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Conserved domains on  [gi|60218875|ref|NP_036124|]
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ATP-binding cassette sub-family D member 2 isoform 1 [Mus musculus]

Protein Classification

ABC transporter D family protein( domain architecture ID 1002808)

ABC transporter D (ABCD) family protein, similar to human ABCD2, an ATP-dependent ABC transporter involved in the transport of very long chain fatty acid (VLCFA)-CoA from the cytosol to the peroxisome lumen

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
3a01203 super family cl36779
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
74-686 0e+00

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


The actual alignment was detected with superfamily member TIGR00954:

Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 825.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875    74 KKPAPGLNAAFFKQLLELRKILFPKLVTTETGWLCLHSVALISRTFLSIYVAGLDGKIVKSIVEKKPRTFIIKLIKWLMI 153
Cdd:TIGR00954  65 AKKKAHVNGVFLGKLDFLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLI 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   154 AIPATFVNSAIRYLECKLALAFRTRLVDHAYETYFANQTYYKVINMDGRLANPDQSLTEDIMMFSQSVAHLYSNLTKPIL 233
Cdd:TIGR00954 145 APPASFINSAIKYLLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPIL 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   234 DVILTSYTLIRTATSRGASPIGPTllaglvVYATAKVLKACSPKFGSLVAEEAHRKGYLRYVHSRIIANVEEIAFYRGHK 313
Cdd:TIGR00954 225 DVILYSFKLLTALGSVGPAGLFAY------LFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNK 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   314 VEMKQLQKCYKALAYQMNLILSKRLWYIMIEQFLMKYVWSSCGLIMVAIPIITATGFADGDLEDgpKQAMvsdrtEAFTT 393
Cdd:TIGR00954 299 VEKETVMSSFYRLVEHLNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKTHPAFLEMSE--EELM-----QEFYN 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   394 ARNLLASGADAIERIMSSYKEITELAGYTARVYNMFWVFDEVKRGIYKRTVTQEPENHSKRGGNLELplsdtLAIKGTVI 473
Cdd:TIGR00954 372 NGRLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNSNL-----VPGRGIVE 446
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   474 DVDHGIICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYM 553
Cdd:TIGR00954 447 YQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYM 526
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   554 SLGSLRDQVIYPDSADDMREKGYTDQDLERILHSVHLYHIVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALL 633
Cdd:TIGR00954 527 TLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAIL 606
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|...
gi 60218875   634 DECTSAVSIDVEGKIFQAAIGAGISLLSITHRPSLWKYHTHLLQFDGEGGWRF 686
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
 
Name Accession Description Interval E-value
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
74-686 0e+00

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: 825.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875    74 KKPAPGLNAAFFKQLLELRKILFPKLVTTETGWLCLHSVALISRTFLSIYVAGLDGKIVKSIVEKKPRTFIIKLIKWLMI 153
Cdd:TIGR00954  65 AKKKAHVNGVFLGKLDFLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLI 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   154 AIPATFVNSAIRYLECKLALAFRTRLVDHAYETYFANQTYYKVINMDGRLANPDQSLTEDIMMFSQSVAHLYSNLTKPIL 233
Cdd:TIGR00954 145 APPASFINSAIKYLLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPIL 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   234 DVILTSYTLIRTATSRGASPIGPTllaglvVYATAKVLKACSPKFGSLVAEEAHRKGYLRYVHSRIIANVEEIAFYRGHK 313
Cdd:TIGR00954 225 DVILYSFKLLTALGSVGPAGLFAY------LFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNK 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   314 VEMKQLQKCYKALAYQMNLILSKRLWYIMIEQFLMKYVWSSCGLIMVAIPIITATGFADGDLEDgpKQAMvsdrtEAFTT 393
Cdd:TIGR00954 299 VEKETVMSSFYRLVEHLNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKTHPAFLEMSE--EELM-----QEFYN 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   394 ARNLLASGADAIERIMSSYKEITELAGYTARVYNMFWVFDEVKRGIYKRTVTQEPENHSKRGGNLELplsdtLAIKGTVI 473
Cdd:TIGR00954 372 NGRLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNSNL-----VPGRGIVE 446
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   474 DVDHGIICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYM 553
Cdd:TIGR00954 447 YQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYM 526
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   554 SLGSLRDQVIYPDSADDMREKGYTDQDLERILHSVHLYHIVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALL 633
Cdd:TIGR00954 527 TLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAIL 606
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|...
gi 60218875   634 DECTSAVSIDVEGKIFQAAIGAGISLLSITHRPSLWKYHTHLLQFDGEGGWRF 686
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
ABC_membrane_2 pfam06472
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ...
91-365 4.35e-127

ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family of ABC transporters and shares sequence similarity with pfam00664. Mutations in this domain in Swiss:P28288 are believed responsible for Zellweger Syndrome-2; mutations in Swiss:P33897 are responsible for recessive X-linked adrenoleukodystrophy. A Saccharomyces cerevisiae homolog is involved in the import of long-chain fatty acids.


Pssm-ID: 399466  Cd Length: 269  Bit Score: 378.88  E-value: 4.35e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875    91 LRKILFPKLVTTETGWLCLHSVALISRTFLSIYVAGLDGKIVKSIVEKKPRTFIIKLIKWLMIAIPATFVNSAIRYLECK 170
Cdd:pfam06472   1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   171 LALAFRTRLVDHAYETYFANQTYYKVINMDGRLANPDQSLTEDIMMFSQSVAHLYSNLTKPILDVILTSYTLIRTATSRG 250
Cdd:pfam06472  81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   251 aspigpTLLAGLVVYATAKVLKACSPKFGSLVAEEAHRKGYLRYVHSRIIANVEEIAFYRGHKVEMKQLQKCYKALAYQM 330
Cdd:pfam06472 161 ------PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHM 234
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 60218875   331 NLILSKRLWYIMIEQFLMKYVWSSCGLIMVAIPII 365
Cdd:pfam06472 235 RRILRRRLWYGFIEDFVLKYTWSILGYVLVALPIF 269
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
134-691 8.62e-90

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 292.48  E-value: 8.62e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 134 SIVEKKPRTFIIKLIKWLMIAIPATFVNSAIRYLECKLALAFRTRLVDHAYETYFANQTYYKVINMDGRLANPDQSLTED 213
Cdd:COG4178  54 ALQARDAAAFWQQLGVFALLAAISILLAVYQTYLRQRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAED 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 214 IMMFSQSVAHLYSNLTKPILDVIltSYTLI-------RTATSRGASPIGPTLLA-GLVVYATakvlkacspkFGSLVA-- 283
Cdd:COG4178 134 IRLFTETTLSLSLGLLSSVVTLI--SFIGIlwslsgsLTFTLGGYSITIPGYMVwAALIYAI----------IGTLLThl 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 284 ----------EEAHRKGYLRY--VHSRiiANVEEIAFYRGHKVEMKQLQKCYKALAYQMNLILSKRLWYIMIEQFlmkYv 351
Cdd:COG4178 202 igrplirlnfEQQRREADFRFalVRVR--ENAESIALYRGEAAERRRLRRRFDAVIANWRRLIRRQRNLTFFTTG---Y- 275
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 352 wsscGLIMVAIPI-ITATGFADGDLEDGpkqamvsdrteAFTTARNLLASGADAIERIMSSYKEITELAGYTARVYNMFW 430
Cdd:COG4178 276 ----GQLAVIFPIlVAAPRYFAGEITLG-----------GLMQAASAFGQVQGALSWFVDNYQSLAEWRATVDRLAGFEE 340
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 431 VFDEVKRgiykrtvtqEPENHSkrggnlelplsdtlaikGTVIDVDHGIICENVPIITPAGEVVASRLNFKVEEGMHLLI 510
Cdd:COG4178 341 ALEAADA---------LPEAAS-----------------RIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLI 394
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 511 TGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYMSLGSLRDQVIYPDSADDmrekgYTDQDLERILHSVHL 590
Cdd:COG4178 395 TGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGTLREALLYPATAEA-----FSDAELREALEAVGL 469
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 591 YHIVQReggWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPSL 668
Cdd:COG4178 470 GHLAER---LDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLlrEELPGTTVISVGHRSTL 546
                       570       580
                ....*....|....*....|...
gi 60218875 669 WKYHTHLLQFDGEGGWRFEQLDT 691
Cdd:COG4178 547 AAFHDRVLELTGDGSWQLLPAEA 569
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
479-684 2.95e-82

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: 258.62  E-value: 2.95e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 479 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYMSLGSL 558
Cdd:cd03223   1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 559 RDQVIYPdsaddmrekgytdqdlerilhsvhlyhivqreggwdavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDECTS 638
Cdd:cd03223  81 REQLIYP----------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 60218875 639 AVSIDVEGKIFQAAIGAGISLLSITHRPSLWKYHTHLLQFDGEGGW 684
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
491-666 3.89e-15

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 74.91  E-value: 3.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQHmfyipqrpymsLGSLRDQVIYPDSAD 569
Cdd:PRK13539  14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtIKLDGGDID-----------DPDVAEACHYLGHRN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  570 DMRE--------------KGYTDQDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMAR-MFYHKPKYaLLD 634
Cdd:PRK13539  83 AMKPaltvaenlefwaafLGGEELDIAAALEAVGLAPLAHLPFG---------YLSAGQKRRVALARlLVSNRPIW-ILD 152
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 60218875  635 ECTSAvsIDVEG-KIFQAAI-----GAGISLLSiTHRP 666
Cdd:PRK13539 153 EPTAA--LDAAAvALFAELIrahlaQGGIVIAA-THIP 187
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
490-676 3.50e-08

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 54.16  E-value: 3.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  490 AGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQR-------PY-----MSLGS 557
Cdd:NF040873   3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRsevpdslPLtvrdlVAMGR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  558 LRDQVIY-PDSADDMREkgyTDQDLERilhsVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHKPKYALLDEC 636
Cdd:NF040873  83 WARRGLWrRLTRDDRAA---VDDALER----VGLADLAGRQ---------LGELSGGQRQRALLAQGLAQEADLLLLDEP 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 60218875  637 TSAVSIDVEGKIFQ---AAIGAGISLLSITHRPSLWKYHTHLL 676
Cdd:NF040873 147 TTGLDAESRERIIAllaEEHARGATVVVVTHDLELVRRADPCV 189
GguA NF040905
sugar ABC transporter ATP-binding protein;
496-534 3.03e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.93  E-value: 3.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 60218875  496 SRLNFKVEEG-MHLLItGPNGCGKSSLFRILSGLWP--VYEG 534
Cdd:NF040905  18 DDVNLSVREGeIHALC-GENGAGKSTLMKVLSGVYPhgSYEG 58
 
Name Accession Description Interval E-value
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
74-686 0e+00

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: 825.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875    74 KKPAPGLNAAFFKQLLELRKILFPKLVTTETGWLCLHSVALISRTFLSIYVAGLDGKIVKSIVEKKPRTFIIKLIKWLMI 153
Cdd:TIGR00954  65 AKKKAHVNGVFLGKLDFLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLI 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   154 AIPATFVNSAIRYLECKLALAFRTRLVDHAYETYFANQTYYKVINMDGRLANPDQSLTEDIMMFSQSVAHLYSNLTKPIL 233
Cdd:TIGR00954 145 APPASFINSAIKYLLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPIL 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   234 DVILTSYTLIRTATSRGASPIGPTllaglvVYATAKVLKACSPKFGSLVAEEAHRKGYLRYVHSRIIANVEEIAFYRGHK 313
Cdd:TIGR00954 225 DVILYSFKLLTALGSVGPAGLFAY------LFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNK 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   314 VEMKQLQKCYKALAYQMNLILSKRLWYIMIEQFLMKYVWSSCGLIMVAIPIITATGFADGDLEDgpKQAMvsdrtEAFTT 393
Cdd:TIGR00954 299 VEKETVMSSFYRLVEHLNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKTHPAFLEMSE--EELM-----QEFYN 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   394 ARNLLASGADAIERIMSSYKEITELAGYTARVYNMFWVFDEVKRGIYKRTVTQEPENHSKRGGNLELplsdtLAIKGTVI 473
Cdd:TIGR00954 372 NGRLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNSNL-----VPGRGIVE 446
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   474 DVDHGIICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYM 553
Cdd:TIGR00954 447 YQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYM 526
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   554 SLGSLRDQVIYPDSADDMREKGYTDQDLERILHSVHLYHIVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALL 633
Cdd:TIGR00954 527 TLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAIL 606
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|...
gi 60218875   634 DECTSAVSIDVEGKIFQAAIGAGISLLSITHRPSLWKYHTHLLQFDGEGGWRF 686
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
ABC_membrane_2 pfam06472
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ...
91-365 4.35e-127

ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family of ABC transporters and shares sequence similarity with pfam00664. Mutations in this domain in Swiss:P28288 are believed responsible for Zellweger Syndrome-2; mutations in Swiss:P33897 are responsible for recessive X-linked adrenoleukodystrophy. A Saccharomyces cerevisiae homolog is involved in the import of long-chain fatty acids.


Pssm-ID: 399466  Cd Length: 269  Bit Score: 378.88  E-value: 4.35e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875    91 LRKILFPKLVTTETGWLCLHSVALISRTFLSIYVAGLDGKIVKSIVEKKPRTFIIKLIKWLMIAIPATFVNSAIRYLECK 170
Cdd:pfam06472   1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   171 LALAFRTRLVDHAYETYFANQTYYKVINMDGRLANPDQSLTEDIMMFSQSVAHLYSNLTKPILDVILTSYTLIRTATSRG 250
Cdd:pfam06472  81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   251 aspigpTLLAGLVVYATAKVLKACSPKFGSLVAEEAHRKGYLRYVHSRIIANVEEIAFYRGHKVEMKQLQKCYKALAYQM 330
Cdd:pfam06472 161 ------PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHM 234
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 60218875   331 NLILSKRLWYIMIEQFLMKYVWSSCGLIMVAIPII 365
Cdd:pfam06472 235 RRILRRRLWYGFIEDFVLKYTWSILGYVLVALPIF 269
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
134-691 8.62e-90

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 292.48  E-value: 8.62e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 134 SIVEKKPRTFIIKLIKWLMIAIPATFVNSAIRYLECKLALAFRTRLVDHAYETYFANQTYYKVINMDGRLANPDQSLTED 213
Cdd:COG4178  54 ALQARDAAAFWQQLGVFALLAAISILLAVYQTYLRQRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAED 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 214 IMMFSQSVAHLYSNLTKPILDVIltSYTLI-------RTATSRGASPIGPTLLA-GLVVYATakvlkacspkFGSLVA-- 283
Cdd:COG4178 134 IRLFTETTLSLSLGLLSSVVTLI--SFIGIlwslsgsLTFTLGGYSITIPGYMVwAALIYAI----------IGTLLThl 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 284 ----------EEAHRKGYLRY--VHSRiiANVEEIAFYRGHKVEMKQLQKCYKALAYQMNLILSKRLWYIMIEQFlmkYv 351
Cdd:COG4178 202 igrplirlnfEQQRREADFRFalVRVR--ENAESIALYRGEAAERRRLRRRFDAVIANWRRLIRRQRNLTFFTTG---Y- 275
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 352 wsscGLIMVAIPI-ITATGFADGDLEDGpkqamvsdrteAFTTARNLLASGADAIERIMSSYKEITELAGYTARVYNMFW 430
Cdd:COG4178 276 ----GQLAVIFPIlVAAPRYFAGEITLG-----------GLMQAASAFGQVQGALSWFVDNYQSLAEWRATVDRLAGFEE 340
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 431 VFDEVKRgiykrtvtqEPENHSkrggnlelplsdtlaikGTVIDVDHGIICENVPIITPAGEVVASRLNFKVEEGMHLLI 510
Cdd:COG4178 341 ALEAADA---------LPEAAS-----------------RIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLI 394
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 511 TGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYMSLGSLRDQVIYPDSADDmrekgYTDQDLERILHSVHL 590
Cdd:COG4178 395 TGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGTLREALLYPATAEA-----FSDAELREALEAVGL 469
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 591 YHIVQReggWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPSL 668
Cdd:COG4178 470 GHLAER---LDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLlrEELPGTTVISVGHRSTL 546
                       570       580
                ....*....|....*....|...
gi 60218875 669 WKYHTHLLQFDGEGGWRFEQLDT 691
Cdd:COG4178 547 AAFHDRVLELTGDGSWQLLPAEA 569
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
479-684 2.95e-82

