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Conserved domains on  [gi|4506341|ref|NP_002849|]
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ATP-binding cassette sub-family D member 3 isoform a [Homo sapiens]

Protein Classification

ABC transporter ATP-binding protein/permease( domain architecture ID 11490015)

ABC transporter ATP-binding protein/permease similar to Homo sapiens ATP-binding cassette sub-family D member 1 (ABCD1) and 3 (ABCD3), and Saccharomyces cerevisiae peroxisomal long-chain fatty acid import protein 1 (PXA1) and 2 (PXA2)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
1-647 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: 1065.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341      1 MAAFSKYLTARNSSL--------AGAAFLLLCLLHKRRRALGLHGKKSGKPPLQNNEK----EGKKERAVVDKVFFSRLI 68
Cdd:TIGR00954   1 MAVLSKYRLLRSTSNnktdkqdsPAAVGMNKVIELKRERAADRRGDKSGKEELTIVGKhstiEGAKKKAHVNGVFLGKLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341     69 QILKIMVPRTFCKETGYLVLIAVMLVSRTYCDVWMIQNGTLIESGIIGRSRKDFKRYLLNFIAAMPLISLVNNFLKYGLN 148
Cdd:TIGR00954  81 FLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    149 ELKLCFRVRLTKYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQ 228
Cdd:TIGR00954 161 ELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTALGSV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    229 GPASMMAYLVVSGLFLTRLRRPIGKMTITEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTVHSVFRKLVEHLHNFIL 308
Cdd:TIGR00954 241 GPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNLIIK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    309 FRFSMGFIDSIIAKYLATVVGYLVVSRPFLDLSHPRHLKSTHSELLEDYYQSGRMLLRMSQALGRIVLAGREMTRLAGFT 388
Cdd:TIGR00954 321 FRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKTHPAFLEMSEEELMQEFYNNGRLLLKAADALGRLMLAGRDMTRLAGFT 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    389 ARITELMQVLKDLNHGKYERTMVSQQEKGIEGVQVIPLIPGAGEIIIADNIIKFDHVPLATPNGDVLIRDLNFEVRSGAN 468
Cdd:TIGR00954 401 ARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNN 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    469 VLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGREDQKRKGISDLVLKEYLDN 548
Cdd:TIGR00954 481 LLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDN 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    549 VQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGITLFTVSHRKS 628
Cdd:TIGR00954 561 VQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKS 640
                         650
                  ....*....|....*....
gi 4506341    629 LWKHHEYYLHMDGRGNYEF 647
Cdd:TIGR00954 641 LWKYHEYLLYMDGRGGYQF 659
 
Name Accession Description Interval E-value
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
1-647 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: 1065.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341      1 MAAFSKYLTARNSSL--------AGAAFLLLCLLHKRRRALGLHGKKSGKPPLQNNEK----EGKKERAVVDKVFFSRLI 68
Cdd:TIGR00954   1 MAVLSKYRLLRSTSNnktdkqdsPAAVGMNKVIELKRERAADRRGDKSGKEELTIVGKhstiEGAKKKAHVNGVFLGKLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341     69 QILKIMVPRTFCKETGYLVLIAVMLVSRTYCDVWMIQNGTLIESGIIGRSRKDFKRYLLNFIAAMPLISLVNNFLKYGLN 148
Cdd:TIGR00954  81 FLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    149 ELKLCFRVRLTKYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQ 228
Cdd:TIGR00954 161 ELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTALGSV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    229 GPASMMAYLVVSGLFLTRLRRPIGKMTITEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTVHSVFRKLVEHLHNFIL 308
Cdd:TIGR00954 241 GPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNLIIK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    309 FRFSMGFIDSIIAKYLATVVGYLVVSRPFLDLSHPRHLKSTHSELLEDYYQSGRMLLRMSQALGRIVLAGREMTRLAGFT 388
Cdd:TIGR00954 321 FRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKTHPAFLEMSEEELMQEFYNNGRLLLKAADALGRLMLAGRDMTRLAGFT 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    389 ARITELMQVLKDLNHGKYERTMVSQQEKGIEGVQVIPLIPGAGEIIIADNIIKFDHVPLATPNGDVLIRDLNFEVRSGAN 468
Cdd:TIGR00954 401 ARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNN 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    469 VLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGREDQKRKGISDLVLKEYLDN 548
Cdd:TIGR00954 481 LLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDN 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    549 VQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGITLFTVSHRKS 628
Cdd:TIGR00954 561 VQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKS 640
                         650
                  ....*....|....*....
gi 4506341    629 LWKHHEYYLHMDGRGNYEF 647
Cdd:TIGR00954 641 LWKYHEYLLYMDGRGGYQF 659
ABC_membrane_2 pfam06472
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ...
70-338 1.47e-122

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: 364.62  E-value: 1.47e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341     70 ILKIMVPRTFCKETGYLVLIAVMLVSRTYCDVWMIQNGTLIESGIIGRSRKDFKRYLLNFIAAMPLISLVNNFLKYGLNE 149
Cdd:pfam06472   1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    150 LKLCFRVRLTKYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQG 229
Cdd:pfam06472  81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    230 PASMMAYLVVSGLFLTRLRRPIGKMTITEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTVHSVFRKLVEHLHNFILF 309
Cdd:pfam06472 161 PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILRR 240
                         250       260
                  ....*....|....*....|....*....
gi 4506341    310 RFSMGFIDSIIAKYLATVVGYLVVSRPFL 338
Cdd:pfam06472 241 RLWYGFIEDFVLKYTWSILGYVLVALPIF 269
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
84-648 1.62e-97

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 310.59  E-value: 1.62e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   84 GYLVLIAVMLVSRTYCDVWMI-QNGTLIESgIIGRSRKDFKRYLLNF---IAAMPLISLVNNFLKYGLnELKLcfRVRLT 159
Cdd:COG4178  25 GLLALLLLLTLASVGLNVLLNfWNRDFYDA-LQARDAAAFWQQLGVFallAAISILLAVYQTYLRQRL-QIRW--REWLT 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  160 KYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQG---------- 229
Cdd:COG4178 101 ERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDIRLFTETTLSLSLGLLSSVVTLISFIGILWSLSGSLTftlggysiti 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  230 PASMM----AYLVVSGLFLTRLRRPIGKMTITEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTVHSVFRKLVEHLHN 305
Cdd:COG4178 181 PGYMVwaalIYAIIGTLLTHLIGRPLIRLNFEQQRREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVIANWRR 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  306 FILFRFSMGFIDSIIAkYLATVVGYLVVSrpfldlshPRhlksthselledyYQSGRM----LLRMSQALGRIVLAGR-- 379
Cdd:COG4178 261 LIRRQRNLTFFTTGYG-QLAVIFPILVAA--------PR-------------YFAGEItlggLMQAASAFGQVQGALSwf 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  380 --EMTRLAGFTA---RITELMQVLKDlnhgkyertmVSQQEKGIEGVqviplipgageIIIADNIIKFDHVPLATPNGDV 454
Cdd:COG4178 319 vdNYQSLAEWRAtvdRLAGFEEALEA----------ADALPEAASRI-----------ETSEDGALALEDLTLRTPDGRP 377
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  455 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGREDqkr 534
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGTLREALLYPATAEA--- 454
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  535 kgISDLVLKEYLDNVQLGHILEReggWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCR 614
Cdd:COG4178 455 --FSDAELREALEAVGLGHLAER---LDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR 529
                       570       580       590
                ....*....|....*....|....*....|....*.
gi 4506341  615 K--VGITLFTVSHRKSLWKHHEYYLHMDGRGNYEFK 648
Cdd:COG4178 530 EelPGTTVISVGHRSTLAAFHDRVLELTGDGSWQLL 565
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
440-645 6.55e-87

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: 268.64  E-value: 6.55e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTL 519
Cdd:cd03223   1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  520 RDQVIYPdgredqkrkgisdlvlkeyldnvqlghilereggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:cd03223  81 REQLIYP----------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 4506341  600 AVSVDVEGYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGNY 645
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
436-644 1.90e-16

