ABC transporter C family member; Provisional

312-565

8.71e-12

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.23 E-value: 8.71e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  312 LRTIEVLEAPEEERSNSSPKLE-DVRSISLENIAFGY---GNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQ 387
Cdd:PLN03130  588 LKRLEELLLAEERVLLPNPPLEpGLPAISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGEL 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  388 KPQSGTiyingdpvsnSALLRPYIGFVEQTPTLFeKCTLLENITLGRSISKASLENIFERTNLDVLLRRFENGLDTLVAD 467
Cdd:PLN03130  668 PPRSDA----------SVVIRGTVAYVPQVSWIF-NATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGE 736

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  468 --IQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLG--LRSEG-IIVLMVAHRLSTVllsDRVALIS 542
Cdd:PLN03130  737 rgVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKdeLRGKTrVLVTNQLHFLSQV---DRIILVH 813

                         250       260
                  ....*....|....*....|...
gi 493533268  543 NGVIVASGTHNELLKTSSEYKKL 565
Cdd:PLN03130  814 EGMIKEEGTYEELSNNGPLFQKL 836

PRK15079

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

354-555

1.44e-11

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.88 E-value: 1.44e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 354 KGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSA-----LLRPYIGFVEQTPTlfekCTLLE 428
Cdd:PRK15079  38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddewrAVRSDIQMIFQDPL----ASLNP 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 429 NITLGRSIS--------KASLENIFERTN--------LDVLLRRFENgldtlvadiQLSGGERQLVALARALVSNPRLLI 492
Cdd:PRK15079 114 RMTIGEIIAeplrtyhpKLSRQEVKDRVKammlkvglLPNLINRYPH---------EFSGGQCQRIGIARALILEPKLII 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 493 LDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNEL 555
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEV 249

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

357-501

2.77e-11

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.69 E-value: 2.77e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 357 SLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV-SNSALLRPYIGFVEQTPTLFEKCTLLENITLgrs 435
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdAGDIATRRRVGYMSQAFSLYGELTVRQNLEL--- 362

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493533268 436 isKASL-----ENIFERtnLDVLLRRF--ENGLDTLVADIQLsgGERQLVALARALVSNPRLLILDEITANID 501
Cdd:NF033858 363 --HARLfhlpaAEIAAR--VAEMLERFdlADVADALPDSLPL--GIRQRLSLAVAVIHKPELLILDEPTSGVD 429

ABC_RNaseL_inhibitor_domain1

cd03236

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

361-538

3.18e-11

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: 63.92 E-value: 3.18e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 361 RKGEITTLVGESGAGKTTTLNILMGLQKPQSGTiyiNGDPVSNSALLRPYIG----------------------FVEQTP 418
Cdd:cd03236   24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---FDDPPDWDEILDEFRGselqnyftkllegdvkvivkpqYVDLIP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 419 TLFeKCTLLENITlgRSISKASLENIFERTNLDVLLrrfENGLDtlvadiQLSGGERQLVALARALVSNPRLLILDEITA 498
Cdd:cd03236  101 KAV-KGKVGELLK--KKDERGKLDELVDQLELRHVL---DRNID------QLSGGELQRVAIAAALARDADFYFFDEPSS 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 493533268 499 NIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRV 538
Cdd:cd03236  169 YLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLdYLSDYI 209

ABC_RNaseL_inhibitor_domain2

cd03237

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

359-502

4.59e-11

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.

Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.20 E-value: 4.59e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 359 ELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSnsalLRP-YIGfVEQTPTLFEkctllenitLGRSIS 437
Cdd:cd03237   21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS----YKPqYIK-ADYEGTVRD---------LLSSIT 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 438 KASLENIFERTNLDVLLRrFENGLDTLVADiqLSGGERQLVALARALVSNPRLLILDEITANIDS 502
Cdd:cd03237   87 KDFYTHPYFKTEIAKPLQ-IEQILDREVPE--LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

360-541

5.77e-11

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];

Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.19 E-value: 5.77e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 360 LRKGEITTLVGESGAGKTTTLNILMGLQKPQSGtiyINGDPVSNSALLRPYIG----------------------FVEQT 417
Cdd:COG1245   96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLG---DYDEEPSWDEVLKRFRGtelqdyfkklangeikvahkpqYVDLI 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PTLFeKCT---LLENITlgrsiSKASLENIFERTNLDVLLRRfengldtlvaDI-QLSGGERQLVALARALVSNPRLLIL 493
Cdd:COG1245  173 PKVF-KGTvreLLEKVD-----ERGKLDELAEKLGLENILDR----------DIsELSGGELQRVAIAAALLRDADFYFF 236

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493533268 494 DEITANIDSK----TEEIIQNtllgLRSEGIIVLMVAHRLSTV-LLSDRVALI 541
Cdd:COG1245  237 DEPSSYLDIYqrlnVARLIRE----LAEEGKYVLVVEHDLAILdYLADYVHIL 285

ABC_6TM_CyaB_HlyB_like

cd18588

Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...

22-283

6.20e-11

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: 63.67 E-value: 6.20e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  22 RELLAAVLVGVMI--ALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQ 99
Cdd:cd18588    1 KKLLGEVLLASLFlqLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 100 LLEKMFVLPFDFFHKNKTGELVSRlISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLVIM 179
Cdd:cd18588   81 LFRHLLRLPLSYFESRQVGDTVAR-VRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 180 FFNIMVEKRSKverEKFGELAGVTSNIIDNMKLIRIAMPFAWVMNF---FDRFQGDHIYAGKRFIKSIKIAGTLKTSING 256
Cdd:cd18588  160 LVTPILRRRLE---EKFQRGAENQSFLVETVTGIETVKSLAVEPQFqrrWEELLARYVKASFKTANLSNLASQIVQLIQK 236

                        250       260
                 ....*....|....*....|....*..
gi 493533268 257 LISFSLLAYGGYLVMKGEITVGILMTF 283
Cdd:cd18588  237 LTTLAILWFGAYLVMDGELTIGQLIAF 263