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: 258.62  E-value: 2.95e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 479 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYMSLGSL 558
Cdd:cd03223   1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 559 RDQVIYPdsaddmrekgytdqdlerilhsvhlyhivqreggwdavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDECTS 638
Cdd:cd03223  81 REQLIYP----------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 60218875 639 AVSIDVEGKIFQAAIGAGISLLSITHRPSLWKYHTHLLQFDGEGGW 684
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
487-664 4.47e-30

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 117.99  E-value: 4.47e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 487 ITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYK-------PPPQH---MFYIPQRPYMSL 555
Cdd:COG4619   8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGeIYLDgkplsamPPPEWrrqVAYVPQEPALWG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 556 GSLRDQVIYPDSaddMREKGYTDQDLERILHSVHLYhivqreggwDAVMDWK-DVLSGGEKQRMGMARMFYHKPKYALLD 634
Cdd:COG4619  88 GTVRDNLPFPFQ---LRERKFDRERALELLERLGLP---------PDILDKPvERLSGGERQRLALIRALLLQPDVLLLD 155
                       170       180       190
                ....*....|....*....|....*....|....
gi 60218875 635 ECTSAVSID----VEGKIFQAAIGAGISLLSITH 664
Cdd:COG4619 156 EPTSALDPEntrrVEELLREYLAEEGRAVLWVSH 189
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
479-668 5.10e-27

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: 116.40  E-value: 5.10e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 479 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL---------YKPPP--QHMFYI 547
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdLDPASwrRQIAWV 416
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 548 PQRPYMSLGSLRDQViypdsadDMREKGYTDQDLERILHSVHLYHIVQR-EGGWDAVmdwkdV------LSGGEKQRMGM 620
Cdd:COG4988 417 PQNPYLFAGTIRENL-------RLGRPDASDEELEAALEAAGLDEFVAAlPDGLDTP-----LgeggrgLSGGQAQRLAL 484
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 60218875 621 ARMFYHKPKYALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPSL 668
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQAlrRLAKGRTVILITHRLAL 534
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
479-668 4.18e-26

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: 105.16  E-value: 4.18e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 479 IICENVPIITPAGEV-VASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhMFYIPQRPYmSLGS 557
Cdd:cd03228   1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL------IDGVDLRDL-DLES 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 558 LRDQViypdsaddmrekGYTDQDlerilhsVHLYHivqreggwDAVMDwkDVLSGGEKQRMGMARMFYHKPKYALLDECT 637
Cdd:cd03228  74 LRKNI------------AYVPQD-------PFLFS--------GTIRE--NILSGGQRQRIAIARALLRDPPILILDEAT 124
                       170       180       190
                ....*....|....*....|....*....|...
gi 60218875 638 SAVSIDVEGKIFQA--AIGAGISLLSITHRPSL 668
Cdd:cd03228 125 SALDPETEALILEAlrALAKGKTVIVIAHRLST 157
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
498-668 3.04e-23

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: 105.30  E-value: 3.04e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY------KPPP----QHMFYIPQRPYMSLGSLRDQVIypd 566
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGrILIdgidlrQIDPaslrRQIGVVLQDVFLFSGTIRENIT--- 570
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 567 saddMREKGYTDQDLERILHSVHLYHIVQR-EGGWDA-VMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDV 644
Cdd:COG2274 571 ----LGDPDATDEEIIEAARLAGLHDFIEAlPMGYDTvVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAET 646
                       170       180
                ....*....|....*....|....*.
gi 60218875 645 EGKIFQA--AIGAGISLLSITHRPSL 668
Cdd:COG2274 647 EAIILENlrRLLKGRTVIIIAHRLST 672
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
112-667 2.97e-21

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 98.31  E-value: 2.97e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 112 VALISRTFLSIYVAGLDGKIVKSIVEKKPRTFIIKLIkWLMIAIpaTFVNSAIRYLEC--------KLALAFRTRLVDHA 183
Cdd:COG1132  28 LLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLL-LLLLGL--ALLRALLSYLQRyllarlaqRVVADLRRDLFEHL 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 184 YE---TYFANQTYYKVINMdgrlanpdqsLTEDIMMFSQSVAHLYSNLTKPILDVILTSYTLIRTatsrgaSP-IGPTLL 259
Cdd:COG1132 105 LRlplSFFDRRRTGDLLSR----------LTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVI------DWrLALIVL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 260 AGLVVYAtakvlkACSPKFGSLVAEEAHRkgyLRYVHSRIIANVEEiaFYRGHKV---------EMKQLQKCYKALayqm 330
Cdd:COG1132 169 LVLPLLL------LVLRLFGRRLRKLFRR---VQEALAELNGRLQE--SLSGIRVvkafgreerELERFREANEEL---- 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 331 nliLSKRLWYIMIEQFLMKYVWSSCGLIMVAIPIITATGFADGDLEDGpkqamvsdrteAFTTARNLLASGADAIERIMS 410
Cdd:COG1132 234 ---RRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVG-----------DLVAFILYLLRLFGPLRQLAN 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 411 SYKEITELAGYTARVynmFWVFDEvkrgiykrtvtqePENHSKRGGNLELPlsdtlaikgtviDVDHGIICENVpiiT-- 488
Cdd:COG1132 300 VLNQLQRALASAERI---FELLDE-------------PPEIPDPPGAVPLP------------PVRGEIEFENV---Sfs 348
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 489 -PAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VL--------YKPP--PQHMFYIPQRPYMSLG 556
Cdd:COG1132 349 yPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGrILidgvdirdLTLEslRRQIGVVPQDTFLFSG 428
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 557 SLRDQVIYPDsaddmreKGYTDQDLERILHSVHLYHIVQR-EGGWDAVmdwkdV------LSGGEKQRMGMARMFYHKPK 629
Cdd:COG1132 429 TIRENIRYGR-------PDATDEEVEEAAKAAQAHEFIEAlPDGYDTV-----VgergvnLSGGQRQRIAIARALLKDPP 496
                       570       580       590       600
                ....*....|....*....|....*....|....*....|
gi 60218875 630 YALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPS 667
Cdd:COG1132 497 ILILDEATSALDTETEALIQEAleRLMKGRTTIVIAHRLS 536
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
479-668 3.38e-21

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: 98.13  E-value: 3.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   479 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV-------LYKPPPQHMF----YI 547
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSiavngvpLADADADSWRdqiaWV 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   548 PQRPYMSLGSLRDQVIypdsaddMREKGYTDQDLERILHSVHLYHIVQ-REGGWDAVMDWKDV-LSGGEKQRMGMARMFY 625
Cdd:TIGR02857 402 PQHPFLFAGTIAENIR-------LARPDASDAEIREALERAGLDEFVAaLPQGLDTPIGEGGAgLSGGQAQRLALARAFL 474
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 60218875   626 HKPKYALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPSL 668
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEAlrALAQGRTVLLVTHRLAL 519
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
479-668 3.62e-21

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: 91.12  E-value: 3.62e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 479 IICENVPIITP-AGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhmfyIPQRPYMSLGS 557
Cdd:cd03246   1 LEVENVSFRYPgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR---------LDGADISQWDP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 558 --LRDQViypdsaddmrekGYTDQDLEriLHSvhlyhivqreggwDAVMDwkDVLSGGEKQRMGMARMFYHKPKYALLDE 635
Cdd:cd03246  72 neLGDHV------------GYLPQDDE--LFS-------------GSIAE--NILSGGQRQRLGLARALYGNPRILVLDE 122
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 60218875 636 CTSavSIDVEG-KIFQAAI----GAGISLLSITHRPSL 668
Cdd:cd03246 123 PNS--HLDVEGeRALNQAIaalkAAGATRIVIAHRPET 158
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
497-638 1.23e-20

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: 88.86  E-value: 1.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   497 RLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY----------KPPPQHMFYIPQRP-YMSLGSLRDQVIY 564
Cdd:pfam00005   3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGtILLdgqdltdderKSLRKEIGYVFQDPqLFPRLTVRENLRL 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60218875   565 PDSADDMREKGYTDQdLERILHSVHLYHIVQReggwdAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTS 638
Cdd:pfam00005  83 GLLLKGLSKREKDAR-AEEALEKLGLGDLADR-----PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
489-667 5.52e-20

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: 94.45  E-value: 5.52e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 489 PAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV-------LYKPPP----QHMFYIPQRPYMSLGS 557
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSitlggvdLRDLDEddlrRRIAVVPQRPHLFDTT 424
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 558 LRD--QVIYPDSaddmrekgyTDQDLERILHSVHLYHIVQR-EGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALL 633
Cdd:COG4987 425 LREnlRLARPDA---------TDEELWAALERVGLGDWLAAlPDGLDTWLGEGGRrLSGGERRRLALARALLRDAPILLL 495
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 60218875 634 DECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPS 667
Cdd:COG4987 496 DEPTEGLDAATEQALLADllEALAGRTVLLITHRLA 531
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
493-668 1.19e-19

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: 86.53  E-value: 1.19e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 493 VVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhmFYIPQRPYMSLGSLRDQViypdsaddmr 572
Cdd:cd00267  13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL-------IDGKDIAKLPLEELRRRI---------- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 573 ekGYTDQdlerilhsvhlyhivqreggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKI---F 649
Cdd:cd00267  76 --GYVPQ------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLlelL 123
                       170
                ....*....|....*....
gi 60218875 650 QAAIGAGISLLSITHRPSL 668
Cdd:cd00267 124 RELAEEGRTVIIVTHDPEL 142
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
482-668 1.28e-19

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: 88.03  E-value: 1.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 482 ENVPIITPAGEVVASR-LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY------KPPP----QHMFYIPQ 549
Cdd:cd03245   6 RNVSFSYPNQEIPALDnVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGsVLLdgtdirQLDPadlrRNIGYVPQ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 550 RPYMSLGSLRDQVIYpdsaddmrekGYTDQDLERILHSVHLYHIVQ-------------REGGwdavmdwkDVLSGGEKQ 616
Cdd:cd03245  86 DVTLFYGTLRDNITL----------GAPLADDERILRAAELAGVTDfvnkhpngldlqiGERG--------RGLSGGQRQ 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 60218875 617 RMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPSL 668
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERlrQLLGDKTLIIITHRPSL 201
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
491-666 6.30e-19

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: 85.61  E-value: 6.30e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYK---------PPPQHMFYIPQRP--YMSLgSL 558
Cdd:COG4133  14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGeVLWNgepirdareDYRRRLAYLGHADglKPEL-TV 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 559 RDQVIYpdsADDMREKGYTDQDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDECTS 638
Cdd:COG4133  93 RENLRF---WAALYGLRADREAIDEALEAVGLAGLADLPVR---------QLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
                       170       180       190
                ....*....|....*....|....*....|...
gi 60218875 639 AvsIDVEGK-----IFQAAIGAGISLLSITHRP 666
Cdd:COG4133 161 A--LDAAGVallaeLIAAHLARGGAVLLTTHQP 191
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
479-667 4.85e-17

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: 80.73  E-value: 4.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 479 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-----------KPPPQHMFYI 547
Cdd:cd03254   3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidgidirdisrKSLRSMIGVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 548 PQRPYMSLGSLRDQVIYPDSaddmrekGYTDQDLERILHSVHLYHIVQR-EGGWDAVM-DWKDVLSGGEKQRMGMARMFY 625
Cdd:cd03254  83 LQDTFLFSGTIMENIRLGRP-------NATDEEVIEAAKEAGAHDFIMKlPNGYDTVLgENGGNLSQGERQLLAIARAML 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 60218875 626 HKPKYALLDECTSavSIDVEG-KIFQAAIGA---GISLLSITHRPS 667
Cdd:cd03254 156 RDPKILILDEATS--NIDTETeKLIQEALEKlmkGRTSIIIAHRLS 199
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
498-676 6.52e-17

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: 79.82  E-value: 6.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPpqHMFYIPQRPYMSLGSLRDQVIYpdsADDMREKGYT 577
Cdd:cd03250  24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEPWIQNGTIRENILF---GKPFDEERYE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 578 --------DQDLErILHSVHLYHIvqREGGwdaVMdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIF 649
Cdd:cd03250  99 kvikacalEPDLE-ILPDGDLTEI--GEKG---IN-----LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIF 167
                       170       180       190
                ....*....|....*....|....*....|..
gi 60218875 650 QAAIGaGISLLS-----ITHRPSLWKYHTHLL 676
Cdd:cd03250 168 ENCIL-GLLLNNktrilVTHQLQLLPHADQIV 198
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
498-672 9.99e-17

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: 79.43  E-value: 9.99e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPP----------QHMFYIPQRPymslgslRDQVIYPD 566
Cdd:cd03225  20 ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGeVLVDGKDltklslkelrRKVGLVFQNP-------DDQFFGPT 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 567 SADD----MREKGYTDQDLERILHSvhlyhiVQREGGWDAVMDWK-DVLSGGEKQRMGMARMFYHKPKYALLDECTSavS 641
Cdd:cd03225  93 VEEEvafgLENLGLPEEEIEERVEE------ALELVGLEGLRDRSpFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA--G 164
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 60218875 642 IDVEG-----KIFQAAIGAGISLLSITHRPSLWKYH 672
Cdd:cd03225 165 LDPAGrrellELLKKLKAEGKTIIIVTHDLDLLLEL 200
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
498-639 2.06e-16

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: 79.15  E-value: 2.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV-------LYKPPPQHMFYIP-----------QRPYMSLGSLR 559
Cdd:cd03260  19 ISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdegevlLDGKDIYDLDVDVlelrrrvgmvfQKPNPFPGSIY 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 560 DQVIYPDSADDMREKGYTDQDLERILHSVHLyhivqreggWDAVMDWKDV--LSGGEKQRMGMARMFYHKPKYALLDECT 637
Cdd:cd03260  99 DNVAYGLRLHGIKLKEELDERVEEALRKAAL---------WDEVKDRLHAlgLSGGQQQRLCLARALANEPEVLLLDEPT 169

                ..
gi 60218875 638 SA 639
Cdd:cd03260 170 SA 171
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
491-639 2.62e-16

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: 79.32  E-value: 2.62e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KP----PP----QHMFYIPQRPYMSLG-SL 558
Cdd:COG1120  13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDlaslSRrelaRRIAYVPQEPPAPFGlTV 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 559 RDQVI---YP-------DSADDMREkgytdqdLERILHSVHLYHIVQREggWDAvmdwkdvLSGGEKQRMGMARMFYHKP 628
Cdd:COG1120  93 RELVAlgrYPhlglfgrPSAEDREA-------VEEALERTGLEHLADRP--VDE-------LSGGERQRVLIARALAQEP 156
                       170
                ....*....|.
gi 60218875 629 KYALLDECTSA 639
Cdd:COG1120 157 PLLLLDEPTSH 167
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
494-680 3.70e-16