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 78.99  E-value: 1.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   436 ADNIIKFDHVPLATpNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGGR---LTKPE--RGK 504
Cdd:PRK10247   4 NSPLLQLQNVGYLA-GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISptsgtlLFEGEdisTLKPEiyRQQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   505 LFYVPQRPYMTLGTLRDQVIYP---DGREDQKRKGISDLVLKEyLDNvqlgHILEReggwdSVQDwmdvLSGGEKQRMAM 581
Cdd:PRK10247  83 VSYCAQTPTLFGDTVYDNLIFPwqiRNQQPDPAIFLDDLERFA-LPD----TILTK-----NIAE----LSGGEKQRISL 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4506341   582 ARLFYHKPQFAILDECTSAVSVD----VEGYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGN 644
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESnkhnVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAG 215
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
451-625 1.03e-10

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 61.48  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLfGGRLTKPERGKLFYVPQR-------PY-----MTLG 517
Cdd:NF040873   3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLaGVLRPT-SGTVRRAGGARVAYVPQRsevpdslPLtvrdlVAMG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   518 TLRDQVIY-PDGREDQkrkgisdLVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:NF040873  82 RWARRGLWrRLTRDDR-------AAVDDALERVGLADLAGRQ---------LGELSGGQRQRALLAQGLAQEADLLLLDE 145
                        170       180       190
                 ....*....|....*....|....*....|..
gi 4506341   597 CTSAVSVDVEGYIYSHCRKV---GITLFTVSH 625
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEharGATVVVVTH 177
 
Name Accession Description Interval E-value
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
1-647 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: 1065.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341      1 MAAFSKYLTARNSSL--------AGAAFLLLCLLHKRRRALGLHGKKSGKPPLQNNEK----EGKKERAVVDKVFFSRLI 68
Cdd:TIGR00954   1 MAVLSKYRLLRSTSNnktdkqdsPAAVGMNKVIELKRERAADRRGDKSGKEELTIVGKhstiEGAKKKAHVNGVFLGKLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341     69 QILKIMVPRTFCKETGYLVLIAVMLVSRTYCDVWMIQNGTLIESGIIGRSRKDFKRYLLNFIAAMPLISLVNNFLKYGLN 148
Cdd:TIGR00954  81 FLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    149 ELKLCFRVRLTKYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQ 228
Cdd:TIGR00954 161 ELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTALGSV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    229 GPASMMAYLVVSGLFLTRLRRPIGKMTITEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTVHSVFRKLVEHLHNFIL 308
Cdd:TIGR00954 241 GPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNLIIK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    309 FRFSMGFIDSIIAKYLATVVGYLVVSRPFLDLSHPRHLKSTHSELLEDYYQSGRMLLRMSQALGRIVLAGREMTRLAGFT 388
Cdd:TIGR00954 321 FRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKTHPAFLEMSEEELMQEFYNNGRLLLKAADALGRLMLAGRDMTRLAGFT 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    389 ARITELMQVLKDLNHGKYERTMVSQQEKGIEGVQVIPLIPGAGEIIIADNIIKFDHVPLATPNGDVLIRDLNFEVRSGAN 468
Cdd:TIGR00954 401 ARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNN 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    469 VLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGREDQKRKGISDLVLKEYLDN 548
Cdd:TIGR00954 481 LLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDN 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    549 VQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGITLFTVSHRKS 628
Cdd:TIGR00954 561 VQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKS 640
                         650
                  ....*....|....*....
gi 4506341    629 LWKHHEYYLHMDGRGNYEF 647
Cdd:TIGR00954 641 LWKYHEYLLYMDGRGGYQF 659
ABC_membrane_2 pfam06472
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ...
70-338 1.47e-122

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: 364.62  E-value: 1.47e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341     70 ILKIMVPRTFCKETGYLVLIAVMLVSRTYCDVWMIQNGTLIESGIIGRSRKDFKRYLLNFIAAMPLISLVNNFLKYGLNE 149
Cdd:pfam06472   1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    150 LKLCFRVRLTKYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQG 229
Cdd:pfam06472  81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    230 PASMMAYLVVSGLFLTRLRRPIGKMTITEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTVHSVFRKLVEHLHNFILF 309
Cdd:pfam06472 161 PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILRR 240
                         250       260
                  ....*....|....*....|....*....
gi 4506341    310 RFSMGFIDSIIAKYLATVVGYLVVSRPFL 338
Cdd:pfam06472 241 RLWYGFIEDFVLKYTWSILGYVLVALPIF 269
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
84-648 1.62e-97

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 310.59  E-value: 1.62e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   84 GYLVLIAVMLVSRTYCDVWMI-QNGTLIESgIIGRSRKDFKRYLLNF---IAAMPLISLVNNFLKYGLnELKLcfRVRLT 159
Cdd:COG4178  25 GLLALLLLLTLASVGLNVLLNfWNRDFYDA-LQARDAAAFWQQLGVFallAAISILLAVYQTYLRQRL-QIRW--REWLT 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  160 KYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQG---------- 229
Cdd:COG4178 101 ERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDIRLFTETTLSLSLGLLSSVVTLISFIGILWSLSGSLTftlggysiti 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  230 PASMM----AYLVVSGLFLTRLRRPIGKMTITEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTVHSVFRKLVEHLHN 305
Cdd:COG4178 181 PGYMVwaalIYAIIGTLLTHLIGRPLIRLNFEQQRREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVIANWRR 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  306 FILFRFSMGFIDSIIAkYLATVVGYLVVSrpfldlshPRhlksthselledyYQSGRM----LLRMSQALGRIVLAGR-- 379
Cdd:COG4178 261 LIRRQRNLTFFTTGYG-QLAVIFPILVAA--------PR-------------YFAGEItlggLMQAASAFGQVQGALSwf 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  380 --EMTRLAGFTA---RITELMQVLKDlnhgkyertmVSQQEKGIEGVqviplipgageIIIADNIIKFDHVPLATPNGDV 454
Cdd:COG4178 319 vdNYQSLAEWRAtvdRLAGFEEALEA----------ADALPEAASRI-----------ETSEDGALALEDLTLRTPDGRP 377
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  455 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGREDqkr 534
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGTLREALLYPATAEA--- 454
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  535 kgISDLVLKEYLDNVQLGHILEReggWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCR 614
Cdd:COG4178 455 --FSDAELREALEAVGLGHLAER---LDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR 529
                       570       580       590
                ....*....|....*....|....*....|....*.
gi 4506341  615 K--VGITLFTVSHRKSLWKHHEYYLHMDGRGNYEFK 648
Cdd:COG4178 530 EelPGTTVISVGHRSTLAAFHDRVLELTGDGSWQLL 565
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
440-645 6.55e-87

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: 268.64  E-value: 6.55e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTL 519
Cdd:cd03223   1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  520 RDQVIYPdgredqkrkgisdlvlkeyldnvqlghilereggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:cd03223  81 REQLIYP----------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 4506341  600 AVSVDVEGYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGNY 645
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
440-625 2.55e-28

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 112.60  E-value: 2.55e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLaTPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPE--RGKLFYV 508
Cdd:COG4619   1 LELEGLSF-RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkplsamPPPewRRQVAYV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  509 PQRPYMTLGTLRDQVIYPDGREDQKrkgISDLVLKEYLDNVQLGH-ILEREggwdsVQDwmdvLSGGEKQRMAMARLFYH 587
Cdd:COG4619  80 PQEPALWGGTVRDNLPFPFQLRERK---FDRERALELLERLGLPPdILDKP-----VER----LSGGERQRLALIRALLL 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 4506341  588 KPQFAILDECTSA---VSVD-VEGYIYSHCRKVGITLFTVSH 625
Cdd:COG4619 148 QPDVLLLDEPTSAldpENTRrVEELLREYLAEEGRAVLWVSH 189
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
64-626 2.96e-27