PRK11147

ABC transporter ATPase component; Reviewed

338-522

7.20e-11

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.97 E-value: 7.20e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVsnsallrpyIGFVEQT 417
Cdd:PRK11147   4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLI---------VARLQQD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PTLFEKCTLLENITLG------------------------RSISK-ASLENIFERTNLdvllRRFEN---------GL-- 461
Cdd:PRK11147  75 PPRNVEGTVYDFVAEGieeqaeylkryhdishlvetdpseKNLNElAKLQEQLDHHNL----WQLENrinevlaqlGLdp 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493533268 462 DTLVADiqLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRseGIIV 522
Cdd:PRK11147 151 DAALSS--LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ--GSII 207

GguA

NF040905

sugar ABC transporter ATP-binding protein;

349-548

1.45e-10

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.66 E-value: 1.45e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 349 NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQ--SGTIYINGDPVSNSALL-------------RPYIGF 413
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRniSGTVFKDGKEVDVSTVSdaidaglayvtedRKGYGL 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VeqtptlfekctLLENITlgRSISKASLENIFERTNLD-----VLLRRFENGLDTLVADI-----QLSGGERQLVALARA 483
Cdd:NF040905 352 N-----------LIDDIK--RNITLANLGKVSRRGVIDeneeiKVAEEYRKKMNIKTPSVfqkvgNLSGGNQQKVVLSKW 418

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 484 LVSNPRLLILDEITANID--SKTE--EIIQNtllgLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVA 548
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDvgAKYEiyTIINE----LAAEGKGVIVISSELPELLgMCDRIYVMNEGRITG 484

PRK15112

peptide ABC transporter ATP-binding protein SapF;

353-556

1.54e-10

peptide ABC transporter ATP-binding protein SapF;

Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.11 E-value: 1.54e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPV-------------------SNSALLRPYIGF 413
Cdd:PRK15112  29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysyrsqrirmifqdpSTSLNPRQRISQ 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 414 VEQTPtlfekctLLENITLGrsiSKASLENIFERTNLDVLLRRFENGLDTLVADiqlsgGERQLVALARALVSNPRLLIL 493
Cdd:PRK15112 109 ILDFP-------LRLNTDLE---PEQREKQIIETLRQVGLLPDHASYYPHMLAP-----GQKQRLGLARALILRPKVIIA 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 494 DEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELL 556
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKhISDQVLVMHQGEVVERGSTADVL 238

PRK10762

D-ribose transporter ATP binding protein; Provisional

353-546

1.89e-10

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.48 E-value: 1.89e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSAllrP---------YIGFVEQTPTLFEK 423
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS---PqdglangivYISEDRKRDGLVLG 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 424 CTLLENITLG--RSISKA--SLENIFERTNLDVLLRRFENGLDTLVADI-QLSGGERQLVALARALVSNPRLLILDEITA 498
Cdd:PRK10762 345 MSVKENMSLTalRYFSRAggSLKHADEQQAVSDFIRLFNIKTPSMEQAIgLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 493533268 499 NIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVL-LSDRVALISNGVI 546
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLgMSDRILVMHEGRI 473

PRK10261

glutathione transporter ATP-binding protein; Provisional

333-557

4.46e-10

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.57 E-value: 4.46e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 333 EDVRSISLENIAFGYGNKQI--LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKpQSGtiyinGDPVSNSALLR-- 408
Cdd:PRK10261  10 RDVLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLE-QAG-----GLVQCDKMLLRrr 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 409 --PYIGFVEQTPT------------LF-EKCTLL-----------ENITL----GRSISKASLENIFERTNL---DVLLR 455
Cdd:PRK10261  84 srQVIELSEQSAAqmrhvrgadmamIFqEPMTSLnpvftvgeqiaESIRLhqgaSREEAMVEAKRMLDQVRIpeaQTILS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 456 RFENgldtlvadiQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE-GIIVLMVAHRLSTVL- 533
Cdd:PRK10261 164 RYPH---------QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAe 234

                        250       260
                 ....*....|....*....|....
gi 493533268 534 LSDRVALISNGVIVASGTHNELLK 557
Cdd:PRK10261 235 IADRVLVMYQGEAVETGSVEQIFH 258

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

359-538

6.46e-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: 61.72 E-value: 6.46e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 359 ELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTI-----------YINGDpvsnsallrpYIGFVEQtptlfekctLL 427
Cdd:COG1245  362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlkisykpqYISPD----------YDGTVEE---------FL 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 428 ENITLGRSISKASLENIFERTNLDVLlrrfengLDTLVADiqLSGGERQLVALARALVSNPRLLILDEITANIDSktEE- 506
Cdd:COG1245  423 RSANTDDFGSSYYKTEIIKPLGLEKL-------LDKNVKD--LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQr 491

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 493533268 507 -----IIQNTllgLRSEGIIVLMVAHRLSTV-LLSDRV 538
Cdd:COG1245  492 lavakAIRRF---AENRGKTAMVVDHDIYLIdYISDRL 526

PRK11147

ABC transporter ATPase component; Reviewed

318-513

6.46e-10

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 6.46e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 318 LEAPEEERSN-----SSPKL---EDVRS----ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMG 385
Cdd:PRK11147 288 LKALRRERSErrevmGTAKMqveEASRSgkivFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLG 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 386 LQKPQSGTIYIngdpvsNSALLRPYigFVEQTPTLFEKCTLLENITLGRSiskaslenifertnlDVLLrrfeNGLDTLV 465
Cdd:PRK11147 368 QLQADSGRIHC------GTKLEVAY--FDQHRAELDPEKTVMDNLAEGKQ---------------EVMV----NGRPRHV 420

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493533268 466 AD-IQ---------------LSGGERQLVALARALVSNPRLLILDEITANIDSKT----EEII---QNTLL 513
Cdd:PRK11147 421 LGyLQdflfhpkramtpvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETlellEELLdsyQGTVL 491