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: 78.28  E-value: 3.70e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 494 VASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPPPQ--HMFY------IPQRPYMSLGSLRDQV 562
Cdd:cd03248  29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPISQyeHKYLhskvslVGQEPVLFARSLQDNI 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 563 IYpdsaddmrekGYTDQDLERILHSVHLYH----IVQREGGWDAVMDWK-DVLSGGEKQRMGMARMFYHKPKYALLDECT 637
Cdd:cd03248 109 AY----------GLQSCSFECVKEAAQKAHahsfISELASGYDTEVGEKgSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 60218875 638 SAVSIDVEGKIFQAAIG--AGISLLSITHRPSLWKYHTHLLQFDG 680
Cdd:cd03248 179 SALDAESEQQVQQALYDwpERRTVLVIAHRLSTVERADQILVLDG 223
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
491-681 4.89e-16

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: 77.57  E-value: 4.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG---VLYKPPPQ--HMF-YIPQRPYMSLG---SLRDQ 561
Cdd:cd03235  11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGsirVFGKPLEKerKRIgYVPQRRSIDRDfpiSVRDV 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 562 V---IYPDSADDMREKGYTDQDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDECTS 638
Cdd:cd03235  91 VlmgLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIG---------ELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 60218875 639 AVsiDVEGK-----IFQAAIGAGISLLSITH-RPSLWKYHTHLLQFDGE 681
Cdd:cd03235 162 GV--DPKTQediyeLLRELRREGMTILVVTHdLGLVLEYFDRVLLLNRT 208
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
482-668 1.44e-15

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: 80.56  E-value: 1.44e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 482 ENVPIITP-AGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV-------LYKPPP----QHMFYIPQ 549
Cdd:COG4618 334 ENLTVVPPgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSvrldgadLSQWDReelgRHIGYLPQ 413
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 550 RPymSL--GSLRdQVI--YPDsADDmrekgytdqdlERILH-----SVH-LyhIVQREGGWDAVMDWKD-VLSGGEKQRM 618
Cdd:COG4618 414 DV--ELfdGTIA-ENIarFGD-ADP-----------EKVVAaaklaGVHeM--ILRLPDGYDTRIGEGGaRLSGGQRQRI 476
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 60218875 619 GMARMFYHKPKYALLDECTSavSIDVEG-KIFQAAIGA----GISLLSITHRPSL 668
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNS--NLDDEGeAALAAAIRAlkarGATVVVITHRPSL 529
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
499-664 1.88e-15

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: 76.77  E-value: 1.88e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 499 NFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-------VLYKPPPQHMF----YIPQRPYMSL---GSLRDQVIY 564
Cdd:COG1124  25 SLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGevtfdgrPVTRRRRKAFRrrvqMVFQDPYASLhprHTVDRILAE 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 565 PdsaddMREKGYTDQD--LERILHSVHLYhivqreggwDAVMD-WKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVs 641
Cdd:COG1124 105 P-----LRIHGLPDREerIAELLEQVGLP---------PSFLDrYPHQLSGGQRQRVAIARALILEPELLLLDEPTSAL- 169
                       170       180       190
                ....*....|....*....|....*....|..
gi 60218875 642 iDVegkIFQAAI---------GAGISLLSITH 664
Cdd:COG1124 170 -DV---SVQAEIlnllkdlreERGLTYLFVSH 197
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
491-666 2.59e-15

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 75.22  E-value: 2.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQHMfyipQRPymslgSLRDQVIYPDSAD 569
Cdd:cd03231  12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGrVLLNGGPLDF----QRD-----SIARGLLYLGHAP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 570 DMREKGYTDQDLeRILHSVHlyhivQREGGWDAVMD-----WKDV----LSGGEKQRMGMARMFYHKPKYALLDECTsaV 640
Cdd:cd03231  83 GIKTTLSVLENL-RFWHADH-----SDEQVEEALARvglngFEDRpvaqLSAGQQRRVALARLLLSGRPLWILDEPT--T 154
                       170       180       190
                ....*....|....*....|....*....|.
gi 60218875 641 SIDVEG-----KIFQAAIGAGISLLSITHRP 666
Cdd:cd03231 155 ALDKAGvarfaEAMAGHCARGGMVVLTTHQD 185
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
491-666 3.89e-15

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 74.91  E-value: 3.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQHmfyipqrpymsLGSLRDQVIYPDSAD 569
Cdd:PRK13539  14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtIKLDGGDID-----------DPDVAEACHYLGHRN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  570 DMRE--------------KGYTDQDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMAR-MFYHKPKYaLLD 634
Cdd:PRK13539  83 AMKPaltvaenlefwaafLGGEELDIAAALEAVGLAPLAHLPFG---------YLSAGQKRRVALARlLVSNRPIW-ILD 152
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 60218875  635 ECTSAvsIDVEG-KIFQAAI-----GAGISLLSiTHRP 666
Cdd:PRK13539 153 EPTAA--LDAAAvALFAELIrahlaQGGIVIAA-THIP 187
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
489-665 4.37e-15

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: 74.84  E-value: 4.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 489 PAGEVVASRLNFKVEEGMHLLITGPNGCGKSS----LFRILsglwPVYEGVLY-------KPPP----QHMFYIPQRPYM 553
Cdd:cd03244  14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILidgvdisKIGLhdlrSRISIIPQDPVL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 554 SLGSLRDQViypdsadDMREKgYTDQDLERILHSVHLY-HIVQREGGWDA-VMDWKDVLSGGEKQRMGMARMFYHKPKYA 631
Cdd:cd03244  90 FSGTIRSNL-------DPFGE-YSDEELWQALERVGLKeFVESLPGGLDTvVEEGGENLSVGQRQLLCLARALLRKSKIL 161
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 60218875 632 LLDECTSavSIDVEG-KIFQAAIG---AGISLLSITHR 665
Cdd:cd03244 162 VLDEATA--SVDPETdALIQKTIReafKDCTVLTIAHR 197
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
491-668 5.93e-15

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: 73.62  E-value: 5.93e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPP----QHMFYIPQrpymSLGSLR 559
Cdd:cd03214  11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILldgkdlaSLSPkelaRKIAYVPQ----ALELLG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 560 dqviypdsADDMREKGYTDqdlerilhsvhlyhivqreggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSA 639
Cdd:cd03214  87 --------LAHLADRPFNE-------------------------------LSGGERQRVLLARALAQEPPILLLDEPTSH 127
                       170       180       190
                ....*....|....*....|....*....|...
gi 60218875 640 V----SIDVEGKIFQAAIGAGISLLSITHRPSL 668
Cdd:cd03214 128 LdiahQIELLELLRRLARERGKTVVMVLHDLNL 160
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
488-635 1.11e-14

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: 73.66  E-value: 1.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 488 TPAGEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY-----KPPPQHMFYIPQR----PYMslg 556
Cdd:cd03293  12 GGGGAVTAlEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGeVLVdgepvTGPGPDRGYVFQQdallPWL--- 88
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60218875 557 SLRDQVIYPDSADDMREKGYTDQdLERILHSVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDE 635
Cdd:cd03293  89 TVLDNVALGLELQGVPKAEARER-AEELLELVGLSGFENA---------YPHQLSGGMRQRVALARALAVDPDVLLLDE 157
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
488-635 1.48e-14

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 74.36  E-value: 1.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 488 TPAGEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY------KPPPQHMFYIPQRPymslgSL-- 558
Cdd:COG1116  19 TGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvTGPGPDRGVVFQEP-----ALlp 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 559 ----RDQVIYPDSADDMReKGYTDQDLERILHSVHLyhivqreggwDAVMD-WKDVLSGGEKQRMGMARMFYHKPKYALL 633
Cdd:COG1116  94 wltvLDNVALGLELRGVP-KAERRERARELLELVGL----------AGFEDaYPHQLSGGMRQRVAIARALANDPEVLLM 162

                ..
gi 60218875 634 DE 635
Cdd:COG1116 163 DE 164
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
498-664 1.67e-14

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: 73.06  E-value: 1.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQH-------MFYIPQRPYMSLG--SLRDQVIYpdS 567
Cdd:cd03226  19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGsILLNGKPIKakerrksIGYVMQDVDYQLFtdSVREELLL--G 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 568 ADDMREKGytdQDLERILHSVHLYhivqreggwdavmDWKDV----LSGGEKQRMGMARMFYHKPKYALLDECTSAV--- 640
Cdd:cd03226  97 LKELDAGN---EQAETVLKDLDLY-------------ALKERhplsLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLdyk 160
                       170       180
                ....*....|....*....|....
gi 60218875 641 SIDVEGKIFQAAIGAGISLLSITH 664
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITH 184
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
494-665 2.15e-14

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 76.79  E-value: 2.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  494 VASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPPP--------QHMFYIPQRPYMSLGSLRD-- 560
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlngQPIAdyseaalrQAISVVSQRVHLFSATLRDnl 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  561 QVIYPDSaddmrekgyTDQDLERILHSVHLYHIVQREGGWDAVM-DWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSA 639
Cdd:PRK11160 435 LLAAPNA---------SDEALIEVLQQVGLEKLLEDDKGLNAWLgEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
                        170       180
                 ....*....|....*....|....*...
gi 60218875  640 VSIDVEGKIFQ--AAIGAGISLLSITHR 665
Cdd:PRK11160 506 LDAETERQILEllAEHAQNKTVLMITHR 533
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
489-666 2.47e-14

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: 76.25  E-value: 2.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   489 PAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQHMF----------YIPQRPYMSLGS 557
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGeVTLDGVPVSSLdqdevrrrvsVCAQDAHLFDTT 424
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   558 LRDQVIY--PDSaddmrekgyTDQDLERILHSVHLY-HIVQREGGWDAVM-DWKDVLSGGEKQRMGMARMFYHKPKYALL 633
Cdd:TIGR02868 425 VRENLRLarPDA---------TDEELWAALERVGLAdWLRALPDGLDTVLgEGGARLSGGERQRLALARALLADAPILLL 495
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 60218875   634 DECTSAVSIDVEGKIFQ--AAIGAGISLLSITHRP 666
Cdd:TIGR02868 496 DEPTEHLDAETADELLEdlLAALSGRTVVLITHHL 530
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
499-671 3.60e-14

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: 72.14  E-value: 3.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 499 NFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPP--------QHMFYIPQR----PYMSLgslR 559
Cdd:cd03255  24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdisKLSEkelaafrrRHIGFVFQSfnllPDLTA---L 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 560 DQVIYP-----DSADDMREKgytdqdLERILHSVHLYHIVQREGGWdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLD 634
Cdd:cd03255 101 ENVELPlllagVPKKERRER------AEELLERVGLGDRLNHYPSE---------LSGGQQQRVAIARALANDPKIILAD 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 60218875 635 ECTSAV----SIDVEGKIFQAAIGAGISLLSITHRPSLWKY 671
Cdd:cd03255 166 EPTGNLdsetGKEVMELLRELNKEAGTTIVVVTHDPELAEY 206
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
499-635 4.99e-14

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 75.49  E-value: 4.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 499 NFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYMSLG-SLRDQVI--YPDSADDMREK- 574
Cdd:COG0488  18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDlTVLDTVLdgDAELRALEAELe 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 575 ------GYTDQDLERIlhsVHLYHIVQREGGWDA------VM--------DW-KDV--LSGGEKQRMGMARMFYHKPKYA 631
Cdd:COG0488  98 eleaklAEPDEDLERL---AELQEEFEALGGWEAearaeeILsglgfpeeDLdRPVseLSGGWRRRVALARALLSEPDLL 174

                ....
gi 60218875 632 LLDE 635
Cdd:COG0488 175 LLDE 178
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
479-667 5.06e-14

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: 72.26  E-value: 5.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 479 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY------KPPPQHMF-----YI 547
Cdd:cd03253   1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdiREVTLDSLrraigVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 548 PQrpymslgslrDQVIYPDS-ADDMRekgY-----TDQDLERILHSVHLYHIVQR-EGGWDAVMDWKDV-LSGGEKQRMG 619
Cdd:cd03253  81 PQ----------DTVLFNDTiGYNIR---YgrpdaTDEEVIEAAKAAQIHDKIMRfPDGYDTIVGERGLkLSGGEKQRVA 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 60218875 620 MARMFYHKPKYALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPS 667
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAAlrDVSKGRTTIVIAHRLS 197
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
491-664 1.13e-13

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 71.27  E-value: 1.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG---VLYKPPPQHMF---YIPQRPYMSLGslrdqviY 564
Cdd:COG1121  18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGtvrLFGKPPRRARRrigYVPQRAEVDWD-------F 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 565 PDSADDM------REKG----YTDQDLERI---LHSVHLYHIVQR---EggwdavmdwkdvLSGGEKQRMGMARMFYHKP 628
Cdd:COG1121  91 PITVRDVvlmgryGRRGlfrrPSRADREAVdeaLERVGLEDLADRpigE------------LSGGQQQRVLLARALAQDP 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 60218875 629 KYALLDECTSAVsiDVEGkifQAAI--------GAGISLLSITH 664
Cdd:COG1121 159 DLLLLDEPFAGV--DAAT---EEALyellrelrREGKTILVVTH 197
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
489-667 1.18e-13

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: 71.36  E-value: 1.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 489 PAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VL-------------YKpppQHMFYIPQRPYMS 554
Cdd:cd03252  12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrVLvdghdlaladpawLR---RQVGVVLQENVLF 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 555 LGSLRDQVIYPDSADDMREKGYTDQdleriLHSVHLYhIVQREGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALL 633
Cdd:cd03252  89 NRSIRDNIALADPGMSMERVIEAAK-----LAGAHDF-ISELPEGYDTIVGEQGAgLSGGQRQRIAIARALIHNPRILIF 162
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 60218875 634 DECTSAVSIDVEGKIFQ--AAIGAGISLLSITHRPS 667
Cdd:cd03252 163 DEATSALDYESEHAIMRnmHDICAGRTVIIIAHRLS 198
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
479-669 1.33e-13

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: 73.78  E-value: 1.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 479 IICENVPIITPAGEVVASR-LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWP---------VYEGV-LYKPPPQ----H 543
Cdd:COG1123   5 LEVRDLSVRYPGGDVPAVDgVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrisgevLLDGRdLLELSEAlrgrR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 544 MFYIPQRPYMSLGSLR--DQVIYP-----DSADDMREKgytdqdLERILHSVHLYHIVQReggwdavmdWKDVLSGGEKQ 616
Cdd:COG1123  85 IGMVFQDPMTQLNPVTvgDQIAEAlenlgLSRAEARAR------VLELLEAVGLERRLDR---------YPHQLSGGQRQ 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 60218875 617 RMGMARMFYHKPKYALLDECTSA----VSIDVEGKIFQAAIGAGISLLSITHRPSLW 669
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTAldvtTQAEILDLLRELQRERGTTVLLITHDLGVV 206
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
498-668 1.37e-13

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 74.37  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPPPQ--HMFY------IPQRPYMSLGSLRDQVIYpd 566
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldgVPLVQydHHYLhrqvalVGQEPVLFSGSVRENIAY-- 577
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   567 saddmrekGYTDQDLERILHSVHLYH----IVQREGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALLDECTSAVS 641
Cdd:TIGR00958 578 --------GLTDTPDEEIMAAAKAANahdfIMEFPNGYDTEVGEKGSqLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
                         170       180
                  ....*....|....*....|....*..
gi 60218875   642 IDVEGKIFQAAIGAGISLLSITHRPSL 668
Cdd:TIGR00958 650 AECEQLLQESRSRASRTVLLIAHRLST 676
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
487-664 2.06e-13