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 116.80  E-value: 2.96e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   64 FSRLIQILKimvprtfcKETGYLVLIAVMLVSRTYCDVWMIQ-NGTLIESGIIGRSRKDFKRYLLNFIAAMPLISLVNNF 142
Cdd:COG1132   9 LRRLLRYLR--------PYRGLLILALLLLLLSALLELLLPLlLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  143 LKYGLNelKLCFRV--RLTKYLYEEYL-QAFTYY---KMGNLDNRIanpdqllTQDVekfcNSVVDLYSNLskpFLDIVL 216
Cdd:COG1132  81 QRYLLA--RLAQRVvaDLRRDLFEHLLrLPLSFFdrrRTGDLLSRL-------TNDV----DAVEQFLAHG---LPQLVR 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  217 YIFKLTSAIGaqgpasMMAYL------------VVSGLFLTRLRRPIGKMTITEQKYEGEyryVNSRL---ITNSEEIAF 281
Cdd:COG1132 145 SVVTLIGALV------VLFVIdwrlalivllvlPLLLLVLRLFGRRLRKLFRRVQEALAE---LNGRLqesLSGIRVVKA 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  282 YNGNKREKQTVHSVFRKLVEHLHNFI----LFRFSMGFIdSIIAKYLATVVGYLVVSRPFLDLShprhlksthsELLEdY 357
Cdd:COG1132 216 FGREERELERFREANEELRRANLRAArlsaLFFPLMELL-GNLGLALVLLVGGLLVLSGSLTVG----------DLVA-F 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  358 YQSGRMLLRMSQALGRIVlagREMTRLAGFTARITELMqvlkdlnhgkyertmvSQQEKGIEGVQVIPLIPGAGEIiiad 437
Cdd:COG1132 284 ILYLLRLFGPLRQLANVL---NQLQRALASAERIFELL----------------DEPPEIPDPPGAVPLPPVRGEI---- 340
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  438 niiKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPE--RGKLF 506
Cdd:COG1132 341 ---EFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidgvdirdlTLEslRRQIG 417
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  507 YVPQRPYMTLGTLRDQVIYpdGREDqkrkgISDLVLKEYLDNVQLGHILER-EGGWDSVqdwmdV------LSGGEKQRM 579
Cdd:COG1132 418 VVPQDTFLFSGTIRENIRY--GRPD-----ATDEEVEEAAKAAQAHEFIEAlPDGYDTV-----VgergvnLSGGQRQRI 485
                       570       580       590       600
                ....*....|....*....|....*....|....*....|....*....
gi 4506341  580 AMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHR 626
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLmkGRTTIVIAHR 534
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
455-641 2.37e-26

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: 106.78  E-value: 2.37e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  455 LIRDLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLfGGRLTKPerGKLFYVPQRPYMTLGTLRDQVIYpdGRE-DQ 532
Cdd:cd03250  20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKL-SGSVSVP--GSIAYVSQEPWIQNGTIRENILF--GKPfDE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  533 KR--KGIS------DLVLKEYLDNVQLGhilerEGGwdsvqdwmdV-LSGGEKQRMAMARLFYHKPQFAILDECTSAVSV 603
Cdd:cd03250  95 ERyeKVIKacalepDLEILPDGDLTEIG-----EKG---------InLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 4506341  604 DVEGYIYSHC----RKVGITLFTVSHRKSLWKHHEYYLHMDG 641
Cdd:cd03250 161 HVGRHIFENCilglLLNNKTRILVTHQLQLLPHADQIVVLDN 202
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
440-629 1.33e-25

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: 103.62  E-value: 1.33e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATPNGDVLI-RDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPE--RGKLFY 507
Cdd:cd03228   1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlrdlDLEslRKNIAY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  508 VPQRPYMTLGTLRDqviypdgredqkrkgisdlvlkeyldNVqlghilereggwdsvqdwmdvLSGGEKQRMAMARLFYH 587
Cdd:cd03228  81 VPQDPFLFSGTIRE--------------------------NI---------------------LSGGQRQRIAIARALLR 113
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 4506341  588 KPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSL 629
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALakGKTVIVIAHRLST 157
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
440-641 2.74e-24

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: 107.54  E-value: 2.74e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPE--RGKLFYV 508
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvdlsdlDPAswRRQIAWV 416
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  509 PQRPYMTLGTLRDQV-IY-PDGREDQkrkgisdlvLKEYLDNVQLGHILER-EGGWDSVqdwmdV------LSGGEKQRM 579
Cdd:COG4988 417 PQNPYLFAGTIRENLrLGrPDASDEE---------LEAALEAAGLDEFVAAlPDGLDTP-----LgeggrgLSGGQAQRL 482
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4506341  580 AMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMDG 641
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLAQADRILVLDD 546
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
371-629 9.24e-23

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: 102.36  E-value: 9.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    371 LGRIVLAGReMTRLAGFTARI--TELMQVLKDLN---HGKYERTMVSQQEKGIEGVQVIPLiPGAGEIIIADNI-IKFDH 444
Cdd:TIGR02857 249 IGFRLLAGD-LDLATGLFVLLlaPEFYLPLRQLGaqyHARADGVAAAEALFAVLDAAPRPL-AGKAPVTAAPASsLEFSG 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    445 VPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL-----------TKPERGKLFYVPQRPY 513
Cdd:TIGR02857 327 VSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladadADSWRDQIAWVPQHPF 406
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    514 MTLGTLRDQVIYpdgredqKRKGISDLVLKEYLDNVQLGHIL-EREGGWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQF 591
Cdd:TIGR02857 407 LFAGTIAENIRL-------ARPDASDAEIREALERAGLDEFVaALPQGLDTpIGEGGAGLSGGQAQRLALARAFLRDAPL 479
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 4506341    592 AILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSL 629
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLAL 519
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
428-626 1.57e-21

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: 99.07  E-value: 1.57e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  428 PGAGEIIIADNIIKFDHVPLATPNGDV-LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-------- 498
Cdd:COG4987 322 PAEPAPAPGGPSLELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrd 401
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  499 KPE---RGKLFYVPQRPYMTLGTLRD--QVIYPDGREDQkrkgisdlvLKEYLDNVQLGHILER-EGGWDSvqdWMDV-- 570
Cdd:COG4987 402 LDEddlRRRIAVVPQRPHLFDTTLREnlRLARPDATDEE---------LWAALERVGLGDWLAAlPDGLDT---WLGEgg 469
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4506341  571 --LSGGEKQRMAMARLFYHKPQFAILDECTSavSVDVE------GYIYSHCRkvGITLFTVSHR 626
Cdd:COG4987 470 rrLSGGERRRLALARALLRDAPILLLDEPTE--GLDAAteqallADLLEALA--GRTVLLITHR 529
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
456-599 3.10e-21

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: 90.40  E-value: 3.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGRLTKPE----RGKLFYVPQ--RPYMTLgTLRDQ 522
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIaGLLSPtegtilLDGQDLTDDErkslRKEIGYVFQdpQLFPRL-TVREN 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4506341    523 VIYPDGREDQKRKGISDlVLKEYLDNVQLGHILEReggwdSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:pfam00005  80 LRLGLLLKGLSKREKDA-RAEEALEKLGLGDLADR-----PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
451-642 1.36e-20

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: 90.67  E-value: 1.36e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFG-----GRLTKPERGKLFYVPQRPY----------- 513
Cdd:cd03235  10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLKPTSGsirvfGKPLEKERKRIGYVPQRRSidrdfpisvrd 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  514 -MTLGTLRDQVIYPDGREDQKRKgisdlvLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFA 592
Cdd:cd03235  90 vVLMGLYGHKGLFRRLSKADKAK------VDEALERVGLSELADRQ---------IGELSGGQQQRVLLARALVQDPDLL 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 4506341  593 ILDECTSAVSVDVEGYIYSHCRKV---GITLFTVSH-RKSLWKHHEYYLHMDGR 642
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELrreGMTILVVTHdLGLVLEYFDRVLLLNRT 208
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
451-626 7.63e-20