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

321-495

9.39e-10

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.18 E-value: 9.39e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 321 PEEERSNSSPKL-EDVRSISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGlQKPQSgtiYingd 399
Cdd:PRK10938 243 PEPDEPSARHALpANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQG---Y---- 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 400 pvSNSALL--------------RPYIGFVEQTPTLFEK--CTLL--------ENITLGRSISKAslENIFERTNLDVLlr 455
Cdd:PRK10938 315 --SNDLTLfgrrrgsgetiwdiKKHIGYVSSSLHLDYRvsTSVRnvilsgffDSIGIYQAVSDR--QQKLAQQWLDIL-- 388

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 493533268 456 rfenGLDTLVADI---QLSGGERQLVALARALVSNPRLLILDE 495
Cdd:PRK10938 389 ----GIDKRTADApfhSLSWGQQRLALIVRALVKHPTLLILDE 427

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

360-538

1.34e-09

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 1.34e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 360 LRKGEITTLVGESGAGKTTTLNILMGLQKPQSGtiyINGDPVSNSALLRPYIGFVEQTptLFEKctLLEN-ITLGRS--- 435
Cdd:PRK13409  96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLG---DYEEEPSWDEVLKRFRGTELQN--YFKK--LYNGeIKVVHKpqy 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 436 ---ISKAS-------LENIFERTNLDVLLRRFenGLDTLV-ADI-QLSGGERQLVALARALVSNPRLLILDEITANIDsk 503
Cdd:PRK13409 169 vdlIPKVFkgkvrelLKKVDERGKLDEVVERL--GLENILdRDIsELSGGELQRVAIAAALLRDADFYFFDEPTSYLD-- 244

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 493533268 504 teeIIQ--NTLLGLR--SEGIIVLMVAHRLsTVL--LSDRV 538
Cdd:PRK13409 245 ---IRQrlNVARLIRelAEGKYVLVVEHDL-AVLdyLADNV 281

ABC_UvrA

cd03238

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...

353-550

1.48e-09

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: 57.33 E-value: 1.48e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 353 LKGLSLELRKGEITTLVGESGAGKTTTLNilmglqkpqsGTIYINGDPVSNSALLRPY---IGFVEQTPTLFEkcTLLEN 429
Cdd:cd03238   11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN----------EGLYASGKARLISFLPKFSrnkLIFIDQLQFLID--VGLGY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 430 ITLGRSISkaslenifertnldvllrrfengldtlvadiQLSGGERQLVALARALVSNPR--LLILDEITANIDSKTEEI 507
Cdd:cd03238   79 LTLGQKLS-------------------------------TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQ 127

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 493533268 508 IQNTLLGLRSEGIIVLMVAHRLSTVLLSDRV------ALISNGVIVASG 550
Cdd:cd03238  128 LLEVIKGLIDLGNTVILIEHNLDVLSSADWIidfgpgSGKSGGKVVFSG 176

ABC_6TM_ABCC_D1

cd18579

Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ...

25-300

1.61e-09

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

Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 59.04 E-value: 1.61e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  25 LAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDllvkyvLLVVGLWFGSLIFTYFGEVVFET--------TALMAKSDL 96
Cdd:cd18579    1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEP------LSEGYLLALALFLVSLLQSLLLHqyfflsfrLGMRVRSAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  97 RKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIaQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVfsfl 176
Cdd:cd18579   75 SSLIYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFF-LFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLL---- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 177 VIMFFNIMVEKRSKVEREKFGELA----GVTSNIIDNMKLIRIampFAWVMNFFDRFQGdhiyAGKRFIKSIKIAGTLKT 252
Cdd:cd18579  150 LLIPLQAFLAKLISKLRKKLMKATdervKLTNEILSGIKVIKL---YAWEKPFLKRIEE----LRKKELKALRKFGYLRA 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493533268 253 SINGLISF-----SLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQV 300
Cdd:cd18579  223 LNSFLFFStpvlvSLATFATYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQA 275

3a01203

TIGR00954

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...

338-530

1.79e-09

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: 60.53 E-value: 1.79e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  338 ISLENIAFGYGNKQIL-KGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYIngdPVSNSallrpyIGFVEQ 416
Cdd:TIGR00954 452 IKFENIPLVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---PAKGK------LFYVPQ 522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  417 TPtLFEKCTLLENIT--------LGRSISKASLENIFERTNLDVLLRRfENGLDTlVADIQ--LSGGERQLVALARALVS 486
Cdd:TIGR00954 523 RP-YMTLGTLRDQIIypdssedmKRRGLSDKDLEQILDNVQLTHILER-EGGWSA-VQDWMdvLSGGEKQRIAMARLFYH 599

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 493533268  487 NPRLLILDEITANIDSKTEEIIQNTllgLRSEGIIVLMVAHRLS 530
Cdd:TIGR00954 600 KPQFAILDECTSAVSVDVEGYMYRL---CREFGITLFSVSHRKS 640

ABC_6TM_TAP1

cd18589

Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...

74-300

2.62e-09

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: 58.64 E-value: 2.62e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  74 SLIFTYFGEVVFETTALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAIL 153
Cdd:cd18589   49 SAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLF 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 154 AIMFAFNWKLTLLPLGFIVFSFLVIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRiamPFAWVMNFFDRFQG-- 231
Cdd:cd18589  129 IFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVR---SFANEEGEAQRYRQrl 205

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 232 DHIYAGKRFIKSIKIAGTLKTSINGL-ISFSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQV 300
Cdd:cd18589  206 QKTYRLNKKEAAAYAVSMWTSSFSGLaLKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSY 275

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

349-562

3.74e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 3.74e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 349 NKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSN-SALLRPYIGFV----EQTPTlfek 423
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhNANEAINHGFAlvteERRST---- 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 424 ctlleNITLGRSISKASL-ENIFERTNLDVLLRRFENGLDT-LVADI-------------QLSGGERQLVALARALVSNP 488
Cdd:PRK10982 336 -----GIYAYLDIGFNSLiSNIRNYKNKVGLLDNSRMKSDTqWVIDSmrvktpghrtqigSLSGGNQQKVIIGRWLLTQP 410