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: 73.40  E-value: 2.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 487 ITPAGEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY-------------KPPPQHMFYIPQRP 551
Cdd:COG1123 272 VRGKGGVRAvDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGsILFdgkdltklsrrslRELRRRVQMVFQDP 351
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 552 YMSL---GSLRDQVIYPDSADDMREKGYTDQDLERILHSVHLYhivqreggwDAVMDWK-DVLSGGEKQRMGMARMFYHK 627
Cdd:COG1123 352 YSSLnprMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP---------PDLADRYpHELSGGQRQRVAIARALALE 422
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 60218875 628 PKYALLDECTSA--VSIdvegkifQAAIGA---------GISLLSITH 664
Cdd:COG1123 423 PKLLILDEPTSAldVSV-------QAQILNllrdlqrelGLTYLFISH 463
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
446-665 5.66e-13

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 72.18  E-value: 5.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  446 QEPENHSKRGGNlELPLSDTLAIKGtvidvdhgiicENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRIL 525
Cdd:PRK11174 329 ETPLAHPQQGEK-ELASNDPVTIEA-----------EDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  526 SGLWPvYEGVL--------------YKpppQHMFYIPQRPYMSLGSLRDQVIypdsaddMREKGYTDQDLERILHSVHLY 591
Cdd:PRK11174 397 LGFLP-YQGSLkingielreldpesWR---KHLSWVGQNPQLPHGTLRDNVL-------LGNPDASDEQLQQALENAWVS 465
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60218875  592 HIVQR-EGGWD-AVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHR 665
Cdd:PRK11174 466 EFLPLlPQGLDtPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQAlnAASRRQTTLMVTHQ 543
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
479-668 6.21e-13

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: 68.90  E-value: 6.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 479 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY-------KPPP---QHMFYI 547
Cdd:COG1122   1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGeVLVdgkditkKNLRelrRKVGLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 548 PQRPymslgslRDQVIYPDSADD----MREKGYTDQDLER----ILHSVHLYHIVQReggwdAVMDwkdvLSGGEKQRMG 619
Cdd:COG1122  81 FQNP-------DDQLFAPTVEEDvafgPENLGLPREEIRErveeALELVGLEHLADR-----PPHE----LSGGQKQRVA 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 60218875 620 MARMFYHKPKYALLDECTSavSIDVEGK-----IFQAAIGAGISLLSITHRPSL 668
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTA--GLDPRGRrelleLLKRLNKEGKTVIIVTHDLDL 196
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
491-646 6.81e-13

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 68.94  E-value: 6.81e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG---VLYKPPP-------QHMFYIPQRP--YMSLgS 557
Cdd:COG1131  11 GDKTAlDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGevrVLGEDVArdpaevrRRIGYVPQEPalYPDL-T 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 558 LRDQV-----IYPDSADDMREKgytdqdLERILHSVHLyhivqreggwDAVMDWK-DVLSGGEKQRMGMARMFYHKPKYA 631
Cdd:COG1131  90 VRENLrffarLYGLPRKEARER------IDELLELFGL----------TDAADRKvGTLSGGMKQRLGLALALLHDPELL 153
                       170
                ....*....|....*
gi 60218875 632 LLDECTSAVsiDVEG 646
Cdd:COG1131 154 ILDEPTSGL--DPEA 166
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
490-664 7.88e-13

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 68.59  E-value: 7.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  490 AGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL---------YKPPP--QHMFYIPQRPYMSLGSL 558
Cdd:PRK10247  18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegedistLKPEIyrQQVSYCAQTPTLFGDTV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  559 RDQVIYPDSaddMREKGYTDQDLERILHSVHL-YHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHKPKYALLDECT 637
Cdd:PRK10247  98 YDNLIFPWQ---IRNQQPDPAIFLDDLERFALpDTILTKN---------IAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
                        170       180       190
                 ....*....|....*....|....*....|.
gi 60218875  638 SAVS----IDVEGKIFQAAIGAGISLLSITH 664
Cdd:PRK10247 166 SALDesnkHNVNEIIHRYVREQNIAVLWVTH 196
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
489-664 1.09e-12

cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130234 [Multi-domain]  Cd Length: 190  Bit Score: 67.06  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   489 PAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSG-LWPVYEGVLYKPPP------------QHMFYIPQRPymsl 555
Cdd:TIGR01166   2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGlLRPQSGAVLIDGEPldysrkgllerrQRVGLVFQDP---- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   556 gslRDQVIYPDSADDM----REKGYTDQDLERI----LHSVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHK 627
Cdd:TIGR01166  78 ---DDQLFAADVDQDVafgpLNLGLSEAEVERRvreaLTAVGASGLRERP---------THCLSGGEKKRVAIAGAVAMR 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 60218875   628 PKYALLDECTSAVsiDVEGKIFQAAI-----GAGISLLSITH 664
Cdd:TIGR01166 146 PDVLLLDEPTAGL--DPAGREQMLAIlrrlrAEGMTVVISTH 185
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
498-667 1.14e-12

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: 68.34  E-value: 1.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL---------YKPP--PQHMFYIPQRPYMSLGSLRDQVIY-- 564
Cdd:cd03249  22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdLNLRwlRSQIGLVSQEPVLFDGTIAENIRYgk 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 565 PDSADDMREKGYTDQDLerilHSVhlyhIVQREGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALLDECTSAVSID 643
Cdd:cd03249 102 PDATDEEVEEAAKKANI----HDF----IMSLPDGYDTLVGERGSqLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
                       170       180
                ....*....|....*....|....*..
gi 60218875 644 VEgKIFQAAIG---AGISLLSITHRPS 667
Cdd:cd03249 174 SE-KLVQEALDramKGRTTIVIAHRLS 199
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
491-666 1.44e-12

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: 67.00  E-value: 1.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKP---------PPQHMFYIPQRPYM--SLGSL 558
Cdd:TIGR01189  12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGeVRWNGtplaeqrdePHENILYLGHLPGLkpELSAL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   559 RDQVIYpdsADDMrekGYTDQDLERILHSVHLYHIVQREGGWdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTs 638
Cdd:TIGR01189  92 ENLHFW---AAIH---GGAQRTIEDALAAVGLTGFEDLPAAQ---------LSAGQQRRLALARLWLSRRPLWILDEPT- 155
                         170       180       190
                  ....*....|....*....|....*....|...
gi 60218875   639 aVSIDVEG-----KIFQAAIGAGISLLSITHRP 666
Cdd:TIGR01189 156 -TALDKAGvallaGLLRAHLARGGIVLLTTHQD 187
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
498-664 2.66e-12

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: 65.50  E-value: 2.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEG--MHLLitGPNGCGKSSLFRILSGLWPVYEG---VLYKPPP-------QHMFYIPQRPYmslgslrdqvIYP 565
Cdd:cd03230  19 ISLTVEKGeiYGLL--GPNGAGKTTLIKIILGLLKPDSGeikVLGKDIKkepeevkRRIGYLPEEPS----------LYE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 566 DsaddmrekgYTdqdlerilhsvhlyhivqregGWDAVMdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDVE 645
Cdd:cd03230  87 N---------LT---------------------VRENLK-----LSGGMKQRLALAQALLHDPELLILDEPTSG--LDPE 129
                       170       180
                ....*....|....*....|....
gi 60218875 646 G-----KIFQAAIGAGISLLSITH 664
Cdd:cd03230 130 SrrefwELLRELKKEGKTILLSSH 153
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
491-648 6.10e-12

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: 66.21  E-value: 6.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY--------KPPPQHMF-YIPQR----PYMSlgs 557
Cdd:cd03299  11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditnLPPEKRDIsYVPQNyalfPHMT--- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 558 lrdqvIYPDSADDMREKGYTDQDLER----ILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALL 633
Cdd:cd03299  88 -----VYKNIAYGLKKRKVDKKEIERkvleIAEMLGIDHLLNRKPE---------TLSGGEQQRVAIARALVVNPKILLL 153
                       170
                ....*....|....*
gi 60218875 634 DECTSAVSIDVEGKI 648
Cdd:cd03299 154 DEPFSALDVRTKEKL 168
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
498-643 1.02e-11

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: 65.65  E-value: 1.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPP---QHMFYIPQRPYMSLG-SLRDQV---- 562
Cdd:COG4555  20 VSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrKEPRearRQIGVLPDERGLYDRlTVRENIryfa 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 563 -IYPDSADDMREKgytdqdLERILHSVHLyhivqreggwDAVMD--WKDvLSGGEKQRMGMARMFYHKPKYALLDECTSA 639
Cdd:COG4555 100 eLYGLFDEELKKR------IEELIELLGL----------EEFLDrrVGE-LSTGMKKKVALARALVHDPKVLLLDEPTNG 162

                ....
gi 60218875 640 VSID 643
Cdd:COG4555 163 LDVM 166
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
492-668 1.14e-11

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 64.98  E-value: 1.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 492 EVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLwpvyegvLYKPPPQHMFYIPQRPYMSLGSLRDQVIYPDSADDM 571
Cdd:COG2401  43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA-------LKGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDA 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 572 REkgytdqdlerILHSVHLYhivqreggwDAVMdWK---DVLSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDVE--- 645
Cdd:COG2401 116 VE----------LLNAVGLS---------DAVL-WLrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSH--LDRQtak 173
                       170       180
                ....*....|....*....|....*.
gi 60218875 646 --GKIFQ-AAIGAGISLLSITHRPSL 668
Cdd:COG2401 174 rvARNLQkLARRAGITLVVATHHYDV 199
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
494-648 1.17e-11

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 65.52  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  494 VASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQR----PYMSLGSLRDQVIYPdsad 569
Cdd:PRK09544  19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKlyldTTLPLTVNRFLRLRP---- 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60218875  570 dmrekGYTDQDLERILHSVHLYHIVqreggwDAVMdwkDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVsiDVEGKI 648
Cdd:PRK09544  95 -----GTKKEDILPALKRVQAGHLI------DAPM---QKLSGGETQRVLLARALLNRPQLLVLDEPTQGV--DVNGQV 157
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
488-667 1.34e-11

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: 64.94  E-value: 1.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 488 TPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-----------VLYKPPPQHMFYIPQRPYMSLG 556
Cdd:cd03251  11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGrilidghdvrdYTLASLRRQIGLVSQDVFLFND 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 557 SLRDQVIYPDSaddmrekGYTDQDLERILHSVHLYHIVQR-EGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALLD 634
Cdd:cd03251  91 TVAENIAYGRP-------GATREEVEEAARAANAHEFIMElPEGYDTVIGERGVkLSGGQRQRIAIARALLKDPPILILD 163
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 60218875 635 ECTSAVSIDVEgKIFQAAIG---AGISLLSITHRPS 667
Cdd:cd03251 164 EATSALDTESE-RLVQAALErlmKNRTTFVIAHRLS 198
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
491-665 3.80e-11

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: 62.06  E-value: 3.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhmfyipqrpymslgsLRDQVIYPDSAD 569
Cdd:cd03216  11 GGVKAlDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL--------------------VDGKEVSFASPR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 570 DMREKGytdqdlerilhsvhLYHIVQreggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSiDVEGKIF 649
Cdd:cd03216  71 DARRAG--------------IAMVYQ--------------LSVGERQMVEIARALARNARLLILDEPTAALT-PAEVERL 121
                       170       180
                ....*....|....*....|
gi 60218875 650 QAAIG----AGISLLSITHR 665
Cdd:cd03216 122 FKVIRrlraQGVAVIFISHR 141
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
498-648 4.90e-11

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: 62.98  E-value: 4.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEGMHLLItGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPP---QHMFYIPQ--RPYMSLgSLRDQVIYP 565
Cdd:cd03264  19 VSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRidgqdvlKQPQklrRRIGYLPQefGVYPNF-TVREFLDYI 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 566 DSADDMREKGyTDQDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDECTsaVSIDVE 645
Cdd:cd03264  97 AWLKGIPSKE-VKARVDEVLELVNLGDRAKKKIG---------SLSGGMRRRVGIAQALVGDPSILIVDEPT--AGLDPE 164

                ...
gi 60218875 646 GKI 648
Cdd:cd03264 165 ERI 167
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
491-665 7.01e-11

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: 62.84  E-value: 7.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVA-SRLNFKVEEG-MHLLItGPNGCGKSSLFRILSGLWPVYEG-VLYK-------PPPQ--HM-----FYIPqRPYM 553
Cdd:cd03219  11 GGLVAlDDVSFSVRPGeIHGLI-GPNGAGKTTLFNLISGFLRPTSGsVLFDgeditglPPHEiaRLgigrtFQIP-RLFP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 554 SLgSLRDQVI---------YPDSADDMREKGYTDQDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMF 624
Cdd:cd03219  89 EL-TVLENVMvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAG---------ELSYGQQRRLEIARAL 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 60218875 625 YHKPKYALLDECTSAVS---IDVEGKIFQAAIGAGISLLSITHR 665
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNpeeTEELAELIRELRERGITVLLVEHD 202
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
491-635 1.68e-10

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: 61.50  E-value: 1.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPPQH----MFYipQR----PYMs 554
Cdd:cd03301  11 GNVTAlDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtDLPPKDrdiaMVF--QNyalyPHM- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 555 lgSLRDQVIYPdsaddMREKGYTDQDLERILHSV-HLYHIvqreggwDAVMDWK-DVLSGGEKQRMGMARMFYHKPKYAL 632
Cdd:cd03301  88 --TVYDNIAFG-----LKLRKVPKDEIDERVREVaELLQI-------EHLLDRKpKQLSGGQRQRVALGRAIVREPKVFL 153

                ...
gi 60218875 633 LDE 635
Cdd:cd03301 154 MDE 156
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
491-667 1.92e-10

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: 61.00  E-value: 1.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPPQhmfyipQR------------ 550
Cdd:cd03259  11 GSVRAlDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILidgrdvtGVPPE------RRnigmvfqdyalf 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 551 PYMslgSLRDQVIYPdsaddMREKGYTDQDLER----ILHSVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYH 626
Cdd:cd03259  85 PHL---TVAENIAFG-----LKLRGVPKAEIRArvreLLELVGLEGLLNR---------YPHELSGGQQQRVALARALAR 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 60218875 627 KPKYALLDECTSAV------SIDVEGKIFQAAigAGISLLSITHRPS 667
Cdd:cd03259 148 EPSLLLLDEPLSALdaklreELREELKELQRE--LGITTIYVTHDQE 192
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
491-665 2.21e-10

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: 61.14  E-value: 2.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVASR-LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL---YKP----PPQHMFYIPQR----PYMslgSL 558
Cdd:cd03269  11 GRVTALDdISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdGKPldiaARNRIGYLPEErglyPKM---KV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 559 RDQVIYPDSADDMReKGYTDQDLERILHSVHLyhivqreggwdavMDWKDV----LSGGEKQRMGMARMFYHKPKYALLD 634
Cdd:cd03269  88 IDQLVYLAQLKGLK-KEEARRRIDEWLERLEL-------------SEYANKrveeLSKGNQQKVQFIAAVIHDPELLILD 153
                       170       180       190
                ....*....|....*....|....*....|....
gi 60218875 635 ECTSA---VSIDVEGKIFQAAIGAGISLLSITHR 665
Cdd:cd03269 154 EPFSGldpVNVELLKDVIRELARAGKTVILSTHQ 187
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
510-639 2.93e-10

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: 60.77  E-value: 2.93e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 510 ITGPNGCGKSSLFRILSGLWPVYEGVLY-------------KPPPQ--HMFYIPQR----PYMSLgslRDQVIYPDSADD 570
Cdd:cd03297  28 IFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrkkiNLPPQqrKIGLVFQQyalfPHLNV---RENLAFGLKRKR 104
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 571 MREkgytDQDLER-ILHSVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSA 639
Cdd:cd03297 105 NRE----DRISVDeLLDLLGLDHLLNR---------YPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
491-635 3.74e-10