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: 86.92  E-value: 7.63e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLFYvpqrpymtlgtlrdqviypDGre 530
Cdd:cd00267  10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAI--------AGLLKPTSGEILI-------------------DG-- 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  531 dqkrKGISDLVLKEYLDNVQLGHilereggwdsvQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVD----VE 606
Cdd:cd00267  61 ----KDIAKLPLEELRRRIGYVP-----------Q-----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAsrerLL 120
                       170       180
                ....*....|....*....|
gi 4506341  607 GYIYSHCRKvGITLFTVSHR 626
Cdd:cd00267 121 ELLRELAEE-GRTVIIVTHD 139
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
451-625 1.53e-19

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: 88.56  E-value: 1.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGR----LTKPERGKLF-YVPQRPYMTLG-T 518
Cdd:COG1120  12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALaGLLKPssgevLLDGRdlasLSRRELARRIaYVPQEPPAPFGlT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  519 LRDQVI---YP-------DGREDQKrkgisdlVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHK 588
Cdd:COG1120  92 VRELVAlgrYPhlglfgrPSAEDRE-------AVEEALERTGLEHLADRP---------VDELSGGERQRVLIARALAQE 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 4506341  589 PQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:COG1120 156 PPLLLLDEPTSHLdlahQLEVLELLRRLARERGRTVVMVLH 196
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
440-628 2.12e-19

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: 87.67  E-value: 2.12e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLFYV 508
Cdd:cd03253   1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevtlDSLRRAIGVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  509 PQRPYMTLGTLRDQVIY--PDGREDQ-----KRKGISDLvlkeyldnvqlghILEREGGWDSVqdwmdV------LSGGE 575
Cdd:cd03253  81 PQDTVLFNDTIGYNIRYgrPDATDEEvieaaKAAQIHDK-------------IMRFPDGYDTI-----VgerglkLSGGE 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4506341  576 KQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKS 628
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLS 197
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
440-646 2.19e-19

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: 92.59  E-value: 2.19e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLA-TPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLF------------ 506
Cdd:COG2274 474 IELENVSFRyPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL--------LGLYEPTSGRILidgidlrqidpa 545
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  507 -------YVPQRPYMTLGTLRDQVIYpdGREDqkrkgISDLVLKEYLDNVQLGH-ILEREGGWDS-VQDWMDVLSGGEKQ 577
Cdd:COG2274 546 slrrqigVVLQDVFLFSGTIRENITL--GDPD-----ATDEEIIEAARLAGLHDfIEALPMGYDTvVGEGGSNLSGGQRQ 618
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4506341  578 RMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMDG-----RGNYE 646
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLlkGRTVIIIAHRLSTIRLADRIIVLDKgriveDGTHE 694
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
437-641 5.48e-19

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: 86.37  E-value: 5.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  437 DNIIKFDHVPLATPN-GDVLI-RDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---KP--------ERG 503
Cdd:cd03248   9 KGIVKFQNVTFAYPTrPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPisqyehkyLHS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  504 KLFYVPQRPYMTLGTLRDQVIYpdgredqkrkGISDLVLKEYLDNVQLGH----ILEREGGWDS-VQDWMDVLSGGEKQR 578
Cdd:cd03248  89 KVSLVGQEPVLFARSLQDNIAY----------GLQSCSFECVKEAAQKAHahsfISELASGYDTeVGEKGSQLSGGQKQR 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4506341  579 MAMARLFYHKPQFAILDECTSAVSVDVEGYIYS--HCRKVGITLFTVSHRKSLWKHHEYYLHMDG 641
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQalYDWPERRTVLVIAHRLSTVERADQILVLDG 223
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
451-625 6.28e-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: 6.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTKPE---RGKLFYVPQRP--YMTLg 517
Cdd:COG4133  13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILagllppsaGEVL-WNGEPIRDARedyRRRLAYLGHADglKPEL- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  518 TLRDQVIYpdgreDQKRKG--ISDLVLKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:COG4133  91 TVRENLRF-----WAALYGlrADREAIDEALEAVGLAGLADLPVR---------QLSAGQKRRVALARLLLSPAPLWLLD 156
                       170       180       190
                ....*....|....*....|....*....|....
gi 4506341  596 ECTSAVSVD----VEGYIYSHCRKVGITLFTvSH 625
Cdd:COG4133 157 EPFTALDAAgvalLAELIAAHLARGGAVLLT-TH 189
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
440-628 9.47e-19

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: 85.74  E-value: 9.47e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLFYV 508
Cdd:cd03254   3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidgidirdisrKSLRSMIGVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  509 PQRPYMTLGTLRDQVIYpdGREDqkrkgISDLVLKEYLDNVQLGHILER-EGGWDS-VQDWMDVLSGGEKQRMAMARLFY 586
Cdd:cd03254  83 LQDTFLFSGTIMENIRL--GRPN-----ATDEEVIEAAKEAGAHDFIMKlPNGYDTvLGENGGNLSQGERQLLAIARAML 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 4506341  587 HKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKS 628
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAHRLS 199
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
436-625 1.16e-18

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 85.91  E-value: 1.16e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  436 ADNIIKFDHVPLATpNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRV-LGELWPL-----FGGRLTKPERGKLFYVP 509
Cdd:COG1121   3 MMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAiLGLLPPTsgtvrLFGKPPRRARRRIGYVP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  510 QRPYMTLG---TLRDQV---IYPD-------GREDQKRkgisdlvLKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEK 576
Cdd:COG1121  82 QRAEVDWDfpiTVRDVVlmgRYGRrglfrrpSRADREA-------VDEALERVGLEDLADR---------PIGELSGGQQ 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 4506341  577 QRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYS---HCRKVGITLFTVSH 625
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYEllrELRREGKTILVVTH 197
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
441-640 5.52e-18

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: 82.90  E-value: 5.52e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  441 KFDHVPLATPNGD-VLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFG-----GRLTKPE-----RGKLFYV 508
Cdd:cd03225   1 ELKNLSFSYPDGArPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLnGLLGPTSGevlvdGKDLTKLslkelRRKVGLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  509 PQRPymtlgtlRDQVIYPDGRED----QKRKGIS----DLVLKEYLDNVQLGHILEReggwdSVQDwmdvLSGGEKQRMA 580
Cdd:cd03225  81 FQNP-------DDQFFGPTVEEEvafgLENLGLPeeeiEERVEEALELVGLEGLRDR-----SPFT----LSGGQKQRVA 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4506341  581 MARLFYHKPQFAILDECTSavSVDVEGY-----IYSHCRKVGITLFTVSHRKSLWKHH-EYYLHMD 640
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTA--GLDPAGRrelleLLKKLKAEGKTIIIVTHDLDLLLELaDRVIVLE 208
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
455-629 1.35e-17

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: 80.72  E-value: 1.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  455 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTkpergkLFYVPQRPYmTLGTLRDQVIYpdgredqkr 534
Cdd:cd03246  17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR------LDGADISQW-DPNELGDHVGY--------- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  535 kgisdlvlkeYLDNVQL--GHILEreggwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYS- 611
Cdd:cd03246  81 ----------LPQDDELfsGSIAE------------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQa 138
                       170       180
                ....*....|....*....|
gi 4506341  612 --HCRKVGITLFTVSHRKSL 629
Cdd:cd03246 139 iaALKAAGATRIVIAHRPET 158
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
451-625 1.95e-17

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: 80.56  E-value: 1.95e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggRLTKPERGKlfyvpqrpymtlgtlrdqvIYPDGR- 529
Cdd:cd03214  10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA--------GLLKPSSGE-------------------ILLDGKd 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  530 -EDQKRKGISDLV--LKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAV----S 602
Cdd:cd03214  63 lASLSPKELARKIayVPQALELLGLAHLADRP---------FNELSGGERQRVLLARALAQEPPILLLDEPTSHLdiahQ 133
                       170       180
                ....*....|....*....|...
gi 4506341  603 VDVEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLH 156
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
440-626 2.98e-17