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 489 RLLILDEITANIDSKTE-EIIQNTL-LGLRSEGIIvlMVAHRLSTVL-LSDRVALISNG-----VIVASGTHNELLKTSS 560
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKfEIYQLIAeLAKKDKGII--IISSEMPELLgITDRILVMSNGlvagiVDTKTTTQNEILRLAS 488


                 ..
gi 493533268 561 EY 562
Cdd:PRK10982 489 LH 490

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

359-501

4.20e-09

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 4.20e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 359 ELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTI-----------YINGDpvsnsallrpYIGFVEQtptlfekctLL 427
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelkisykpqYIKPD----------YDGTVED---------LL 421

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 428 ENIT--LGRSISKaslENIFERTNLDVLlrrfengLDTLVADiqLSGGERQLVALARALVSNPRLLILDEITANID 501
Cdd:PRK13409 422 RSITddLGSSYYK---SEIIKPLQLERL-------LDKNVKD--LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485

PLN03140

ABC transporter G family member; Provisional

351-530

6.55e-09

ABC transporter G family member; Provisional

Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.09 E-value: 6.55e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  351 QILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQ--SGTIYINGDPVSNSALLRpYIGFVEQTPTLFEKCTLLE 428
Cdd:PLN03140  894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETFAR-ISGYCEQNDIHSPQVTVRE 972

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  429 NIT------LGRSISKASLENIFERTNLDVLLRRFENGLDTLVADIQLSGGERQLVALARALVSNPRLLILDEITANIDS 502
Cdd:PLN03140  973 SLIysaflrLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052

                         170       180
                  ....*....|....*....|....*...
gi 493533268  503 KTEEIIQNTLLGLRSEGIIVLMVAHRLS 530
Cdd:PLN03140 1053 RAAAIVMRTVRNTVDTGRTVVCTIHQPS 1080

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

338-501

7.36e-09

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.60 E-value: 7.36e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSNSALLR---PYIGFV 414
Cdd:NF033858   2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRavcPRIAYM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 415 EQT------PTLfekcTLLENIT-------LGRSISKASLENIFERTNLDvllrRFengLDTLVAdiQLSGGERQLVALA 481
Cdd:NF033858  82 PQGlgknlyPTL----SVFENLDffgrlfgQDAAERRRRIDELLRATGLA----PF---ADRPAG--KLSGGMKQKLGLC 148

                        170       180
                 ....*....|....*....|
gi 493533268 482 RALVSNPRLLILDEITANID 501
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVD 168

PRK15064

ABC transporter ATP-binding protein; Provisional

340-394

1.07e-08

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 1.07e-08

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 340 LENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTI 394
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376

ABC_6TM_PrtD_LapB_HlyB_like

cd18783

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...

22-283

2.94e-08

Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 55.22 E-value: 2.94e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  22 RELLAAVLVGVMI--ALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGE--VVFETTALMAKsdLR 97
Cdd:cd18783    1 KRLFRDVAIASLIlhVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRylLLVATTRIDAR--LA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  98 KQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFpILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSFLV 177
Cdd:cd18783   79 LRTFDRLLSLPIDFFERTPAGVLTKHMQQIERIRQFLTGQLF-GTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 178 IMFF----NIMVEKRSKVEREKfGELAGVTSNIIDNMKL-----IRIAmpfAWvmnffDRFQGDHIYAGKRFIKSIKIAG 248
Cdd:cd18783  158 ILAFlppfRRRLQALYRAEGER-QAFLVETVHGIRTVKSlalepRQRR---EW-----DERVARAIRARFAVGRLSNWPQ 228

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 493533268 249 TLKTSINGLISFSLLAYGGYLVMKGEITVGILMTF 283
Cdd:cd18783  229 TLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAF 263

ABC_6TM_TAP2

cd18590

Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...

111-179

3.86e-08

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: 55.04 E-value: 3.86e-08

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493533268 111 FFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPlgFIVFSFLVIM 179
Cdd:cd18590   86 FFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLT--LIEMPLTAIA 152

ABC_6TM_ABCB8_like

cd18574

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...

96-290

6.67e-08

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: 54.47 E-value: 6.67e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  96 LRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWKLTLLPLGFIVFSF 175
Cdd:cd18574   77 LRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVV 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 176 LVIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRiampfAWVMNffDRfqgdhiyAGKRFIKSIKIAGTLKT--- 252
Cdd:cd18574  157 LVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVR-----AFAME--DR-------ELELYEEEVEKAAKLNEklg 222

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 493533268 253 ------------SINGLIsFSLLAYGGYLVMKGEITVGILMTFWAYVQSL 290
Cdd:cd18574  223 lgigifqglsnlALNGIV-LGVLYYGGSLVSRGELTAGDLMSFLVATQTI 271

AAA

smart00382

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...

362-547

7.92e-08

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.61 E-value: 7.92e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   362 KGEITTLVGESGAGKTTTLNILMG-LQKPQSGTIYINGDPVSNSALLRpyigfveqtptlfekctllenitlgrsiskas 440
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQ-------------------------------- 48

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268   441 lenifertnldvllrrfENGLDTLVADIQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQ-----NTLLGL 515
Cdd:smart00382  49 -----------------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLL 111

                          170       180       190
                   ....*....|....*....|....*....|..
gi 493533268   516 RSEGIIVLMVAHRLSTVLLSDRVALISNGVIV 547
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143

ABC_6TM_T1SS_like

cd18779

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ...