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 62.35  E-value: 3.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  491 GEVVASR-LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKpPPQHMFYIP--QRpymSLGSL-RDQVIYP- 565
Cdd:PRK11000  14 GDVVISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRMNDVPpaER---GVGMVfQSYALYPh 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60218875  566 -DSADDMR--------EKGYTDQDLERILHSVHLYHIVQREGgwdavmdwKDvLSGGEKQRMGMARMFYHKPKYALLDE 635
Cdd:PRK11000  90 lSVAENMSfglklagaKKEEINQRVNQVAEVLQLAHLLDRKP--------KA-LSGGQRQRVAIGRTLVAEPSVFLLDE 159
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
498-664 4.09e-10

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: 60.60  E-value: 4.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYK-----PPPQHMF--------YIPQRPYMSLG---SLRD 560
Cdd:cd03257  24 VSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGsIIFDgkdllKLSRRLRkirrkeiqMVFQDPMSSLNprmTIGE 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 561 QVIYP-----DSADDMREKGYTDQDLERILHSVHLYHIVQREggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDE 635
Cdd:cd03257 104 QIAEPlrihgKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHE------------LSGGQRQRVAIARALALNPKLLIADE 171
                       170       180       190
                ....*....|....*....|....*....|....*
gi 60218875 636 CTSAVSIDVEGKI------FQAAIgaGISLLSITH 664
Cdd:cd03257 172 PTSALDVSVQAQIldllkkLQEEL--GLTLLFITH 204
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
498-664 4.21e-10

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: 63.43  E-value: 4.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875    498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKpppQHMFYIPQRPYMSLGSLRDQVIYPDSADDMREKGY 576
Cdd:TIGR00957  657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGhVHMK---GSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQV 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875    577 TDQ-----DLErILHSVHlyhivQREGGWDAVMdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQA 651
Cdd:TIGR00957  734 LEAcallpDLE-ILPSGD-----RTEIGEKGVN-----LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802
                          170
                   ....*....|....*...
gi 60218875    652 AIG-----AGISLLSITH 664
Cdd:TIGR00957  803 VIGpegvlKNKTRILVTH 820
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
490-639 5.00e-10

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 60.90  E-value: 5.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 490 AGEVVAsrlnfkveegmhllITGPNGCGKSSLFRILSGLWPVYEG-VLY--KP----PPQH-------MfyiPQRPYMSL 555
Cdd:COG4559  26 PGELTA--------------IIGPNGAGKSTLLKLLTGELTPSSGeVRLngRPlaawSPWElarrravL---PQHSSLAF 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 556 GSLRDQVI----YP---DSADDmrekgytDQDLERILHSVHLYHIVQReggwdavmDWKDvLSGGEKQRMGMAR------ 622
Cdd:COG4559  89 PFTVEEVValgrAPhgsSAAQD-------RQIVREALALVGLAHLAGR--------SYQT-LSGGEQQRVQLARvlaqlw 152
                       170
                ....*....|....*...
gi 60218875 623 -MFYHKPKYALLDECTSA 639
Cdd:COG4559 153 ePVDGGPRWLFLDEPTSA 170
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
491-666 5.84e-10

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: 60.48  E-value: 5.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSG-LWPVYEGVLY--------------KPppqHMFYI-P--QRPY 552
Cdd:COG1119  15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRlfgerrggedvwelRK---RIGLVsPalQLRF 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 553 MSLGSLRDQVI---YpDSADDMREkgYTDQDLER---ILHSVHLYHIVQREggwdavmdWKDvLSGGEKQRMGMARMFYH 626
Cdd:COG1119  92 PRDETVLDVVLsgfF-DSIGLYRE--PTDEQRERareLLELLGLAHLADRP--------FGT-LSQGEQRRVLIARALVK 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 60218875 627 KPKYALLDECTSavSIDVEGK-IFQAAIGA-----GISLLSITHRP 666
Cdd:COG1119 160 DPELLILDEPTA--GLDLGAReLLLALLDKlaaegAPTLVLVTHHV 203
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
476-653 1.18e-09

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: 62.24  E-value: 1.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875    476 DHGIICENVPI-ITPagevVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLykpppQH---MFYIPQRP 551
Cdd:TIGR01271  426 DDGLFFSNFSLyVTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----KHsgrISFSPQTS 496
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875    552 YMSLGSLRDQVIYPDSADDMRekgYTD-----QDLERILHSVHLYHIVQREGGWdavmdwkdVLSGGEKQRMGMARMFYH 626
Cdd:TIGR01271  497 WIMPGTIKDNIIFGLSYDEYR---YTSvikacQLEEDIALFPEKDKTVLGEGGI--------TLSGGQRARISLARAVYK 565
                          170       180
                   ....*....|....*....|....*..
gi 60218875    627 KPKYALLDECTSAVSIDVEGKIFQAAI 653
Cdd:TIGR01271  566 DADLYLLDSPFTHLDVVTEKEIFESCL 592
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
494-635 1.87e-09

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: 58.00  E-value: 1.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 494 VASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL---------YKPPPQHMFYIPQRP--YMSLgSLRDQV 562
Cdd:cd03268  15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItfdgksyqkNIEALRRIGALIEAPgfYPNL-TARENL 93
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60218875 563 IYPDsaddmREKGYTDQDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDE 635
Cdd:cd03268  94 RLLA-----RLLGIRKKRIDEVLDVVGLKDSAKKKVK---------GFSLGMKQRLGIALALLGNPDLLILDE 152
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
498-660 1.92e-09

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: 58.21  E-value: 1.92e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKP------PPQHMF-----YIPQR----PYMS------L 555
Cdd:cd03224  19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsIRFDGrditglPPHERAragigYVPEGrrifPELTveenllL 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 556 GSLRdqviypdsaddmREKGYTDQDLERILHSV-HLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLD 634
Cdd:cd03224  99 GAYA------------RRRAKRKARLERVYELFpRLKERRKQLAG---------TLSGGEQQMLAIARALMSRPKLLLLD 157
                       170       180
                ....*....|....*....|....*....
gi 60218875 635 ECTSAVSIDVEGKIFQAAIG---AGISLL 660
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRElrdEGVTIL 186
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
491-664 2.42e-09

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: 58.40  E-value: 2.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQHMFYIPQR------------PYMSLGs 557
Cdd:cd03300  12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGeILLDGKDITNLPPHKRpvntvfqnyalfPHLTVF- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 558 lrDQVIYPdsaddMREKGYTDQDL----ERILHSVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHKPKYALL 633
Cdd:cd03300  91 --ENIAFG-----LRLKKLPKAEIkervAEALDLVQLEGYANRK---------PSQLSGGQQQRVAIARALVNEPKVLLL 154
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 60218875 634 DECTSAV------SIDVEGKIFQAAIgaGISLLSITH 664
Cdd:cd03300 155 DEPLGALdlklrkDMQLELKRLQKEL--GITFVFVTH 189
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
498-676 2.98e-09

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 58.15  E-value: 2.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEG-MHLlITGPNGCGKSSLFRILSGLwPVYE---G-VLYK-------PPPQH----MFYIPQRP---------- 551
Cdd:COG0396  19 VNLTIKPGeVHA-IMGPNGSGKSTLAKVLMGH-PKYEvtsGsILLDgedilelSPDERaragIFLAFQYPveipgvsvsn 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 552 --YMSLGSLRDQVIY-PDSADDMREKGYT---DQD-LERilhSVHlyhivqrEGgwdavmdwkdvLSGGEKQRMGMARMF 624
Cdd:COG0396  97 flRTALNARRGEELSaREFLKLLKEKMKElglDEDfLDR---YVN-------EG-----------FSGGEKKRNEILQML 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 60218875 625 YHKPKYALLDECTSAVSID---VEGKIFQAAIGAGISLLSITHRPSLWKY----HTHLL 676
Cdd:COG0396 156 LLEPKLAILDETDSGLDIDalrIVAEGVNKLRSPDRGILIITHYQRILDYikpdFVHVL 214
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
498-665 3.16e-09

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: 57.42  E-value: 3.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY------KPPPQH-----MFYIPQRPYMSLGSLRDQViypD 566
Cdd:cd03369  27 VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgidiSTIPLEdlrssLTIIPQDPTLFSGTIRSNL---D 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 567 SADDmrekgYTDQDLERILhSVhlyhivqREGGwdavmdwkDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEG 646
Cdd:cd03369 104 PFDE-----YSDEEIYGAL-RV-------SEGG--------LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
                       170       180
                ....*....|....*....|..
gi 60218875 647 KIfQAAIG---AGISLLSITHR 665
Cdd:cd03369 163 LI-QKTIReefTNSTILTIAHR 183
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
494-653 4.81e-09

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: 58.33  E-value: 4.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 494 VASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLykpppQH---MFYIPQRPYMSLGSLRDQVIYPDSADD 570
Cdd:cd03291  52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----KHsgrISFSSQFSWIMPGTIKENIIFGVSYDE 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 571 MREKGYTD--QDLERILHSVHLYHIVQREGGWdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKI 648
Cdd:cd03291 127 YRYKSVVKacQLEEDITKFPEKDNTVLGEGGI--------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198

                ....*
gi 60218875 649 FQAAI 653
Cdd:cd03291 199 FESCV 203
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
510-666 5.31e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 57.75  E-value: 5.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  510 ITGPNGCGKSSLFRILSGLWPVYEG-------VLY-------------KPPPQHMFYIPQrPYMSLgSLRDQVIYPDSAD 569
Cdd:PRK14246  41 IMGPSGSGKSTLLKVLNRLIEIYDSkikvdgkVLYfgkdifqidaiklRKEVGMVFQQPN-PFPHL-SIYDNIAYPLKSH 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  570 DMREKGYTDQDLERILHSVHLYHIVqreggWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSI----DVE 645
Cdd:PRK14246 119 GIKEKREIKKIVEECLRKVGLWKEV-----YDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIvnsqAIE 193
                        170       180
                 ....*....|....*....|.
gi 60218875  646 GKIFQaaIGAGISLLSITHRP 666
Cdd:PRK14246 194 KLITE--LKNEIAIVIVSHNP 212
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
498-664 5.78e-09

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: 56.04  E-value: 5.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLwpvyegvlykpppqhmfyipQRPYMSLGSLRDQVIYPDSADDMREK--- 574
Cdd:cd03229  19 VSLNIEAGEIVALLGPSGSGKSTLLRCIAGL--------------------EEPDSGSILIDGEDLTDLEDELPPLRrri 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 575 GYTDQDLERILH-SVhlyhivqreggWDAVMdwkDVLSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDVEGKI-FQAA 652
Cdd:cd03229  79 GMVFQDFALFPHlTV-----------LENIA---LGLSGGQQQRVALARALAMDPDVLLLDEPTSA--LDPITRReVRAL 142
                       170
                ....*....|....*..
gi 60218875 653 I-----GAGISLLSITH 664
Cdd:cd03229 143 LkslqaQLGITVVLVTH 159
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
488-668 7.68e-09

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 56.59  E-value: 7.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 488 TPAGEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY--------KPPPQ-------HMFYIPQR- 550
Cdd:COG1136  16 TGEGEVTAlRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdissLSERElarlrrrHIGFVFQFf 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 551 ---PYMSLgslRDQVIYP-----DSADDMREKgytdqdLERILHSVHLYHIvqreggwdavMDWK-DVLSGGEKQRMGMA 621
Cdd:COG1136  96 nllPELTA---LENVALPlllagVSRKERRER------ARELLERVGLGDR----------LDHRpSQLSGGQQQRVAIA 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 60218875 622 RMFYHKPKYALLDECTSAV----SIDVEGKIFQAAIGAGISLLSITHRPSL 668
Cdd:COG1136 157 RALVNRPKLILADEPTGNLdsktGEEVLELLRELNRELGTTIVMVTHDPEL 207
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
491-639 7.72e-09

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 58.42  E-value: 7.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPPQH-----------MFyipqrPY 552
Cdd:PRK09452  26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMldgqditHVPAENrhvntvfqsyaLF-----PH 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  553 MSLgslRDQVIYpdsadDMREKGYTDQDLER----ILHSVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHKP 628
Cdd:PRK09452 101 MTV---FENVAF-----GLRMQKTPAAEITPrvmeALRMVQLEEFAQRK---------PHQLSGGQQQRVAIARAVVNKP 163
                        170
                 ....*....|.
gi 60218875  629 KYALLDECTSA 639
Cdd:PRK09452 164 KVLLLDESLSA 174
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
479-637 9.11e-09

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: 54.76  E-value: 9.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 479 IICENVPIITPaGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQrpymslgsl 558
Cdd:cd03221   1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60218875 559 rdqviypdsaddmrekgytdqdlerilhsvhlyhivqreggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECT 637
Cdd:cd03221  71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
496-666 9.88e-09

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 55.97  E-value: 9.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  496 SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPP---------QHMFYIPQRPymslGslrdqvIYP 565
Cdd:PRK13538  18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGeVLWQGEPirrqrdeyhQDLLYLGHQP----G------IKT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  566 D-SAddmrekgytdqdLE--RILHSVHlyHIVQREGGWDA-----VMDWKDV----LSGGEKQRMGMARMFYHKPKYALL 633
Cdd:PRK13538  88 ElTA------------LEnlRFYQRLH--GPGDDEALWEAlaqvgLAGFEDVpvrqLSAGQQRRVALARLWLTRAPLWIL 153
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 60218875  634 DECTSAvsIDVEG-KIFQAAIGA-----GISLLSiTHRP 666
Cdd:PRK13538 154 DEPFTA--IDKQGvARLEALLAQhaeqgGMVILT-THQD 189
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
498-671 2.18e-08

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: 54.84  E-value: 2.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLwPVYE----GVLYKP------PPQH-----MFYIPQRPymslgslrdqv 562
Cdd:cd03217  19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEvtegEILFKGeditdlPPEErarlgIFLAFQYP----------- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 563 iypdsaddMREKGYTDQDLERILHsvhlyhivqrEGgwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSI 642
Cdd:cd03217  87 --------PEIPGVKNADFLRYVN----------EG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
                       170       180       190
                ....*....|....*....|....*....|..
gi 60218875 643 D---VEGKIFQAAIGAGISLLSITHRPSLWKY 671
Cdd:cd03217 138 DalrLVAEVINKLREEGKSVLIITHYQRLLDY 169
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
491-635 3.15e-08

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 56.38  E-value: 3.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG--VL----------YKPPPQHMFyipQR----PYMS 554
Cdd:PRK11607  31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGqiMLdgvdlshvppYQRPINMMF---QSyalfPHMT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  555 LgslrDQVIYPDSADDMREKGYTDQDLERILHSVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHKPKYALLD 634
Cdd:PRK11607 108 V----EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRK---------PHQLSGGQRQRVALARSLAKRPKLLLLD 174

                 .
gi 60218875  635 E 635
Cdd:PRK11607 175 E 175
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
490-676 3.50e-08

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 54.16  E-value: 3.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  490 AGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQR-------PY-----MSLGS 557
Cdd:NF040873   3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRsevpdslPLtvrdlVAMGR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  558 LRDQVIY-PDSADDMREkgyTDQDLERilhsVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHKPKYALLDEC 636
Cdd:NF040873  83 WARRGLWrRLTRDDRAA---VDDALER----VGLADLAGRQ---------LGELSGGQRQRALLAQGLAQEADLLLLDEP 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 60218875  637 TSAVSIDVEGKIFQ---AAIGAGISLLSITHRPSLWKYHTHLL 676
Cdd:NF040873 147 TTGLDAESRERIIAllaEEHARGATVVVVTHDLELVRRADPCV 189
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
492-665 6.21e-08