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: 81.00  E-value: 2.98e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLA-TPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLFY 507
Cdd:cd03244   3 IEFKNVSLRyRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdiskiglHDLRSRISI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  508 VPQRPYMTLGTLRDQV----IYPDGRedqkrkgisdlvLKEYLDNVQL-GHILEREGGWDS-VQDWMDVLSGGEKQRMAM 581
Cdd:cd03244  83 IPQDPVLFSGTIRSNLdpfgEYSDEE------------LWQALERVGLkEFVESLPGGLDTvVEEGGENLSVGQRQLLCL 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 4506341  582 ARLFYHKPQFAILDECTSavSVDVEG------YIYSHCRkvGITLFTVSHR 626
Cdd:cd03244 151 ARALLRKSKILVLDEATA--SVDPETdaliqkTIREAFK--DCTVLTIAHR 197
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
440-629 3.78e-17

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: 80.71  E-value: 3.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATPNGDVL-IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggRLTKPERGKLF------------ 506
Cdd:cd03245   3 IEFRNVSFSYPNQEIPaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLA--------GLYKPTSGSVLldgtdirqldpa 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  507 -------YVPQRPYMTLGTLRDQVIYPDGREDQKR-------KGISDLVLKEYL-DNVQLGhilerEGGwdsvqdwmDVL 571
Cdd:cd03245  75 dlrrnigYVPQDVTLFYGTLRDNITLGAPLADDERilraaelAGVTDFVNKHPNgLDLQIG-----ERG--------RGL 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  572 SGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSL 629
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSL 201
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
452-596 1.00e-16

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 83.58  E-value: 1.00e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  452 GDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELwPLFGGRLTKPERGKLFYVPQRPYMTLG-TLRDQVIYPDGR 529
Cdd:COG0488  10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILaGEL-EPDSGEVSIPKGLRIGYLPQEPPLDDDlTVLDTVLDGDAE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  530 EDQKRK---------GISDLVLKEYLDnvqLGHILEREGGWD--------------SVQDW---MDVLSGGEKQRMAMAR 583
Cdd:COG0488  89 LRALEAeleeleaklAEPDEDLERLAE---LQEEFEALGGWEaearaeeilsglgfPEEDLdrpVSELSGGWRRRVALAR 165
                       170
                ....*....|...
gi 4506341  584 LFYHKPQFAILDE 596
Cdd:COG0488 166 ALLSEPDLLLLDE 178
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
451-625 1.32e-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: 79.53  E-value: 1.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRltkPERGKLFY---------------------VP 509
Cdd:cd03260  11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGA---PDEGEVLLdgkdiydldvdvlelrrrvgmVF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  510 QRPYMTLGTLRDQVIYPDG-REDQKRKGISDLVLKeyldnvqlghILEREGGWDSVQDWMDV--LSGGEKQRMAMARLFY 586
Cdd:cd03260  88 QKPNPFPGSIYDNVAYGLRlHGIKLKEELDERVEE----------ALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALA 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 4506341  587 HKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLftVSH 625
Cdd:cd03260 158 NEPEVLLLDEPTSALdpisTAKIEELIAELKKEYTIVI--VTH 198
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
440-641 1.65e-16

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: 79.45  E-value: 1.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLA-TPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGR---------LTKPE--RGKLFY 507
Cdd:cd03252   1 ITFEHVRFRyKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRvlvdghdlaLADPAwlRRQVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  508 VPQRPYMTLGTLRDQVIYPDGREDQKRKgisdlvlkEYLDNVQLGH--ILEREGGWDSVQDWMDV-LSGGEKQRMAMARL 584
Cdd:cd03252  81 VLQENVLFNRSIRDNIALADPGMSMERV--------IEAAKLAGAHdfISELPEGYDTIVGEQGAgLSGGQRQRIAIARA 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4506341  585 FYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMDG 641
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNADRIIVMEK 211
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
436-644 1.90e-16

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 78.99  E-value: 1.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   436 ADNIIKFDHVPLATpNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGGR---LTKPE--RGK 504
Cdd:PRK10247   4 NSPLLQLQNVGYLA-GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISptsgtlLFEGEdisTLKPEiyRQQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   505 LFYVPQRPYMTLGTLRDQVIYP---DGREDQKRKGISDLVLKEyLDNvqlgHILEReggwdSVQDwmdvLSGGEKQRMAM 581
Cdd:PRK10247  83 VSYCAQTPTLFGDTVYDNLIFPwqiRNQQPDPAIFLDDLERFA-LPD----TILTK-----NIAE----LSGGEKQRISL 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4506341   582 ARLFYHKPQFAILDECTSAVSVD----VEGYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGN 644
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESnkhnVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAG 215
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
440-599 2.59e-16

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: 78.53  E-value: 2.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGRLTKPERGKLF----- 506
Cdd:COG1122   1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngllkptsGEV--LVDGKDITKKNLRELrrkvg 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  507 YVPQRPymtlgtlRDQVIYPDGRED---------QKRKGISDLVlKEYLDNVQLGHILEReggwdSVQDwmdvLSGGEKQ 577
Cdd:COG1122  79 LVFQNP-------DDQLFAPTVEEDvafgpenlgLPREEIRERV-EEALELVGLEHLADR-----PPHE----LSGGQKQ 141
                       170       180
                ....*....|....*....|..
gi 4506341  578 RMAMARLFYHKPQFAILDECTS 599
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTA 163
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
457-625 3.10e-16

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: 78.69  E-value: 3.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  457 RDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGRLTKPERGKLFY-----VPQRPYMTL---GTLR 520
Cdd:COG1124  22 KDVSLEVAPGESFGLVGESGSGKSTLLRALaglerpwsGEV--TFDGRPVTRRRRKAFRrrvqmVFQDPYASLhprHTVD 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  521 DQVIYP---DGREDQKRKgisdlvLKEYLDNVQLG-HILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:COG1124 100 RILAEPlriHGLPDREER------IAELLEQVGLPpSFLDR---------YPHQLSGGQRQRVAIARALILEPELLLLDE 164
                       170       180       190
                ....*....|....*....|....*....|...
gi 4506341  597 CTSA--VSVDVE--GYIYSHCRKVGITLFTVSH 625
Cdd:COG1124 165 PTSAldVSVQAEilNLLKDLREERGLTYLFVSH 197
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
440-628 4.82e-16

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: 77.97  E-value: 4.82e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATPN-GDVLI-RDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLF 506
Cdd:cd03249   1 IEFKNVSFRYPSrPDVPIlKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldgvdirdlnlRWLRSQIG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  507 YVPQRPYMTLGTLRDQVIYpdGREDQKRKGISDLVLKEYLDNVqlghILEREGGWDSV------QdwmdvLSGGEKQRMA 580
Cdd:cd03249  81 LVSQEPVLFDGTIAENIRY--GKPDATDEEVEEAAKKANIHDF----IMSLPDGYDTLvgergsQ-----LSGGQKQRIA 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 4506341  581 MARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKS 628
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAHRLS 199
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
440-628 6.89e-16

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: 77.27  E-value: 6.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATPN-GDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLFY 507
Cdd:cd03251   1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILidghdvrdytlASLRRQIGL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  508 VPQRPYMTLGTLRDQVIYpdGREDQKRKGISDLVLKEYLDNVqlghILEREGGWDSVQDWMDV-LSGGEKQRMAMARLFY 586
Cdd:cd03251  81 VSQDVFLFNDTVAENIAY--GRPGATREEVEEAARAANAHEF----IMELPEGYDTVIGERGVkLSGGQRQRIAIARALL 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 4506341  587 HKPQFAILDECTSAVSVDVEGYIYSHCRK--VGITLFTVSHRKS 628
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERlmKNRTTFVIAHRLS 198
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
440-629 7.36e-16