22-300

8.68e-08

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

Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 54.09 E-value: 8.68e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  22 RELLAAVLV--GVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVvglwfGSLIFTYFGEVVFETTALM-----AKS 94
Cdd:cd18779    1 PGLLGQILLasLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGL-----AALVLTQLLAGLLRSHLLLrlrtrLDT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  95 DLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITaILAIMFAFNWKLTLLPLGFIVFS 174
Cdd:cd18779   76 QLTLGFLEHLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSALLDGTLVLG-YLALLFAQSPLLGLVVLGLAALQ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 175 FLVIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNMKLIRiAMPFAWVMnfFDRFQGdhiyagkRFIKSIKIA---GTLK 251
Cdd:cd18779  155 VALLLATRRRVRELMARELAAQAEAQSYLVEALSGIETLK-ASGAEDRA--LDRWSN-------LFVDQLNASlrrGRLD 224

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493533268 252 TSINGLIS-------FSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLLMQV 300
Cdd:cd18779  225 ALVDALLAtlrlaapLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGT 280

dppD

PRK11022

dipeptide transporter ATP-binding subunit; Provisional

356-558

1.92e-07

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 53.21 E-value: 1.92e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 356 LSLELRKGEITTLVGESGAGKTTTLNILMGL----QKPQSGTIYING------DPVSNSALLRPYIGFVEQTP-TLFEKC 424
Cdd:PRK11022  26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGqdlqriSEKERRNLVGAEVAMIFQDPmTSLNPC 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 425 -----TLLENITLGRSISKASLEnifERTnLDVL----LRRFENGLDtlVADIQLSGGERQLVALARALVSNPRLLILDE 495
Cdd:PRK11022 106 ytvgfQIMEAIKVHQGGNKKTRR---QRA-IDLLnqvgIPDPASRLD--VYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 496 ITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAHRLSTVL-LSDRVALISNGVIVASGTHNELLKT 558
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAeAAHKIIVMYAGQVVETGKAHDIFRA 244

ABC_6TM_AarD_CydDC_like

cd18561

Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ...

76-210

2.64e-07

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

Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 52.28 E-value: 2.64e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  76 IFTYFGEVVFETTALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAI 155
Cdd:cd18561   51 ALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIY 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 156 MFAFNWKLTLLPLGFIVFSFLVIMFFNIMVEKRSkveREKFGELAGVTSNIIDNM 210
Cdd:cd18561  131 LFFLDPLVALILLVFALLIPLSPALWDRLAKDTG---RRHWAAYGRLSAQFLDSL 182

ycf16

CHL00131

sulfate ABC transporter protein; Validated

340-551

3.36e-07

sulfate ABC transporter protein; Validated

Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.57 E-value: 3.36e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 340 LENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQ--SGTIYING------DP----------- 400
Cdd:CHL00131  10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGesildlEPeerahlgifla 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 401 ---------VSNSALLR-------PYIGFVEQTPTLFekctlLENITlgRSISKASLENIFertnldvLLRRFENGldtl 464
Cdd:CHL00131  90 fqypieipgVSNADFLRlaynskrKFQGLPELDPLEF-----LEIIN--EKLKLVGMDPSF-------LSRNVNEG---- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 465 vadiqLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAH--RLSTVLLSDRVALIS 542
Cdd:CHL00131 152 -----FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqRLLDYIKPDYVHVMQ 226


                 ....*....
gi 493533268 543 NGVIVASGT 551
Cdd:CHL00131 227 NGKIIKTGD 235

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

420-560

5.97e-07

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: 52.71 E-value: 5.97e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  420 LFEKCTLLENITLG---RSISKASLENIFERTN--LDVllrrfenGLDTLV---ADIQLSGGERQLVALARALVSNPR-- 489
Cdd:TIGR00630 438 IREAHEFFNQLTLTpeeKKIAEEVLKEIRERLGflIDV-------GLDYLSlsrAAGTLSGGEAQRIRLATQIGSGLTgv 510

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268  490 LLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRV------ALISNGVIVASGTHNELLKTSS 560
Cdd:TIGR00630 511 LYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVidigpgAGEHGGEVVASGTPEEILANPD 587

ABC_6TM_AarD_CydD

cd18584

Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ...

24-161

6.02e-07

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

Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 51.26 E-value: 6.02e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALAVvfpLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLEK 103
Cdd:cd18584    3 LLGLLAALLIIAQAW---LLARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLAR 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 104 MFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNW 161
Cdd:cd18584   80 LLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDW 137

PRK15093

peptide ABC transporter ATP-binding protein SapD;

332-558

2.32e-06

peptide ABC transporter ATP-binding protein SapD;

Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.80 E-value: 2.32e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 332 LEDVRSISLENIAFGyGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPqsgTIYINGD------------ 399
Cdd:PRK15093   3 LLDIRNLTIEFKTSD-GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKD---NWRVTADrmrfddidllrl 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 400 -PVSNSALLRPYIGFVEQTPtlfEKCtLLENITLGRSISKA-----------SLENIFERTNLDVLLR-RFENGLDTLVA 466
Cdd:PRK15093  79 sPRERRKLVGHNVSMIFQEP---QSC-LDPSERVGRQLMQNipgwtykgrwwQRFGWRKRRAIELLHRvGIKDHKDAMRS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 467 -DIQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGL-RSEGIIVLMVAHRLSTV-LLSDRVALISN 543
Cdd:PRK15093 155 fPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLsQWADKINVLYC 234

                        250
                 ....*....|....*
gi 493533268 544 GVIVASGTHNELLKT 558
Cdd:PRK15093 235 GQTVETAPSKELVTT 249

40850658_otr

NF000106

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

347-555

3.62e-06

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.35 E-value: 3.62e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 347 YGNKQILKGLSLELRKGEITTLVGESGAGKTTTLnILMGLQKPQSGT-IYINGDPVSNSALLRPYIGFveQTPtlfekct 425
Cdd:NF000106  23 FGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRrPWRF*TWCANRRALRRTIG*--HRP------- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 426 llenITLGRSISKASLENIF------------ERTNLDVLLRRFENGLDTLVADIQLSGGERQLVALARALVSNPRLLIL 493
Cdd:NF000106  93 ----VR*GRRESFSGRENLYmigr*ldlsrkdARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493533268 494 DEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV-LLSDRVALISNGVIVASGTHNEL 555
Cdd:NF000106 169 DEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVIDRGRVIADGKVDEL 231