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: 53.09  E-value: 6.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 492 EVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPPP-------QHMFYIPQRPYMSLGSLRDQ 561
Cdd:cd03247  15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITldgVPVSdlekalsSLISVLNQRPYLFDTTLRNN 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 562 VIYPdsaddmrekgytdqdlerilhsvhlyhivqreggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTsaVS 641
Cdd:cd03247  95 LGRR--------------------------------------------FSGGERQRLALARILLQDAPIVLLDEPT--VG 128
                       170       180       190
                ....*....|....*....|....*....|
gi 60218875 642 IDVEGK------IFQAAigAGISLLSITHR 665
Cdd:cd03247 129 LDPITErqllslIFEVL--KDKTLIWITHH 156
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
496-684 9.55e-08

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: 53.49  E-value: 9.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 496 SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPPPQHMF------------YIPQRPYMSLGSLRD 560
Cdd:cd03290  18 SNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnKNESEPSFeatrsrnrysvaYAAQKPWLLNATVEE 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 561 QVIYPDSADDMREKGYTDQ-----DLERILHSVhlyhivQREGGWDAVMdwkdvLSGGEKQRMGMARMFYHKPKYALLDE 635
Cdd:cd03290  98 NITFGSPFNKQRYKAVTDAcslqpDIDLLPFGD------QTEIGERGIN-----LSGGQRQRICVARALYQNTNIVFLDD 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 60218875 636 CTSAVSIDVEGKIFQAAIgagISLLSITHRPSLWKyhTHLLQFDGEGGW 684
Cdd:cd03290 167 PFSALDIHLSDHLMQEGI---LKFLQDDKRTLVLV--THKLQYLPHADW 210
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
512-648 9.67e-08

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 54.01  E-value: 9.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  512 GPNGCGKSSLFRIL---SGLWP---VYEGVLYKpppQHMFYIP---------------QRPYMSLGSLRDQVIYPDSADD 570
Cdd:PRK14239  38 GPSGSGKSTLLRSInrmNDLNPevtITGSIVYN---GHNIYSPrtdtvdlrkeigmvfQQPNPFPMSIYENVVYGLRLKG 114
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60218875  571 MREKGYTDQDLERILHSVHLYHIVQreggwDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKI 648
Cdd:PRK14239 115 IKDKQVLDEAVEKSLKGASIWDEVK-----DRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKI 187
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
498-664 1.02e-07

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: 53.62  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGL-WPVYEGVLYK------PPPQHMFYIPQRPYMSLGSLRDQV-IYPDSAD 569
Cdd:TIGR01184   4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEgkqitePGPDRMVVFQNYSLLPWLTVRENIaLAVDRVL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   570 DMREKGYTDQDLERILHSVHLYHivqreggwdAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSI----DVE 645
Cdd:TIGR01184  84 PDLSKSERRAIVEEHIALVGLTE---------AADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgNLQ 154
                         170
                  ....*....|....*....
gi 60218875   646 GKIFQAAIGAGISLLSITH 664
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTH 173
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
489-667 1.06e-07

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: 55.11  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   489 PAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG--VLYKPPPQHMfyipqrpymSLGSLRDQV---- 562
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGqiLLDGHDLADY---------TLASLRRQValvs 412
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   563 ----IYPDS-ADDM---REKGYTDQDLERILHSVHLYHIVQR-EGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYAL 632
Cdd:TIGR02203 413 qdvvLFNDTiANNIaygRTEQADRAEIERALAAAYAQDFVDKlPLGLDTPIGENGVlLSGGQRQRLAIARALLKDAPILI 492
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 60218875   633 LDECTSAVSIDVEGKIfQAAIGA---GISLLSITHRPS 667
Cdd:TIGR02203 493 LDEATSALDNESERLV-QAALERlmqGRTTLVIAHRLS 529
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
493-681 1.06e-07

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 53.84  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  493 VVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYMSLGSLRDQVIYPD--SADD 570
Cdd:PRK10253  21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdiTVQE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  571 MREKG-YTDQDL---ERILHSVHLYHIVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAV----SI 642
Cdd:PRK10253 101 LVARGrYPHQPLftrWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLdishQI 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 60218875  643 DVEGKIFQAAIGAGISLLSITHR-PSLWKYHTHLLQF-DGE 681
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALrEGK 221
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
491-635 1.51e-07

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: 53.12  E-value: 1.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVA-SRLNFKVEEG-MHLLItGPNGCGKSSLFRILSGLWPVYEG-VLYK-------PPPQ--HM-----FYIPQ---- 549
Cdd:COG0411  15 GGLVAvDDVSLEVERGeIVGLI-GPNGAGKTTLFNLITGFYRPTSGrILFDgrditglPPHRiaRLgiartFQNPRlfpe 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 550 --------------RPYMSLGSLRDQVIYPDSADDMREKGytdqdlERILHSVHLYHIVQREGGwdavmdwkdVLSGGEK 615
Cdd:COG0411  94 ltvlenvlvaaharLGRGLLAALLRLPRARREEREARERA------EELLERVGLADRADEPAG---------NLSYGQQ 158
                       170       180
                ....*....|....*....|
gi 60218875 616 QRMGMARMFYHKPKYALLDE 635
Cdd:COG0411 159 RRLEIARALATEPKLLLLDE 178
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
491-635 1.98e-07

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 54.30  E-value: 1.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQ-RPYMSLG-SLRDQVIypDSA 568
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQhQEELDPDkTVLDELR--DGA 404
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60218875 569 DDMREK---GYtdqdLERILHSvhlyhivqregGWDAvmdWK--DVLSGGEKQRMGMARMFYHKPKYALLDE 635
Cdd:COG0488 405 PGGTEQevrGY----LGRFLFS-----------GDDA---FKpvGVLSGGEKARLALAKLLLSPPNVLLLDE 458
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
466-635 2.18e-07

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 52.76  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  466 LAIKGTVIDVDHGIICENVPIITPAGEVVAsrlnfkveegmhllITGPNGCGKSSLFRILSGLWPVYEGVLykpppqhmf 545
Cdd:PRK11247  13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVA--------------VVGRSGCGKSTLLRLLAGLETPSAGEL--------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  546 yipqrpymslgsLRDQVIYPDSADDMREKgYTDQDL---ERILHSVHLyhivQREGGW--------DAV------MDWKD 608
Cdd:PRK11247  70 ------------LAGTAPLAEAREDTRLM-FQDARLlpwKKVIDNVGL----GLKGQWrdaalqalAAVgladraNEWPA 132
                        170       180
                 ....*....|....*....|....*..
gi 60218875  609 VLSGGEKQRMGMARMFYHKPKYALLDE 635
Cdd:PRK11247 133 ALSGGQKQRVALARALIHRPGLLLLDE 159
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
491-665 3.04e-07

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: 53.98  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPP----------QHMFYIPQRPYMSLGSLR 559
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGeILLNGFSlkdidrhtlrQFINYLPQEPYIFSGSIL 565
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   560 DQVIYPDsaddmrEKGYTDQDLERILHSVHLY-HIVQREGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALLDECT 637
Cdd:TIGR01193 566 ENLLLGA------KENVSQDEIWAACEIAEIKdDIENMPLGYQTELSEEGSsISGGQKQRIALARALLTDSKVLILDEST 639
                         170       180
                  ....*....|....*....|....*...
gi 60218875   638 SAVSIDVEGKIFQaaigagiSLLSITHR 665
Cdd:TIGR01193 640 SNLDTITEKKIVN-------NLLNLQDK 660
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
479-637 3.29e-07

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 51.59  E-value: 3.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 479 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhMF-----YIPQR--P 551
Cdd:COG2884   2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVL------VNgqdlsRLKRReiP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 552 YM--SLG------------SLRDQVIYPdsaddMREKGYTDQDLER----ILHSVHLYHivqreggwdavmdwK-----D 608
Cdd:COG2884  76 YLrrRIGvvfqdfrllpdrTVYENVALP-----LRVTGKSRKEIRRrvreVLDLVGLSD--------------KakalpH 136
                       170       180
                ....*....|....*....|....*....
gi 60218875 609 VLSGGEKQRMGMARMFYHKPKYALLDECT 637
Cdd:COG2884 137 ELSGGEQQRVAIARALVNRPELLLADEPT 165
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
480-639 3.32e-07

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 52.08  E-value: 3.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  480 ICENVPIITPAGEVVAsrlnfkveegmhllITGPNGCGKSSLFRILSGLWPVYEG-VLY--KP----PPQHMFYI----P 548
Cdd:PRK13548  17 LLDDVSLTLRPGEVVA--------------ILGPNGAGKSTLLRALSGELSPDSGeVRLngRPladwSPAELARRravlP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  549 QRPYMSLGSLRDQVI----YPDSaddmREKGYTDQDLERILHSVHLYHIVQReggwdavmdwkDV--LSGGEKQRMGMAR 622
Cdd:PRK13548  83 QHSSLSFPFTVEEVVamgrAPHG----LSRAEDDALVAAALAQVDLAHLAGR-----------DYpqLSGGEQQRVQLAR 147
                        170       180
                 ....*....|....*....|...
gi 60218875  623 MF------YHKPKYALLDECTSA 639
Cdd:PRK13548 148 VLaqlwepDGPPRWLLLDEPTSA 170
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
479-667 4.11e-07

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 53.48  E-value: 4.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  479 IICENVPIITPAGEVVASR-LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhMFYIPQRPYmSLGS 557
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRnINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIL------LDGHDLRDY-TLAS 414
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  558 LRDQV--------IYPDS-ADDM---REKGYTDQDLERILHSVH-LYHIVQREGGWDAVMDWKDV-LSGGEKQRMGMARM 623
Cdd:PRK11176 415 LRNQValvsqnvhLFNDTiANNIayaRTEQYSREQIEEAARMAYaMDFINKMDNGLDTVIGENGVlLSGGQRQRIAIARA 494
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 60218875  624 FYHKPKYALLDECTSAVSIDVEGKIfQAAIGA---GISLLSITHRPS 667
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAI-QAALDElqkNRTSLVIAHRLS 540
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
487-664 5.38e-07

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 50.94  E-value: 5.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 487 ITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSG-LWPV--YEGVLY--------KPPPQ-HMFYIPQR---- 550
Cdd:COG4136   9 ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLlngrrltaLPAEQrRIGILFQDdllf 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 551 PYMSLG-------------SLRDQVIypdsaddmrekgytdqdlERILHSVHLYHIVQReggwdavmdwkDV--LSGGEK 615
Cdd:COG4136  89 PHLSVGenlafalpptigrAQRRARV------------------EQALEEAGLAGFADR-----------DPatLSGGQR 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 60218875 616 QRMGMARMFYHKPKYALLDECTS----AVSIDVEGKIFQAAIGAGISLLSITH 664
Cdd:COG4136 140 ARVALLRALLAEPRALLLDEPFSkldaALRAQFREFVFEQIRQRGIPALLVTH 192
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
498-667 6.08e-07

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: 52.90  E-value: 6.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGlwpvyegvlykpppqhmFYIPQ-----------RPYmSLGSLRDQV-IYP 565
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFR-----------------FYDVTsgrilidgqdiRDV-TQASLRAAIgIVP 438
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 566 -DSA---DDMREK-GY-----TDQDLERILHSVHLYHIVQR-EGGWDAVmdwkdV------LSGGEKQRMGMARMFYHKP 628
Cdd:COG5265 439 qDTVlfnDTIAYNiAYgrpdaSEEEVEAAARAAQIHDFIESlPDGYDTR-----VgerglkLSGGEKQRVAIARTLLKNP 513
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 60218875 629 KYALLDECTSAVSIDVEGKIfQAA---IGAGISLLSITHRPS 667
Cdd:COG5265 514 PILIFDEATSALDSRTERAI-QAAlreVARGRTTLVIAHRLS 554
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
493-664 6.83e-07

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: 50.90  E-value: 6.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 493 VVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY----------KPPPQHMFYipqrpymslgsLRDQ 561
Cdd:COG4778  25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsILVrhdggwvdlaQASPREILA-----------LRRR 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 562 VIypdsaddmrekGYTDQDLeRILHSVHLYHIVQ---REGGWD---AVMDWKDVL-----------------SGGEKQRM 618
Cdd:COG4778  94 TI-----------GYVSQFL-RVIPRVSALDVVAeplLERGVDreeARARARELLarlnlperlwdlppatfSGGEQQRV 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 60218875 619 GMARMFYHKPKYALLDECTSavSIDVEGK-----IFQAAIGAGISLLSITH 664
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTA--SLDAANRavvveLIEEAKARGTAIIGIFH 210
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
498-664 7.18e-07

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 51.55  E-value: 7.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLykpppqhmfyipqrpymslgSLRDQVIYPDSADDMREK--- 574
Cdd:PRK13635  26 VSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI--------------------TVGGMVLSEETVWDVRRQvgm 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  575 ----------GYTDQD----------------LERI---LHSVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFY 625
Cdd:PRK13635  86 vfqnpdnqfvGATVQDdvafglenigvpreemVERVdqaLRQVGMEDFLNRE---------PHRLSGGQKQRVAIAGVLA 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 60218875  626 HKPKYALLDECTSAVS----IDVEGKIFQAAIGAGISLLSITH 664
Cdd:PRK13635 157 LQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITH 199
cbiO PRK13642
energy-coupling factor transporter ATPase;
498-664 7.24e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 51.63  E-value: 7.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY----KPPPQHMFYIPQRPYMSLGSLRDQVIYPDSADD--- 570
Cdd:PRK13642  26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKidgeLLTAENVWNLRRKIGMVFQNPDNQFVGATVEDDvaf 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  571 -MREKGYTDQDL----ERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDVE 645
Cdd:PRK13642 106 gMENQGIPREEMikrvDEALLAVNMLDFKTREPA---------RLSGGQKQRVAVAGIIALRPEIIILDESTSM--LDPT 174
                        170       180
                 ....*....|....*....|....*
gi 60218875  646 GK------IFQAAIGAGISLLSITH 664
Cdd:PRK13642 175 GRqeimrvIHEIKEKYQLTVLSITH 199
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
491-664 9.69e-07

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 50.66  E-value: 9.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  491 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV------------LYKPPPQHMFYIPQRPYMslgsL 558
Cdd:PRK10895  15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddedisllpLHARARRGIGYLPQEASI----F 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  559 RDQVIYPD--SADDMREKGYTDQDLER---ILHSVHLYHIVQREGgwdavmdwkDVLSGGEKQRMGMARMFYHKPKYALL 633
Cdd:PRK10895  91 RRLSVYDNlmAVLQIRDDLSAEQREDRaneLMEEFHIEHLRDSMG---------QSLSGGERRRVEIARALAANPKFILL 161
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 60218875  634 DECTSAVS----IDVEgKIFQAAIGAGISLLSITH 664
Cdd:PRK10895 162 DEPFAGVDpisvIDIK-RIIEHLRDSGLGVLITDH 195
cbiO PRK13650
energy-coupling factor transporter ATPase;
498-664 1.05e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 50.89  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY----KPPPQHMFYIPQRPYMSLGSLRDQVIYPDSADD--- 570
Cdd:PRK13650  26 VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIidgdLLTEENVWDIRHKIGMVFQNPDNQFVGATVEDDvaf 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  571 -MREKGYTDQDL-ERILHSVHLYhivqreggwdAVMDWKDV----LSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDV 644
Cdd:PRK13650 106 gLENKGIPHEEMkERVNEALELV----------GMQDFKEReparLSGGQKQRVAIAGAVAMRPKIIILDEATSM--LDP 173
                        170       180
                 ....*....|....*....|....*...
gi 60218875  645 EGKifQAAIGA--------GISLLSITH 664
Cdd:PRK13650 174 EGR--LELIKTikgirddyQMTVISITH 199
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
463-667 1.36e-06