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 81.31  E-value: 7.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    440 IKFDHVPLATPN-GDVLI-RDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLF 506
Cdd:TIGR00958 479 IEFQDVSFSYPNrPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldgvplvqydhHYLHRQVA 558
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    507 YVPQRPYMTLGTLRDQVIYpdgredqkrkGISDLVLKEYLDNVQLGH----ILEREGGWDSVQDWMDV-LSGGEKQRMAM 581
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAY----------GLTDTPDEEIMAAAKAANahdfIMEFPNGYDTEVGEKGSqLSGGQKQRIAI 628
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 4506341    582 ARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGITLFTVSHRKSL 629
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLST 676
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
440-642 2.31e-15

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: 75.60  E-value: 2.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATPNGDV---LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--------KPERGKLF-- 506
Cdd:cd03255   1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdiskLSEKELAAfr 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  507 -----YVPQR----PYMTLgtlRDQVIYP---DGREDQKRKgisdLVLKEYLDNVQLGHILEREGGWdsvqdwmdvLSGG 574
Cdd:cd03255  81 rrhigFVFQSfnllPDLTA---LENVELPlllAGVPKKERR----ERAEELLERVGLGDRLNHYPSE---------LSGG 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4506341  575 EKQRMAMARLFYHKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHM-DGR 642
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLdsetGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELrDGK 217
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
451-625 2.70e-15

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: 74.15  E-value: 2.70e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLFyvpqrpymtlgtLRDQVIYPDGRE 530
Cdd:cd03229  11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCI--------AGLEEPDSGSIL------------IDGEDLTDLEDE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  531 DQKRKGISDLVLKEY--------LDNVQLGhilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSA-- 600
Cdd:cd03229  71 LPPLRRRIGMVFQDFalfphltvLENIALG------------------LSGGQQQRVALARALAMDPDVLLLDEPTSAld 132
                       170       180
                ....*....|....*....|....*..
gi 4506341  601 --VSVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03229 133 piTRREVRALLKSLQAQLGITVVLVTH 159
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
455-600 2.71e-15

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 76.31  E-value: 2.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  455 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGRLT--KPE-----RGKLfyvPQRPYMTLG-TL 519
Cdd:COG4559  16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGELTPssgevrLNGRPLAawSPWelarrRAVL---PQHSSLAFPfTV 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  520 RdQVI----YPDGREDQKRKGIsdlvLKEYLDNVQLGHILEReggwdSVQDwmdvLSGGEKQRMAMARLF-------YHK 588
Cdd:COG4559  93 E-EVValgrAPHGSSAAQDRQI----VREALALVGLAHLAGR-----SYQT----LSGGEQQRVQLARVLaqlwepvDGG 158
                       170
                ....*....|..
gi 4506341  589 PQFAILDECTSA 600
Cdd:COG4559 159 PRWLFLDEPTSA 170
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
437-626 3.66e-15

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: 78.79  E-value: 3.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  437 DNIIKFDHVPLATPNGDV-LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWP---------LFGGR----LTKPER 502
Cdd:COG1123   2 TPLLEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrisgevLLDGRdlleLSEALR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  503 GKLF-YVPQRPYMTL--GTLRDQVIYPDGREDQKRKGISDLVLkEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRM 579
Cdd:COG1123  82 GRRIgMVFQDPMTQLnpVTVGDQIAEALENLGLSRAEARARVL-ELLEAVGLERRLDR---------YPHQLSGGQRQRV 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 4506341  580 AMARLFYHKPQFAILDECTSAVSVDVEGYIYSH----CRKVGITLFTVSHR 626
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLlrelQRERGTTVLLITHD 202
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
369-626 3.92e-15

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: 78.56  E-value: 3.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    369 QALGRIVLAGREMTRLAGFTARITELMQvlkdlnhGKYERTMVSQQEKGIEGVQVIPLipgageiiiadniiKFDHVPLA 448
Cdd:TIGR02868 285 EAFAALPAAAQQLTRVRAAAERIVEVLD-------AAGPVAEGSAPAAGAVGLGKPTL--------------ELRDLSAG 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    449 TPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-----------KPERGKLFYVPQRPYMTLG 517
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTldgvpvssldqDEVRRRVSVCAQDAHLFDT 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    518 TLRDQVIYpdGREDqkrkgISDLVLKEYLDNVQLG-HILEREGGWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:TIGR02868 424 TVRENLRL--ARPD-----ATDEELWAALERVGLAdWLRALPDGLDTvLGEGGARLSGGERQRLALARALLADAPILLLD 496
                         250       260       270
                  ....*....|....*....|....*....|...
gi 4506341    596 ECTSAVSVDVEGYIYSHCRKV--GITLFTVSHR 626
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAAlsGRTVVLITHH 529
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
440-629 4.58e-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: 78.64  E-value: 4.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATPNGD-VLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG--RL--------TKPERGKLF-Y 507
Cdd:COG4618 331 LSVENLTVVPPGSKrPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGsvRLdgadlsqwDREELGRHIgY 410
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  508 VPQRPymTL--GTLRdQVI--YPDGREDQ-----KRKGISDLVLK---EYldNVQLGhilerEGGwdsvqdwmDVLSGGE 575
Cdd:COG4618 411 LPQDV--ELfdGTIA-ENIarFGDADPEKvvaaaKLAGVHEMILRlpdGY--DTRIG-----EGG--------ARLSGGQ 472
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  576 KQRMAMARLFYHKPQFAILDECTSavSVDVEG------YIySHCRKVGITLFTVSHRKSL 629
Cdd:COG4618 473 RQRIGLARALYGDPRLVVLDEPNS--NLDDEGeaalaaAI-RALKARGATVVVITHRPSL 529
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
440-625 1.14e-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: 1.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATPNGD---VLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPERGklfY 507
Cdd:cd03293   1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvtgpGPDRG---Y 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  508 VPQR----PYMtlgTLRDQVIYPDGREDQKRKGISDLVLkEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMAR 583
Cdd:cd03293  78 VFQQdallPWL---TVLDNVALGLELQGVPKAEARERAE-ELLELVGLSGFENA---------YPHQLSGGMRQRVALAR 144
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 4506341  584 LFYHKPQFAILDECTSAVSV----DVEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRETGKTVLLVTH 190
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
436-596 1.15e-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: 1.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  436 ADNIIKFDHVPLA--TPNGDVLI-RDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTKP--ER 502
Cdd:COG1116   4 AAPALELRGVSKRfpTGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIaglekptsGEVL-VDGKPVTGPgpDR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  503 GklfYVPQR----PYMTLgtlRDQVIYP---DGREDQKRKGISDlvlkEYLDNVQLGHILEReggwdsvqdWMDVLSGGE 575
Cdd:COG1116  83 G---VVFQEpallPWLTV---LDNVALGlelRGVPKAERRERAR----ELLELVGLAGFEDA---------YPHQLSGGM 143
                       170       180
                ....*....|....*....|.
gi 4506341  576 KQRMAMARLFYHKPQFAILDE 596
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDE 164
PLN03232 PLN03232
ABC transporter C family member; Provisional
425-618 2.16e-14

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 77.32  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    425 PLIPGAGEIIIADNIIKFDhVPLATPNgdvlIRDLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFGGRLTKpeRG 503
Cdd:PLN03232  607 PLQPGAPAISIKNGYFSWD-SKTSKPT----LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI--RG 679
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    504 KLFYVPQRPYMTLGTLRDQVIYPDGREDQKR-KGISDLVLKEYLDnVQLGHILErEGGWDSVQdwmdvLSGGEKQRMAMA 582
Cdd:PLN03232  680 SVAYVPQVSWIFNATVRENILFGSDFESERYwRAIDVTALQHDLD-LLPGRDLT-EIGERGVN-----ISGGQKQRVSMA 752
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 4506341    583 RLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGI 618
Cdd:PLN03232  753 RAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDEL 788
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
438-625 2.28e-14