PLN03073

ABC transporter F family; Provisional

335-501

4.61e-06

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 4.61e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 335 VRSISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNiLMGLQK----PQSGTIY-----INGDPVS--- 402
Cdd:PLN03073 175 IKDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLR-YMAMHAidgiPKNCQILhveqeVVGDDTTalq 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 403 --------NSALLRPYIGFVEQ-----TPTLFEKCTLLENITLGRSISKASLENIFERTNL---DVLLRRFENGLDTL-- 464
Cdd:PLN03073 254 cvlntdieRTQLLEEEAQLVAQqreleFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELidaYTAEARAASILAGLsf 333

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 493533268 465 VADIQL------SGGERQLVALARALVSNPRLLILDEITANID 501
Cdd:PLN03073 334 TPEMQVkatktfSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376

sufC

PRK09580

cysteine desulfurase ATPase component; Reviewed

338-552

4.72e-06

cysteine desulfurase ATPase component; Reviewed

Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 4.72e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQ--SGTIYING------DP--------- 400
Cdd:PRK09580   2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGkdllelSPedragegif 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 401 -----------VSNSALLRPYIGFV----EQTP-TLFEKCTLLENitlgrsisKASLENIFErtnlDVLLRRFENGldtl 464
Cdd:PRK09580  82 mafqypveipgVSNQFFLQTALNAVrsyrGQEPlDRFDFQDLMEE--------KIALLKMPE----DLLTRSVNVG---- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 465 vadiqLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAH--RLSTVLLSDRVALIS 542
Cdd:PRK09580 146 -----FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHyqRILDYIKPDYVHVLY 220

                        250
                 ....*....|
gi 493533268 543 NGVIVASGTH 552
Cdd:PRK09580 221 QGRIVKSGDF 230

ABC_6TM_ATM1_ABCB7

cd18582

Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...

26-297

5.72e-06

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

Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 48.26 E-value: 5.72e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  26 AAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVV--GLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLEK 103
Cdd:cd18582    1 ALLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVPLLLLLAygLARILSSLFNELRDALFARVSQRAVRRLALRVFRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 104 MFVLPFDFFHKNKTGEL---VSRLISDLE-LVGTVIAQVFPILLlgvvQITAILAIMFA-FNWKLTLLplgfIVFSFLVI 178
Cdd:cd18582   81 LHSLSLRFHLSRKTGALsraIERGTRGIEfLLRFLLFNILPTIL----ELLLVCGILWYlYGWSYALI----TLVTVALY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 179 MFFNIMV-EKRSKVEREKFGELAGVTSNIIDnmkliriampfaWVMNF---------------FDRFQGDhiYAgKRFIK 242
Cdd:cd18582  153 VAFTIKVtEWRTKFRREMNEADNEANAKAVD------------SLLNYetvkyfnneeyeaerYDKALAK--YE-KAAVK 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 243 SIKIAGTLKTSINGLIS---FSLLAYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLL 297
Cdd:cd18582  218 SQTSLALLNIGQALIISlglTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFL 275

ABCG_PDR_domain1

cd03233

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...

346-509

5.85e-06

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: 47.26 E-value: 5.85e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 346 GYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKpqsGTIYINGDPVSNSallRPYIGFVEQTPtlfekct 425
Cdd:cd03233   16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSVEGDIHYNG---IPYKEFAEKYP------- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 426 llenitlgRSISKASLENIF------ERTnLDVLLR----RFENGldtlvadiqLSGGERQLVALARALVSNPRLLILDE 495
Cdd:cd03233   83 --------GEIIYVSEEDVHfptltvRET-LDFALRckgnEFVRG---------ISGGERKRVSIAEALVSRASVLCWDN 144

                        170
                 ....*....|....*
gi 493533268 496 ITANIDSKTE-EIIQ 509
Cdd:cd03233  145 STRGLDSSTAlEILK 159

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

451-559

7.68e-06

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 7.68e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 451 DVLLRRFengldtlvadIQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLS 530
Cdd:PRK10938 127 ALLDRRF----------KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFD 196

                         90       100       110
                 ....*....|....*....|....*....|
gi 493533268 531 TV-LLSDRVALISNGVIVASGTHNELLKTS 559
Cdd:PRK10938 197 EIpDFVQFAGVLADCTLAETGEREEILQQA 226

ABC_Class2

cd03227

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...

464-539

1.03e-05

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: 45.81 E-value: 1.03e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 464 LVADIQLSGGERQLVALARALVS---NPR-LLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRVA 539
Cdd:cd03227   72 IFTRLQLSGGEKELSALALILALaslKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLI 151

PRK10636

putative ABC transporter ATP-binding protein; Provisional

338-394

1.61e-05

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 1.61e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTI 394
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369

ABC_6TM_ABCC_D2

cd18580

Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...

24-181

2.16e-05

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

Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 46.73 E-value: 2.16e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALAVVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLEK 103
Cdd:cd18580    2 LLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRS 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493533268 104 MFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAIMFAFNWkLTLLPLGFIVFSFLVIMFF 181
Cdd:cd18580   82 VLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP-YFLIVLPPLLVVYYLLQRY 158

ABC_UvrA_I

cd03270

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...

353-550

4.56e-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: 44.94 E-value: 4.56e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 353 LKGLSLELRKGEITTLVGESGAGKTTtLNIlmglqkpqsGTIYING-----DPVSNSA------LLRPYIGFVEQ-TPTL 420
Cdd:cd03270   11 LKNVDVDIPRNKLVVITGVSGSGKSS-LAF---------DTIYAEGqrryvESLSAYArqflgqMDKPDVDSIEGlSPAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 421 fekctLLENITLGRSiSKASLENIFE--------------RTNLDVLLrrfENGLDTLVADIQ---LSGGERQLVALARA 483
Cdd:cd03270   81 -----AIDQKTTSRN-PRSTVGTVTEiydylrllfarvgiRERLGFLV---DVGLGYLTLSRSaptLSGGEAQRIRLATQ 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268 484 LVSNPR--LLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRV------ALISNGVIVASG 550
Cdd:cd03270  152 IGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVidigpgAGVHGGEIVAQG 226

ABC_6TM_HMT1

cd18583

Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ...