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 51.64  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  463 SDTLAIKGTVIDVDhgiiceNVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppq 542
Cdd:PRK10790 331 NDDRPLQSGRIDID------NVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR----- 399
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  543 hmfyIPQRPYMSL--GSLR--------DQVIYPDS--ADDMREKGYTDQDLERILHSVHLYHIVQR--EGGWDAVMDWKD 608
Cdd:PRK10790 400 ----LDGRPLSSLshSVLRqgvamvqqDPVVLADTflANVTLGRDISEEQVWQALETVQLAELARSlpDGLYTPLGEQGN 475
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60218875  609 VLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPS 667
Cdd:PRK10790 476 NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAlaAVREHTTLVVIAHRLS 536
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
490-635 1.61e-06

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: 49.85  E-value: 1.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 490 AGEVVAsrlnfkveegmhLLitGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPPQH-----MFYIPQRP--YMSL 555
Cdd:cd03218  25 QGEIVG------------LL--GPNGAGKTTTFYMIVGLVKPDSGKILldgqditKLPMHKrarlgIGYLPQEAsiFRKL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 556 gSLRDQVIypdSADDMREKGYTDQD--LERILHSVHLYHIVQREGgwdavmdwkDVLSGGEKQRMGMARMFYHKPKYALL 633
Cdd:cd03218  91 -TVEENIL---AVLEIRGLSKKEREekLEELLEEFHITHLRKSKA---------SSLSGGERRRVEIARALATNPKFLLL 157

                ..
gi 60218875 634 DE 635
Cdd:cd03218 158 DE 159
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
492-679 1.69e-06

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: 51.87  E-value: 1.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875    492 EVVASRLNFKVEEGMHLLITGPNGCGKSS----LFRILSGLWP--VYEGVLYKPPPQH-----MFYIPQRPYMSLGSLRD 560
Cdd:TIGR00957 1299 DLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINESAEGeiIIDGLNIAKIGLHdlrfkITIIPQDPVLFSGSLRM 1378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875    561 QvIYPDSAddmrekgYTDQDLERILHSVHLYHIVQR----------EGGwdavmdwkDVLSGGEKQRMGMARMFYHKPKY 630
Cdd:TIGR00957 1379 N-LDPFSQ-------YSDEEVWWALELAHLKTFVSAlpdkldhecaEGG--------ENLSVGQRQLVCLARALLRKTKI 1442
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 60218875    631 ALLDECTSAVSIDVEGKIfQAAIGAGI---SLLSITHRPSLWKYHTHLLQFD 679
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLI-QSTIRTQFedcTVLTIAHRLNTIMDYTRVIVLD 1493
cbiO PRK13640
energy-coupling factor transporter ATPase;
494-664 2.18e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 50.18  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  494 VASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGL-----------------------WPVYE--GVLYKPPPQHMfyip 548
Cdd:PRK13640  22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnskitvdgitltaktvWDIREkvGIVFQNPDNQF---- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  549 qrpymsLGSlrdqVIYPDSADDMREKGYTDQDLERILHSVhlyhiVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKP 628
Cdd:PRK13640  98 ------VGA----TVGDDVAFGLENRAVPRPEMIKIVRDV-----LADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 60218875  629 KYALLDECTSAvsIDVEGK------IFQAAIGAGISLLSITH 664
Cdd:PRK13640 163 KIIILDESTSM--LDPAGKeqilklIRKLKKKNNLTVISITH 202
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
479-640 2.53e-06

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: 49.49  E-value: 2.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 479 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhmFY---IPQRPYMSL 555
Cdd:cd03256   1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL-------IDgtdINKLKGKAL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 556 GSLRDQViypdsaddmrekGYTDQD---------LERILHS-----------VHLYHIVQREGGWDAV----MDWK---- 607
Cdd:cd03256  74 RQLRRQI------------GMIFQQfnlierlsvLENVLSGrlgrrstwrslFGLFPKEEKQRALAALervgLLDKayqr 141
                       170       180       190
                ....*....|....*....|....*....|....
gi 60218875 608 -DVLSGGEKQRMGMARMFYHKPKYALLDECTSAV 640
Cdd:cd03256 142 aDQLSGGQQQRVAIARALMQQPKLILADEPVASL 175
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
498-680 3.23e-06

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 48.69  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPP-----PQHMFYIPQrpymsLGSLRdqviypdsad 569
Cdd:PRK13543  30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQidgKTAtrgdrSRFMAYLGH-----LPGLK---------- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  570 dmrekgytdQDLERI--LH---SVHLYHIVQREGGWDAVM---DWKDV----LSGGEKQRMGMARMFYHKPKYALLDEct 637
Cdd:PRK13543  95 ---------ADLSTLenLHflcGLHGRRAKQMPGSALAIVglaGYEDTlvrqLSAGQKKRLALARLWLSPAPLWLLDE-- 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 60218875  638 SAVSIDVEG-----KIFQAAIGAGISLLSITH--RPSLwKYHTHLLQFDG 680
Cdd:PRK13543 164 PYANLDLEGitlvnRMISAHLRGGGAALVTTHgaYAAP-PVRTRMLTLEA 212
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
498-679 4.91e-06

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 49.96  E-value: 4.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  498 LNFKVEEGMHLLITGPNGCGKSSLFRILsglwpvyegvlykpppqHMFYIPQRPY----------MSLGSLRDQ--VIYP 565
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLL-----------------QRVFDPQSGRilidgtdirtVTRASLRRNiaVVFQ 416
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  566 DS-------ADDMR--EKGYTDQDLERILHSVH-LYHIVQREGGWDAVMDWK-DVLSGGEKQRMGMARMFYHKPKYALLD 634
Cdd:PRK13657 417 DAglfnrsiEDNIRvgRPDATDEEMRAAAERAQaHDFIERKPDGYDTVVGERgRQLSGGERQRLAIARALLKDPPILILD 496
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 60218875  635 ECTSAVSIDVEGKIfQAAIGA---GISLLSITHRPSLWKYHTHLLQFD 679
Cdd:PRK13657 497 EATSALDVETEAKV-KAALDElmkGRTTFIIAHRLSTVRNADRILVFD 543
PLN03232 PLN03232
ABC transporter C family member; Provisional
496-657 6.95e-06

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 49.59  E-value: 6.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   496 SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYE--GVLYKpppQHMFYIPQRPYMSLGSLRDQVIYpdSADDMRE 573
Cdd:PLN03232  634 SDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtsSVVIR---GSVAYVPQVSWIFNATVRENILF--GSDFESE 708
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   574 KGYTDQDLERILHSVHLYHIVQR-EGGWDAVMdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQAA 652
Cdd:PLN03232  709 RYWRAIDVTALQHDLDLLPGRDLtEIGERGVN-----ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSC 783

                  ....*
gi 60218875   653 IGAGI 657
Cdd:PLN03232  784 MKDEL 788
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
489-635 8.78e-06

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: 47.67  E-value: 8.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 489 PAGEVVAsrlnfkveegmhlLItGPNGCGKSSLFRILSGLWPVYEG-VLYK-------PPPQ----HMFYIPQR----PY 552
Cdd:COG0410  27 EEGEIVA-------------LL-GRNGAGKTTLLKAISGLLPPRSGsIRFDgeditglPPHRiarlGIGYVPEGrrifPS 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 553 MS------LGSLRdqviypdsaddMREKGYTDQDLERILHSV-HLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFY 625
Cdd:COG0410  93 LTveenllLGAYA-----------RRDRAEVRADLERVYELFpRLKERRRQRAG---------TLSGGEQQMLAIGRALM 152
                       170
                ....*....|
gi 60218875 626 HKPKYALLDE 635
Cdd:COG0410 153 SRPKLLLLDE 162
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
498-668 8.95e-06

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 47.56  E-value: 8.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGlwpvyegvLYKPPPQHMFY-------IPQR--PYM--SLGS-------LR 559
Cdd:PRK10908  21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICG--------IERPSAGKIWFsghditrLKNRevPFLrrQIGMifqdhhlLM 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  560 DQVIYPDSADDMREKGYTDQDLERILHSVhlyhiVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECT-- 637
Cdd:PRK10908  93 DRTVYDNVAIPLIIAGASGDDIRRRVSAA-----LDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTgn 167
                        170       180       190
                 ....*....|....*....|....*....|...
gi 60218875  638 --SAVSIDVEgKIFQAAIGAGISLLSITHRPSL 668
Cdd:PRK10908 168 ldDALSEGIL-RLFEEFNRVGVTVLMATHDIGL 199
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
477-667 9.83e-06

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: 46.78  E-value: 9.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 477 HGIICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGL--WPVYEG-VLYKPPPQHMFyipqrpym 553
Cdd:cd03213   7 RNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGeVLINGRPLDKR-------- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 554 slgSLRDQViypdsaddmrekGYTDQDLerILHS---VH--LYHIVQREGgwdavmdwkdvLSGGEKQRMGMARMFYHKP 628
Cdd:cd03213  79 ---SFRKII------------GYVPQDD--ILHPtltVRetLMFAAKLRG-----------LSGGERKRVSIALELVSNP 130
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 60218875 629 KYALLDECTS------AVSIdveGKIFQAAIGAGISLLSITHRPS 667
Cdd:cd03213 131 SLLFLDEPTSgldsssALQV---MSLLRRLADTGRTIICSIHQPS 172
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
497-686 1.05e-05

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: 48.78  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   497 RLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQrpymSLGSLRD-----QVIyPDSADDM 571
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQ----SRDALDPnktvwEEI-SGGLDII 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   572 REKGY---------------TDQdlerilhsvhlyhivQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDEC 636
Cdd:TIGR03719 415 KLGKReipsrayvgrfnfkgSDQ---------------QKKVG---------QLSGGERNRVHLAKTLKSGGNVLLLDEP 470
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 60218875   637 TSavSIDVEG-KIFQAAIG--AGISLLsITH-RPSLWKYHTHLLQFDGEGGWRF 686
Cdd:TIGR03719 471 TN--DLDVETlRALEEALLnfAGCAVV-ISHdRWFLDRIATHILAFEGDSHVEW 521
PLN03232 PLN03232
ABC transporter C family member; Provisional
498-665 1.07e-05

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 49.20  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL-----------YKPPPQHMFYIPQRPYMSLGSLRDQViypd 566
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRImiddcdvakfgLTDLRRVLSIIPQSPVLFSGTVRFNI---- 1330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   567 saDDMREkgYTDQDLERILHSVHLYHIVQREG-GWDA-VMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDV 644
Cdd:PLN03232 1331 --DPFSE--HNDADLWEALERAHIKDVIDRNPfGLDAeVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
                         170       180
                  ....*....|....*....|....
gi 60218875   645 EGKIfQAAIGA---GISLLSITHR 665
Cdd:PLN03232 1407 DSLI-QRTIREefkSCTMLVIAHR 1429
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
488-639 1.32e-05

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: 47.19  E-value: 1.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 488 TPAGEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY-------------KPPPQHMFYIPQRpY 552
Cdd:cd03258  13 DTGGKVTAlKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGsVLVdgtdltllsgkelRKARRRIGMIFQH-F 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 553 MSLGSL--RDQVIYPDSADDMrEKGYTDQDLERILHSVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYHKPKY 630
Cdd:cd03258  92 NLLSSRtvFENVALPLEIAGV-PKAEIEERVLELLELVGLEDKADA---------YPAQLSGGQKQRVGIARALANNPKV 161

                ....*....
gi 60218875 631 ALLDECTSA 639
Cdd:cd03258 162 LLCDEATSA 170
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
488-638 1.92e-05

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: 48.37  E-value: 1.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875    488 TPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLF----RILSGLWPV------YEGVLYKPPPQHMFYIPQRPYMSLGS 557
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLSTEGEIqidgvsWNSVTLQTWRKAFGVIPQKVFIFSGT 1307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875    558 LRDQViypdsadDMREKgYTDQDLERILHSVHLYHIV-QREGGWDAVM-DWKDVLSGGEKQRMGMARMFYHKPKYALLDE 635
Cdd:TIGR01271 1308 FRKNL-------DPYEQ-WSDEEIWKVAEEVGLKSVIeQFPDKLDFVLvDGGYVLSNGHKQLMCLARSILSKAKILLLDE 1379

                   ...
gi 60218875    636 CTS 638
Cdd:TIGR01271 1380 PSA 1382
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
492-637 2.07e-05

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: 46.56  E-value: 2.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 492 EVVASR-LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-------VLYKPPPQHMFYIP----QR--------P 551
Cdd:cd03267  33 EVEALKgISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGevrvaglVPWKRRKKFLRRIGvvfgQKtqlwwdlpV 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 552 YMSLGSLRDqvIY--PDSADDMREKGYTDQ-DLERILHSVhlyhiVQReggwdavmdwkdvLSGGEKQRMGMARMFYHKP 628
Cdd:cd03267 113 IDSFYLLAA--IYdlPPARFKKRLDELSELlDLEELLDTP-----VRQ-------------LSLGQRMRAEIAAALLHEP 172

                ....*....
gi 60218875 629 KYALLDECT 637
Cdd:cd03267 173 EILFLDEPT 181
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
498-639 2.48e-05

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: 45.98  E-value: 2.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-------VLYKPPP------QHMFYIPQR----PYMSLgsLRD 560
Cdd:cd03262  19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtiiidglKLTDDKKninelrQKVGMVFQQfnlfPHLTV--LEN 96
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60218875 561 QVIYPdsaddMREKGYTDQDLERILhsvhlYHIVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSA 639
Cdd:cd03262  97 ITLAP-----IKVKGMSKAEAEERA-----LELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
510-653 4.32e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 45.77  E-value: 4.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  510 ITGPNGCGKSSLFRILSGLW-PVYEGVLYKPPP-----QHMFYIPQRPYMSLGSLRDQVIYPDSADD----MREKGYTDQ 579
Cdd:PRK13638  32 LVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKPldyskRGLLALRQQVATVFQDPEQQIFYTDIDSDiafsLRNLGVPEA 111
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60218875  580 DLER----ILHSVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDVEGKIFQAAI 653
Cdd:PRK13638 112 EITRrvdeALTLVDAQHFRHQP---------IQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG--LDPAGRTQMIAI 178
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
488-635 4.92e-05

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: 45.62  E-value: 4.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 488 TPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLF----RILSGLWPV-YEGVLYKPPPQHMF-----YIPQRPYMSLGS 557
Cdd:cd03289  13 TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLNTEGDIqIDGVSWNSVPLQKWrkafgVIPQKVFIFSGT 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 558 LRDQViypdsadDMREKgYTDQDLERILHSVHLYHIV-QREGGWDAVM-DWKDVLSGGEKQRMGMARMFYHKPKYALLDE 635
Cdd:cd03289  93 FRKNL-------DPYGK-WSDEEIWKVAEEVGLKSVIeQFPGQLDFVLvDGGCVLSHGHKQLMCLARSVLSKAKILLLDE 164
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
451-527 5.00e-05

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 46.55  E-value: 5.00e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60218875  451 HSKRGGNLELPLSDTLAIKGTVIDVDHGIICENVpIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSG 527
Cdd:PRK10938 233 HSEQLEGVQLPEPDEPSARHALPANEPRIVLNNG-VVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
488-528 7.19e-05

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 45.07  E-value: 7.19e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 60218875 488 TPAGEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGL 528
Cdd:COG1134  34 TRREEFWAlKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI 75
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
478-648 7.42e-05