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 73.22  E-value: 2.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   438 NIIKFDHVPLATPNGDVLiRDLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLfGGRLTKPERGKLFYVPQRPYMTl 516
Cdd:PRK09544   3 SLVSLENVSVSFGQRRVL-SDVSLELKPGKILTLLGPNGAGKSTLVRvVLGLVAPD-EGVIKRNGKLRIGYVPQKLYLD- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   517 GTLRDQViypdGREDQKRKGISDLVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:PRK09544  80 TTLPLTV----NRFLRLRPGTKKEDILPALKRVQAGHLIDAP---------MQKLSGGETQRVLLARALLNRPQLLVLDE 146
                        170       180       190
                 ....*....|....*....|....*....|...
gi 4506341   597 CTSAVSVDVEGYIYSHC----RKVGITLFTVSH 625
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIdqlrRELDCAVLMVSH 179
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
451-625 3.05e-14

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: 72.17  E-value: 3.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGR-LTK--PERGKLFYVPQR----PYMt 515
Cdd:cd03259  11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIaglerpdsGEI--LIDGRdVTGvpPERRNIGMVFQDyalfPHL- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  516 lgTLRDQVIYPDGREDQKRKGISDLVlKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:cd03259  88 --TVAENIAFGLKLRGVPKAEIRARV-RELLELVGLEGLLNR---------YPHELSGGQQQRVALARALAREPSLLLLD 155
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4506341  596 ECTSAvsVDVE------GYIYSHCRKVGITLFTVSH 625
Cdd:cd03259 156 EPLSA--LDAKlreelrEELKELQRELGITTIYVTH 189
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
452-596 3.06e-14

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 75.87  E-value: 3.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  452 GDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLfGGRLTKPERGKLFYVPQ-RPYMTLG-TLRDQVIypDG 528
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGELEPD-SGTVKLGETVKIGYFDQhQEELDPDkTVLDELR--DG 403
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4506341  529 REDQKRKGISDLvlkeyldnvqLGHILEREggwDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:COG0488 404 APGGTEQEVRGY----------LGRFLFSG---DDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
450-607 3.29e-14

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: 71.30  E-value: 3.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    450 PNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGRLTKPERGKLFYVPQRPYMTLGTLRDQV 523
Cdd:TIGR01166   2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLnGLLRPqsgavLIDGEPLDYSRKGLLERRQRVGLVFQDPDDQL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    524 IYPDGRED----QKRKGISD----LVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:TIGR01166  82 FAADVDQDvafgPLNLGLSEaeveRRVREALTAVGASGLRERP---------THCLSGGEKKRVAIAGAVAMRPDVLLLD 152
                         170
                  ....*....|..
gi 4506341    596 ECTSAvsVDVEG 607
Cdd:TIGR01166 153 EPTAG--LDPAG 162
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
440-626 4.01e-14

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 75.63  E-value: 4.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   440 IKFDHVPLATPNG-DVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTK-PE---RGKLF 506
Cdd:PRK11160 339 LTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLtrawdpqqGEIL-LNGQPIADySEaalRQAIS 417
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   507 YVPQRPYMTLGTLRDQVIYPDgredqkrKGISDLVLKEYLDNVQLGHILEREGGWDSvqdWMD----VLSGGEKQRMAMA 582
Cdd:PRK11160 418 VVSQRVHLFSATLRDNLLLAA-------PNASDEALIEVLQQVGLEKLLEDDKGLNA---WLGeggrQLSGGEQRRLGIA 487
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 4506341   583 RLFYHKPQFAILDECTSAVSVDVEGYIYS----HCRkvGITLFTVSHR 626
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILEllaeHAQ--NKTVLMITHR 533
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
456-625 4.43e-14

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 72.00  E-value: 4.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWplFGGR----LTKPERGKL------FyVPQR----PY 513
Cdd:COG1136  24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggldrptsGEVL--IDGQdissLSERELARLrrrhigF-VFQFfnllPE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  514 MTLgtlRDQVIYP------DGREDQKRkgisdlvLKEYLDNVQLGHILER---EggwdsvqdwmdvLSGGEKQRMAMARL 584
Cdd:COG1136 101 LTA---LENVALPlllagvSRKERRER-------ARELLERVGLGDRLDHrpsQ------------LSGGQQQRVAIARA 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 4506341  585 FYHKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:COG1136 159 LVNRPKLILADEPTGNLdsktGEEVLELLRELNRELGTTIVMVTH 203
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
436-625 4.67e-14

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: 74.94  E-value: 4.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  436 ADNIIKFDHV----PLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------------GELWPLFGGRL 497
Cdd:COG1123 257 AEPLLEVRNLskryPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLlgllrptsgsilfdGKDLTKLSRRS 336
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  498 TKPERGKLFYVPQRPYMTL---GTLRDQVIYP-DGREDQKRKGISDLVlKEYLDNVQLG-HILER---Eggwdsvqdwmd 569
Cdd:COG1123 337 LRELRRRVQMVFQDPYSSLnprMTVGDIIAEPlRLHGLLSRAERRERV-AELLERVGLPpDLADRyphE----------- 404
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  570 vLSGGEKQRMAMARLFYHKPQFAILDECTSA--VSV--DVEGYIYSHCRKVGITLFTVSH 625
Cdd:COG1123 405 -LSGGQRQRVAIARALALEPKLLILDEPTSAldVSVqaQILNLLRDLQRELGLTYLFISH 463
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
456-625 8.27e-14

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 72.02  E-value: 8.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELwplfggrlTKPERGKLFyVPQRPymtLGTLRD--QVIYPDGREdqk 533
Cdd:PRK11247  28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL--------ETPSAGELL-AGTAP---LAEAREdtRLMFQDARL--- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   534 rkgisdLVLKEYLDNVQLG----------HILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVS- 602
Cdd:PRK11247  93 ------LPWKKVIDNVGLGlkgqwrdaalQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDa 166
                        170       180
                 ....*....|....*....|....*.
gi 4506341   603 ---VDVEGYIYSHCRKVGITLFTVSH 625
Cdd:PRK11247 167 ltrIEMQDLIESLWQQHGFTVLLVTH 192
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
451-620 9.86e-14

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 70.67  E-value: 9.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGklfyvpqrpyMTLGTLRDQVIY---PD 527
Cdd:PRK13539  13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----------IDDPDVAEACHYlghRN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   528 G-------RED----QKRKGISDLVLKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLF-YHKPQFaILD 595
Cdd:PRK13539  83 AmkpaltvAENlefwAAFLGGEELDIAAALEAVGLAPLAHLPFG---------YLSAGQKRRVALARLLvSNRPIW-ILD 152
                        170       180
                 ....*....|....*....|....*....
gi 4506341   596 ECTSAVSVD----VEGYIYSHCRKVGITL 620
Cdd:PRK13539 153 EPTAALDAAavalFAELIRAHLAQGGIVI 181
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
434-604 1.03e-13

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: 71.43  E-value: 1.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  434 IIADNIIK-FDHVPLatpngdvlIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGRLTKPE---R 502
Cdd:COG4555   2 IEVENLSKkYGKVPA--------LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLaGLLKPdsgsilIDGEDVRKEPreaR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  503 GKLFYVPQRPYMTLG-TLRDQV-----IYPDGREDQKRKgisdlvLKEYLDNVQLGHILEReggwdSVQDwmdvLSGGEK 576
Cdd:COG4555  74 RQIGVLPDERGLYDRlTVRENIryfaeLYGLFDEELKKR------IEELIELLGLEEFLDR-----RVGE----LSTGMK 138
                       170       180
                ....*....|....*....|....*...
gi 4506341  577 QRMAMARLFYHKPQFAILDECTSAVSVD 604
Cdd:COG4555 139 KKVALARALVHDPKVLLLDEPTNGLDVM 166
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
456-625 1.40e-13