107-297

1.75e-04

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

Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 43.67 E-value: 1.75e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 107 LPFDFFHKNKTGELVSRL-----ISDLelVGTVIAQVFPILL-LGVvqitAILAIMFAFNWKLTLLplgFIVFSFLVIMF 180
Cdd:cd18583   83 LSMDFHDSKKSGEVLKAIeqgssINDL--LEQILFQIVPMIIdLVI----AIVYLYYLFDPYMGLI---VAVVMVLYVWS 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 181 FNIMVEKRSKVER---EKFGELAGVTSNIIDNmkliriampfaW--VMNF------FDRFQG---DHIYAGKRFIKSIKI 246
Cdd:cd18583  154 TIKLTSWRTKLRRdmiDADREERSILTESLLN-----------WetVKYFnrepyeKERYREavkNYQKAERKYLFSLNL 222

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493533268 247 AGTLKTSIN--GLISFSLLAYggYLVMKGEITVGILMTFWAYVQSLFNPIQLL 297
Cdd:cd18583  223 LNAVQSLILtlGLLAGCFLAA--YQVSQGQATVGDFVTLLTYWAQLSGPLNFF 273

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

265-555

1.85e-04

Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 1.85e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  265 YGGYLVMKGeitvgilmtfwayvqslfNPIQLLMQVNILLRQSWGGLlRTIEVleaPEEERSNSSPKLEDVRSislenia 344
Cdd:TIGR00630 569 HGGEVVASG------------------TPEEILANPDSLTGQYLSGR-KKIEV---PAERRPGNGKFLTLKGA------- 619

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  345 fgygNKQILKGLSLELRKGEITTLVGESGAGKTTTLN----------ILMGLQKPQSGT-----------IYINGDPV-- 401
Cdd:TIGR00630 620 ----RENNLKNITVSIPLGLFTCITGVSGSGKSTLINdtlypalanrLNGAKTVPGRYTsieglehldkvIHIDQSPIgr 695

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  402 ---SNSAllrPYIGFVEQTPTLF-------------------------EKCTLLENIT----------------LGRSIS 437
Cdd:TIGR00630 696 tprSNPA---TYTGVFDEIRELFaetpeakvrgytpgrfsfnvkggrcEACQGDGVIKiemhflpdvyvpcevcKGKRYN 772

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  438 KASLE------NIFERTNLDVLLRR--FEN------GLDTLVaDI------------QLSGGERQLVALARAL---VSNP 488
Cdd:TIGR00630 773 RETLEvkykgkNIADVLDMTVEEAYefFEAvpsisrKLQTLC-DVglgyirlgqpatTLSGGEAQRIKLAKELskrSTGR 851

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493533268  489 RLLILDEITANIdsKTEEIIQ--NTLLGLRSEGIIVLMVAHRLSTVLLSDRVALI------SNGVIVASGTHNEL 555
Cdd:TIGR00630 852 TLYILDEPTTGL--HFDDIKKllEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924

ABC_RNaseL_inhibitor

cd03222

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...

359-538

3.45e-04

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: 41.79 E-value: 3.45e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 359 ELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYINGDPVSnsalLRPyigfveqtptlfekctllenitlgrsisk 438
Cdd:cd03222   21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV----YKP----------------------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 439 aslenifertnldvllrrfengldtlvADIQLSGGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSE 518
Cdd:cd03222   68 ---------------------------QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120

                        170       180
                 ....*....|....*....|..
gi 493533268 519 GI-IVLMVAHRLSTV-LLSDRV 538
Cdd:cd03222  121 GKkTALVVEHDLAVLdYLSDRI 142

ABC_6TM_peptidase_like

cd18571

Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ...

24-281

4.05e-04

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

Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 42.43 E-value: 4.05e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  24 LLAAVLVGVMIALavVFPLLIRLLIDVVIPSGDMDLLVKYVLLVVGLWFGSLIFTYF-GEVVFETTALMAKSdLRKQLLE 102
Cdd:cd18571    7 LLLGLLLGSLLQL--IFPFLTQSIVDKGINNKDLNFIYLILIAQLVLFLGSTSIEFIrSWILLHISSRINIS-IISDFLI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 103 KMFVLPFDFFHKNKTGELVSRlISDLE-----LVGTVIAQVFPILLLGVVQItailaIMFAFNWKLTLLPLGFIVFSFLV 177
Cdd:cd18571   84 KLMRLPISFFDTKMTGDILQR-INDHSriesfLTSSSLSILFSLLNLIVFSI-----VLAYYNLTIFLIFLIGSVLYILW 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 178 IMFFnimVEKRSKVEREKFGELAGVTSN---IIDNMKLIRIAmpfawvmNF--FDRFQGDHIYAG--KRFIKSIKI---- 246
Cdd:cd18571  158 ILLF---LKKRKKLDYKRFDLSSENQSKlieLINGMQEIKLN-------NSerQKRWEWERIQAKlfKINIKSLKLdqyq 227

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 493533268 247 -AGTlkTSINGLISFSLLAYGGYLVMKGEITVGILM 281
Cdd:cd18571  228 qIGA--LFINQLKNILITFLAAKLVIDGEITLGMML 261

ABC_6TM_ATM1_ABCB7_HMT1_ABCB6

cd18560

Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ...

28-297

4.72e-04

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

Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 42.21 E-value: 4.72e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  28 VLVGVMIALAVVFPLLIRLLID--VVIPSGDMDLLVKYVLLVVGLWFGSLIFTYFGEVVFETTALMAKSDLRKQLLEKMF 105
Cdd:cd18560    3 LLLILGKACNVLAPLFLGRAVNalTLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 106 VLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILAI-MFAFNWkltllPLGFIVFSFLVIMF-FNI 183
Cdd:cd18560   83 SLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVfAFHFGA-----WLALIVFLSVLLYGvFTI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 184 MVEKRskveREKFGELAgvtsNIIDNMKLIRIA---MPFAWVMNFfdrfqGDHIYAGKRFIKSIKIagTLKTSINGLISF 260
Cdd:cd18560  158 KVTEW----RTKFRRAA----NKKDNEAHDIAVdslLNFETVKYF-----TNEKYEVDRYGEAVKE--YQKSSVKVQASL 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493533268 261 SLL----------------AYGGYLVMKGEITVGILMTFWAYVQSLFNPIQLL 297
Cdd:cd18560  223 SLLnvgqqliiqlgltlglLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFL 275