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 45.26  E-value: 7.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  478 GIICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG---VLYKPPPQHM-----FYIPQ 549
Cdd:PRK15056   6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGkisILGQPTRQALqknlvAYVPQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  550 RPYM--SLGSLRDQVIYPDSADDM----REKGYTDQDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARM 623
Cdd:PRK15056  86 SEEVdwSFPVLVEDVVMMGRYGHMgwlrRAKKRDRQIVTAALARVDMVEFRHRQIG---------ELSGGQKKRVFLARA 156
                        170       180
                 ....*....|....*....|....*
gi 60218875  624 FYHKPKYALLDECTSAVSIDVEGKI 648
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARI 181
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
497-647 7.82e-05

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: 44.42  E-value: 7.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 497 RLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY----------KPPPQHMFYIPQrpymslgslrDQVIYPD 566
Cdd:cd03263  20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYingysirtdrKAARQSLGYCPQ----------FDALFDE 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 567 -SADDM-----REKGYT----DQDLERILHSVHLYhivqreggwdavmDWKDV----LSGGEKQRMGMARMFYHKPKYAL 632
Cdd:cd03263  90 lTVREHlrfyaRLKGLPkseiKEEVELLLRVLGLT-------------DKANKrartLSGGMKRKLSLAIALIGGPSVLL 156
                       170
                ....*....|....*
gi 60218875 633 LDECTSavSIDVEGK 647
Cdd:cd03263 157 LDEPTS--GLDPASR 169
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
494-534 8.12e-05

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 44.83  E-value: 8.12e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 60218875 494 VASRL---NFKVEEGMHLLITGPNGCGKSSLFRILSGLWPvYEG 534
Cdd:COG4138   8 VAGRLgpiSAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQG 50
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
489-638 8.53e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 45.07  E-value: 8.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  489 PAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPP------------QHMFYIPQRPymsl 555
Cdd:PRK13639  12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGeVLIKGEPikydkksllevrKTVGIVFQNP---- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  556 gslRDQVIYPDSADD-----MREKGYTDQDLERILHSVHLyhiVQREGGWDAVmdwKDVLSGGEKQRMGMARMFYHKPKY 630
Cdd:PRK13639  88 ---DDQLFAPTVEEDvafgpLNLGLSKEEVEKRVKEALKA---VGMEGFENKP---PHHLSGGQKKRVAIAGILAMKPEI 158

                 ....*...
gi 60218875  631 ALLDECTS 638
Cdd:PRK13639 159 IVLDEPTS 166
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
491-637 8.58e-05

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: 44.67  E-value: 8.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 491 GEVVASR-LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLykpppqHMFyipqrpymSLGSLRDqviypdsAD 569
Cdd:cd03265  11 GDFEAVRgVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRA------TVA--------GHDVVRE-------PR 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 570 DMREK-GYTDQDL---------ERILHSVHLYHIVQREggWD----------AVMDWKDVL----SGGEKQRMGMARMFY 625
Cdd:cd03265  70 EVRRRiGIVFQDLsvddeltgwENLYIHARLYGVPGAE--RReridelldfvGLLEAADRLvktySGGMRRRLEIARSLV 147
                       170
                ....*....|..
gi 60218875 626 HKPKYALLDECT 637
Cdd:cd03265 148 HRPEVLFLDEPT 159
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
498-667 1.05e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 44.45  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV------------LYKPPPQ---------HMFYIPQrPYMSLG 556
Cdd:PRK14267  23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEArvegevrlfgrnIYSPDVDpievrrevgMVFQYPN-PFPHLT 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  557 SLRDQVIYPDSADDMREKGYTDQDLERILHSVHLYHIVQreggwDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDEC 636
Cdd:PRK14267 102 IYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVK-----DRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 60218875  637 TSAV----SIDVEGKIFQAAIGAGISLlsITHRPS 667
Cdd:PRK14267 177 TANIdpvgTAKIEELLFELKKEYTIVL--VTHSPA 209
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
498-664 1.06e-04

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 44.62  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPppQHMFYIPQRPYMSLG-SLRDQV--------IYPDSA 568
Cdd:PRK11124  21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIA--GNHFDFSKTPSDKAIrELRRNVgmvfqqynLWPHLT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  569 -------DDMREKGYT-DQDLER---ILHSVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDECT 637
Cdd:PRK11124  99 vqqnlieAPCRVLGLSkDQALARaekLLERLRLKPYADR---------FPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
                        170       180       190
                 ....*....|....*....|....*....|
gi 60218875  638 SAVSIDVEG---KIFQAAIGAGISLLSITH 664
Cdd:PRK11124 170 AALDPEITAqivSIIRELAETGITQVIVTH 199
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
498-534 1.20e-04

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: 44.06  E-value: 1.20e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 60218875 498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG 534
Cdd:cd03220  41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG 77
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
610-665 1.33e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 45.41  E-value: 1.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60218875   610 LSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEgKIFQAAI-----GAGISLLSITHR 665
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE-KLIEKTIvdikdKADKTIITIAHR 1418
PTZ00243 PTZ00243
ABC transporter; Provisional
498-653 1.87e-04

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 45.15  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPppQHMFYIPQRPYMSLGSLRDQVIYPDSADDMREkgyt 577
Cdd:PTZ00243  679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--RSIAYVPQQAWIMNATVRGNILFFDEEDAARL---- 752
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60218875   578 dQDLERIlhSVHLYHIVQREGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQAAI 653
Cdd:PTZ00243  753 -ADAVRV--SQLEADLAQLGGGLETEIGEKGVnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF 826
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
499-639 1.95e-04

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 43.44  E-value: 1.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 499 NFKVEEGMHLLITGPNGCGKSSLFRILSGLWP------VYEGVLYKPPPQHMFYIPQR-----------PYMSLgslRDQ 561
Cdd:COG1126  21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiTVDGEDLTDSKKDINKLRRKvgmvfqqfnlfPHLTV---LEN 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 562 VIYP------DSADDMREKGytdqdlERILHSVHLYhivqreggwdavmDWKDV----LSGGEKQRMGMAR---MfyhKP 628
Cdd:COG1126  98 VTLApikvkkMSKAEAEERA------MELLERVGLA-------------DKADAypaqLSGGQQQRVAIARalaM---EP 155
                       170
                ....*....|.
gi 60218875 629 KYALLDECTSA 639
Cdd:COG1126 156 KVMLFDEPTSA 166
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
493-664 3.03e-04

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 43.16  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  493 VVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY------KPPPQHMFYIPQRPYM---------SLGS 557
Cdd:PRK09493  15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdglkvNDPKVDERLIRQEAGMvfqqfylfpHLTA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  558 LRDQVIYPdsaddMREKGYTDQDLERILHSvhlyhIVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECT 637
Cdd:PRK09493  95 LENVMFGP-----LRVRGASKEEAEKQARE-----LLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
                        170       180       190
                 ....*....|....*....|....*....|..
gi 60218875  638 SAvsIDVE-----GKIFQAAIGAGISLLSITH 664
Cdd:PRK09493 165 SA--LDPElrhevLKVMQDLAEEGMTMVIVTH 194
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
466-676 3.32e-04

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: 43.02  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   466 LAIKGTVIDVDHGIICENVPIITPAGEVVAsrlnfkveegmhllITGPNGCGKSSLFRILSGlWPVYEgvlykpppqhmf 545
Cdd:TIGR01978   1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHA--------------IMGPNGSGKSTLSKTIAG-HPSYE------------ 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   546 yipqrpyMSLGS--LRDQVIYPDSADDMREKG--YTDQDLERI--------LHSVhlYHIVQREGGWDA--VMDWKDVL- 610
Cdd:TIGR01978  54 -------VTSGTilFKGQDLLELEPDERARAGlfLAFQYPEEIpgvsnlefLRSA--LNARRSARGEEPldLLDFEKLLk 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   611 ---------------------SGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEgKIFQAAIGA----GISLLSITHR 665
Cdd:TIGR01978 125 eklalldmdeeflnrsvnegfSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDAL-KIVAEGINRlrepDRSFLIITHY 203
                         250
                  ....*....|....*
gi 60218875   666 PSLWKY----HTHLL 676
Cdd:TIGR01978 204 QRLLNYikpdYVHVL 218
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
497-664 5.43e-04

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 43.31  E-value: 5.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  497 RLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL--------------YKPPPQHMFYIPQRPYMSLGSlRDQV 562
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIifngqridtlspgkLQALRRDIQFIFQDPYASLDP-RQTV 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  563 IYpDSADDMREKGYTDQDLER-----ILHSVHLyhivQREGGWDavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDECT 637
Cdd:PRK10261 421 GD-SIMEPLRVHGLLPGKAAAarvawLLERVGL----LPEHAWR----YPHEFSGGQRQRICIARALALNPKVIIADEAV 491
                        170       180       190
                 ....*....|....*....|....*....|.
gi 60218875  638 SAVSIDVEGKIFQAAIGA----GISLLSITH 664
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLqrdfGIAYLFISH 522
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
610-639 8.01e-04

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 42.48  E-value: 8.01e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 60218875  610 LSGGEKQRMGMARMFYHKPKYALLDECTSA 639
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSA 170
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
480-642 8.82e-04

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 41.92  E-value: 8.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  480 ICENVPIITPAGEVVAsrlnfkveegmhlLItGPNGCGKSSLFRILSG-LWPVYEGVLYKPPP----------QHMFYIP 548
Cdd:PRK11231  17 ILNDLSLSLPTGKITA-------------LI-GPNGCGKSTLLKCFARlLTPQSGTVFLGDKPismlssrqlaRRLALLP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  549 QRPYMSLG-SLRDQVIYPDS----------ADDmrekgytDQDLERILHSVHLYHIVQReggwdAVMDwkdvLSGGEKQR 617
Cdd:PRK11231  83 QHHLTPEGiTVRELVAYGRSpwlslwgrlsAED-------NARVNQAMEQTRINHLADR-----RLTD----LSGGQRQR 146
                        170       180
                 ....*....|....*....|....*
gi 60218875  618 MGMARMFYHKPKYALLDECTSAVSI 642
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDI 171
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
512-664 1.56e-03

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 40.93  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  512 GPNGCGKSSLFRILSGLWPVYEG-VLYKPPP----------QHMFYIPQR-PYMSLGSLRDQVI---YPDSADDMREKGY 576
Cdd:PRK10575  44 GHNGSGKSTLLKMLGRHQPPSEGeILLDAQPleswsskafaRKVAYLPQQlPAAEGMTVRELVAigrYPWHGALGRFGAA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  577 TDQDLERILHSVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSI----DVEGKIFQAA 652
Cdd:PRK10575 124 DREKVEEAISLVGLKPLAHR---------LVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLS 194
                        170
                 ....*....|..
gi 60218875  653 IGAGISLLSITH 664
Cdd:PRK10575 195 QERGLTVIAVLH 206
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
610-664 1.92e-03

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 40.72  E-value: 1.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 60218875  610 LSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEG---KIFQAAIGAGISLLSITH 664
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQQLAEEGKTMVVVTH 210
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
494-667 2.00e-03

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: 40.66  E-value: 2.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 494 VASRLNFKVEEGMHLLITGPNGCGKSSL----FR---ILSGLWpVYEGVLYKPPPQHMF-----YIPQRPYMSLGSLRDQ 561
Cdd:cd03288  36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRmvdIFDGKI-VIDGIDISKLPLHTLrsrlsIILQDPILFSGSIRFN 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875 562 ViypDSaddmrEKGYTDQDLERILHSVHLYHIVQR-EGGWDAVM-DWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSA 639
Cdd:cd03288 115 L---DP-----ECKCTDDRLWEALEIAQLKNMVKSlPGGLDAVVtEGGENFSVGQRQLFCLARAFVRKSSILIMDEATAS 186
                       170       180       190
                ....*....|....*....|....*....|.
gi 60218875 640 VSIDVEG---KIFQAAIgAGISLLSITHRPS 667
Cdd:cd03288 187 IDMATENilqKVVMTAF-ADRTVVTIAHRVS 216
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
610-639 2.09e-03

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 40.83  E-value: 2.09e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 60218875 610 LSGGEKQRMGMARMFYHKPKYALLDECTSA 639
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSA 170
PLN03130 PLN03130
ABC transporter C family member; Provisional
496-653 2.29e-03

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 41.65  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   496 SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG--VLYKpppQHMFYIPQRPYMSLGSLRDQVIYPDSADDMRe 573
Cdd:PLN03130  634 SNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDasVVIR---GTVAYVPQVSWIFNATVRDNILFGSPFDPER- 709
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   574 kgytdqdLERILHSVHLYHIVQREGGWDAV-MDWKDV-LSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQA 651
Cdd:PLN03130  710 -------YERAIDVTALQHDLDLLPGGDLTeIGERGVnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDK 782

                  ..
gi 60218875   652 AI 653
Cdd:PLN03130  783 CI 784
PLN03130 PLN03130
ABC transporter C family member; Provisional
498-665 2.64e-03

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 41.26  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   498 LNFKVEEGMHLLITGPNGCGKSS----LFRILS----------------GLWPvyegvLYKpppqHMFYIPQRPYMSLGS 557
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSmlnaLFRIVElergrilidgcdiskfGLMD-----LRK----VLGIIPQAPVLFSGT 1328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875   558 LRDQViypdsaDDMREkgYTDQDLERILHSVHLYHIVQREG-GWDA-VMDWKDVLSGGEKQRMGMARMFYHKPKYALLDE 635
Cdd:PLN03130 1329 VRFNL------DPFNE--HNDADLWESLERAHLKDVIRRNSlGLDAeVSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
                         170       180       190
                  ....*....|....*....|....*....|...
gi 60218875   636 CTSAVSIDVEGKIfQAAIGA---GISLLSITHR 665
Cdd:PLN03130 1401 ATAAVDVRTDALI-QKTIREefkSCTMLIIAHR 1432
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
494-664 2.82e-03

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 40.84  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  494 VASRLNFKVEEGMHLLITGPNGCGKS----SLFRILSGLWPVY---------EGVLYKPPPQ-------HMFYIPQRPYM 553
Cdd:PRK15134  24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYpsgdirfhgESLLHASEQTlrgvrgnKIAMIFQEPMV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  554 SLG---SLRDQVIYPDSAD-DMREKGYTDQDLeRILHSVHLYHIVQReggwdaVMDWKDVLSGGEKQRMGMARMFYHKPK 629
Cdd:PRK15134 104 SLNplhTLEKQLYEVLSLHrGMRREAARGEIL-NCLDRVGIRQAAKR------LTDYPHQLSGGERQRVMIAMALLTRPE 176
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 60218875  630 YALLDECTSAVSIDVEGKIFQ----AAIGAGISLLSITH 664
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQllreLQQELNMGLLFITH 215
GguA NF040905
sugar ABC transporter ATP-binding protein;
496-534 3.03e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.93  E-value: 3.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 60218875  496 SRLNFKVEEG-MHLLItGPNGCGKSSLFRILSGLWP--VYEG 534
Cdd:NF040905  18 DDVNLSVREGeIHALC-GENGAGKSTLMKVLSGVYPhgSYEG 58
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
498-537 3.50e-03

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 40.21  E-value: 3.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 60218875  498 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY 537
Cdd:PRK11650  23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIW 62
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
492-635 4.47e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 39.16  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60218875  492 EVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGlwpvyegvLYKPPPQHMFYIPQRPYMSLGSLRDQV--------I 563
Cdd:PRK13540  14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAG--------LLNPEKGEILFERQSIKKDLCTYQKQLcfvghrsgI 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60218875  564 YPDSAddMREKGYTD-------QDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDE 635
Cdd:PRK13540  86 NPYLT--LRENCLYDihfspgaVGITELCRLFSLEHLIDYPCG---------LLSSGQKRQVALLRLWMSKAKLWLLDE 153
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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