PRK15064

ABC transporter ATP-binding protein; Provisional

338-532

5.60e-04

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 5.60e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 338 ISLENIAFGYGNKQILKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYIngDPvsNSALlrpyiGFVEQT 417
Cdd:PRK15064   2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL--DP--NERL-----GKLRQD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 418 PTLFEKCTLLENITLGRS-----------------------ISKASLENIF--------ERTNLDVLL-----RRFENGL 461
Cdd:PRK15064  73 QFAFEEFTVLDTVIMGHTelwevkqerdriyalpemseedgMKVADLEVKFaemdgytaEARAGELLLgvgipEEQHYGL 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493533268 462 DTLVADiqlsgGERQLVALARALVSNPRLLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTV 532
Cdd:PRK15064 153 MSEVAP-----GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSV 218

ABC_6TM_MRP5_8_9_D2

cd18599

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ...

75-180

6.31e-04

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

Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 42.16 E-value: 6.31e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  75 LIFTYFGEVVFETTALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAILA 154
Cdd:cd18599   72 LLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLI 151

                         90       100
                 ....*....|....*....|....*..
gi 493533268 155 -IMFAFNWKLTLLPLGFIVFSFLVIMF 180
Cdd:cd18599  152 iIAIVFPWFLIALIPLAIIFVFLSKIF 178

PRK00635

excinuclease ABC subunit A; Provisional

470-560

7.02e-04

excinuclease ABC subunit A; Provisional

Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 7.02e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  470 LSGGERQLVALARALVSNPR--LLILDEITANIDSKTEEIIQNTLLGLRSEGIIVLMVAHRLSTVLLSDRV------ALI 541
Cdd:PRK00635  477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIidigpgAGI 556

                          90
                  ....*....|....*....
gi 493533268  542 SNGVIVASGTHNELLKTSS 560
Cdd:PRK00635  557 FGGEVLFNGSPREFLAKSD 575

tagH

PRK13545

teichoic acids export protein ATP-binding subunit; Provisional

353-398

8.24e-04

teichoic acids export protein ATP-binding subunit; Provisional

Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.18 E-value: 8.24e-04

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 493533268 353 LKGLSLELRKGEITTLVGESGAGKTTTLNILMGLQKPQSGTIYING 398
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85

ABC_Rad50

cd03240

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...

335-522

1.06e-03

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: 40.67 E-value: 1.06e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 335 VRSISLENIAFGYGNKQIlkglslELRKGeITTLVGESGAGKTTTLN-ILMGL--QKPQSGTIYINGDPVSNSALLRpyi 411
Cdd:cd03240    1 IDKLSIRNIRSFHERSEI------EFFSP-LTLIVGQNGAGKTTIIEaLKYALtgELPPNSKGGAHDPKLIREGEVR--- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 412 GFVEQTPTLFEKctllENITLGRSIskasleNIFERTnldVLLRRFEngLDTLVADI--QLSGGERQLV------ALARA 483
Cdd:cd03240   71 AQVKLAFENANG----KKYTITRSL------AILENV---IFCHQGE--SNWPLLDMrgRCSGGEKVLAsliirlALAET 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 493533268 484 LVSNPRLLILDEITANIDS-----KTEEIIQNTLLGLRSEGIIV 522
Cdd:cd03240  136 FGSNCGILALDEPTTNLDEenieeSLAEIIEERKSQKNFQLIVI 179

ABC_6TM_Pgp_ABCB1

cd18558

Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...

73-282

2.09e-03

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: 40.34 E-value: 2.09e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  73 GSLIFTYFGEVVFETTALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITAI 152
Cdd:cd18558   71 IVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268 153 LAIMFAFNWKLTLLPLGFIVFSFLVIMFFNIMVEKRSKVEREKFGELAGVTSNIIDNmklIRIAMPFAWVMNFFDRFQGD 232
Cdd:cd18558  151 FIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEA---FRTVIAFGGQQKEETRYAQN 227

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493533268 233 HIYAGKRFIKSIKIAGTLKTSINGLISFSLLA---YGGYLVMKGEITVGILMT 282
Cdd:cd18558  228 LEIAKRNGIKKAITFNISMGAAFLLIYASYALafwYGTYLVTQQEYSIGEVLT 280

AAA_22

pfam13401

AAA domain;

365-431

4.24e-03

AAA domain;

Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 37.71 E-value: 4.24e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  365 ITTLVGESGAGKTTTL-NILMGLQKPQSGTIYINGDPVSNSALLRPYI--GFVEQTPTLFEKCTLLENIT 431
Cdd:pfam13401   7 ILVLTGESGTGKTTLLrRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALlrALGLPLSGRLSKEELLAALQ 76

ABC_6TM_VMR1_D2_like

cd18604

Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...

72-178

6.32e-03

Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.

Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 38.99 E-value: 6.32e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  72 FGSLIFTYFGEVVFETTALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITA 151
Cdd:cd18604   54 LLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLV 133

                         90       100
                 ....*....|....*....|....*..
gi 493533268 152 ILAIMFAFNWkLTLLPLGFIVFSFLVI 178
Cdd:cd18604  134 ILIAIVVVSP-AFLLPAVVLAALYVYI 159

ABC_6TM_MRP1_2_3_6_D2_like

cd18603

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ...

72-181

7.21e-03

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).

Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 38.61 E-value: 7.21e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493533268  72 FGSLIFTYFGEVVFETTALMAKSDLRKQLLEKMFVLPFDFFHKNKTGELVSRLISDLELVGTVIAQVFPILLLGVVQITA 151
Cdd:cd18603   52 LGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVIS 131

                         90       100       110
                 ....*....|....*....|....*....|..
gi 493533268 152 IL-AIMFAFNWKLT-LLPLGFIvfsFLVIMFF 181
Cdd:cd18603  132 TLvVISISTPIFLVvIIPLAIL---YFFIQRF 160

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