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 70.86  E-value: 1.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTKPE---RGKLFYVPQRP--YMTLgTLRDQ 522
Cdd:COG1131  16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLlgllrptsGEVR-VLGEDVARDPaevRRRIGYVPQEPalYPDL-TVREN 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  523 V-----IYPDGREDQKRKgisdlvLKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDEC 597
Cdd:COG1131  94 LrffarLYGLPRKEARER------IDELLELFGLTDAADR---------KVGTLSGGMKQRLGLALALLHDPELLILDEP 158
                       170       180       190
                ....*....|....*....|....*....|....
gi 4506341  598 TSAvsVDVEG------YIYSHCRKvGITLFTVSH 625
Cdd:COG1131 159 TSG--LDPEArrelweLLRELAAE-GKTVLLSTH 189
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
124-640 2.50e-13

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: 72.83  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    124 RYLLNFIAAMpLISLVNNFLKYGlnelklcFRVRLtkylYEEYLQA----FTYYKMGNLDNRIanpdqllTQDVEKFCNS 199
Cdd:TIGR02203  67 RGICSFVSTY-LLSWVSNKVVRD-------IRVRM----FEKLLGLpvsfFDRQPTGTLLSRI-------TFDSEQVASA 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    200 VVDLYSNLSKP-----FLDIVL--YIFKLTSAIGAQGPASMMAYLVVSglflTRLRRPIGKMtiteQKYEGEYRYVNSRL 272
Cdd:TIGR02203 128 ATDAFIVLVREtltviGLFIVLlyYSWQLTLIVVVMLPVLSILMRRVS----KRLRRISKEI----QNSMGQVTTVAEET 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    273 ITNSEEIAFYNGNKREKQtvhsvfrklvehlhnfilfRFsmGFIDSIIAKYLATVVGYLVVSRPFldlshprhlksthSE 352
Cdd:TIGR02203 200 LQGYRVVKLFGGQAYETR-------------------RF--DAVSNRNRRLAMKMTSAGSISSPI-------------TQ 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    353 LLEDYYQSGRMLLRMSQALGRIVLAGremtrlaGFTARITELMQVLKDLNHgkyeRTMVSQQ-EKGIEGVQVI------P 425
Cdd:TIGR02203 246 LIASLALAVVLFIALFQAQAGSLTAG-------DFTAFITAMIALIRPLKS----LTNVNAPmQRGLAAAESLftlldsP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    426 LIPGAGEIII--ADNIIKFDHVPLATPNGDV-LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---- 498
Cdd:TIGR02203 315 PEKDTGTRAIerARGDVEFRNVTFRYPGRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILldgh 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    499 -------KPERGKLFYVPQRPYMTLGTLRDQVIYPDGRE---DQKRKGISDLVLKEYLDNVQLGhiLEREGGWDSVQdwm 568
Cdd:TIGR02203 395 dladytlASLRRQVALVSQDVVLFNDTIANNIAYGRTEQadrAEIERALAAAYAQDFVDKLPLG--LDTPIGENGVL--- 469
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4506341    569 dvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKSLWKHHEYYLHMD 640
Cdd:TIGR02203 470 --LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLmqGRTTLVIAHRLSTIEKADRIVVMD 541
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
439-598 4.01e-13

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 68.93  E-value: 4.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  439 IIKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFGGRLTKPERGKLfyvpqr 511
Cdd:COG2884   1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLyGEERPtsgqvlVNGQDLSRLKRREI------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  512 PYM--TLGT-------LRD-----------QVIYPDGREDQKRkgisdlvLKEYLDNVQLGHILEReggwdsvqdwM-DV 570
Cdd:COG2884  75 PYLrrRIGVvfqdfrlLPDrtvyenvalplRVTGKSRKEIRRR-------VREVLDLVGLSDKAKA----------LpHE 137
                       170       180
                ....*....|....*....|....*...
gi 4506341  571 LSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:COG2884 138 LSGGEQQRVAIARALVNRPELLLADEPT 165
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
456-625 5.14e-13

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: 67.42  E-value: 5.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTKPE---RGKLFYVPQRPYmtlgtlrdqvI 524
Cdd:cd03230  16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlgllkpdsGEIK-VLGKDIKKEPeevKRRIGYLPEEPS----------L 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  525 YPdgredqkrkgisDLVLKEYLDnvqlghilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAV--- 601
Cdd:cd03230  85 YE------------NLTVRENLK-----------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLdpe 129
                       170       180
                ....*....|....*....|....*
gi 4506341  602 -SVDVEGYIYSHcRKVGITLFTVSH 625
Cdd:cd03230 130 sRREFWELLREL-KKEGKTILLSSH 153
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
439-625 5.70e-13

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: 68.69  E-value: 5.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  439 IIKFDHVPLATPNGD---VLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------------GELWPLFGGRLTKPE 501
Cdd:cd03257   1 LLEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAIlgllkptsgsiifdGKDLLKLSRRLRKIR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  502 RGKLFYVPQRPYMTLG---TLRDQVIYP-----DGREDQKRKGISDLVLKEYLDNVQLGHILEREggwdsvqdwmdvLSG 573
Cdd:cd03257  81 RKEIQMVFQDPMSSLNprmTIGEQIAEPlrihgKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHE------------LSG 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4506341  574 GEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSH----CRKVGITLFTVSH 625
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLlkklQEELGLTLLFITH 204
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
440-625 7.47e-13

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: 68.75  E-value: 7.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggRLTKPERGKLFY----VPQRPYMT 515
Cdd:cd03256   1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLN--------GLVEPTSGSVLIdgtdINKLKGKA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  516 LGTLRDQV--IYPDGRedqkrkgisdLVLKEY-LDNVQLG------------------------HILEREGGWDSVQDWM 568
Cdd:cd03256  73 LRQLRRQIgmIFQQFN----------LIERLSvLENVLSGrlgrrstwrslfglfpkeekqralAALERVGLLDKAYQRA 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506341  569 DVLSGGEKQRMAMARLFYHKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03256 143 DQLSGGQQQRVAIARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLH 203
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
451-600 1.47e-12

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 68.26  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP------LFG---GRLTKPERGKLFYV-PQRPYMTLGTL 519
Cdd:PRK13548  13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGELSPdsgevrLNGrplADWSPAELARRRAVlPQHSSLSFPFT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   520 RDQVI----YPDGREDQKRKGISDlvlkEYLDNVQLGHILEReggwdSVQdwmdVLSGGEKQRMAMARLF------YHKP 589
Cdd:PRK13548  93 VEEVVamgrAPHGLSRAEDDALVA----AALAQVDLAHLAGR-----DYP----QLSGGEQQRVQLARVLaqlwepDGPP 159
                        170
                 ....*....|.
gi 4506341   590 QFAILDECTSA 600
Cdd:PRK13548 160 RWLLLDEPTSA 170
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
434-598 1.86e-12

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 70.26  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   434 IIADNIIKFdhvplaTPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-------GELwpLFGG----RLTKPE- 501
Cdd:PRK11174 350 IEAEDLEIL------SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlgflpyqGSL--KINGielrELDPESw 421
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   502 RGKLFYVPQRPYMTLGTLRDQVIYpdGREDqkrkgISDLVLKEYLDNVQLGHILER-EGGWDS-VQDWMDVLSGGEKQRM 579
Cdd:PRK11174 422 RKHLSWVGQNPQLPHGTLRDNVLL--GNPD-----ASDEQLQQALENAWVSEFLPLlPQGLDTpIGDQAAGLSVGQAQRL 494
                        170
                 ....*....|....*....
gi 4506341   580 AMARLFYHKPQFAILDECT 598
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPT 513
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
408-612 1.97e-12

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: 70.74  E-value: 1.97e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341     408 RTMVSQQEKGIEGVQVIPLIPGAG-EIIIADNIIKFDHVPLATPNGdvlirdLNFEVRSGANVLICGPNGCGKSSLFR-V 485
Cdd:TIGR00957  611 RIFLSHEELEPDSIERRTIKPGEGnSITVHNATFTWARDLPPTLNG------ITFSIPEGALVAVVGQVGCGKSSLLSaL 684
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341     486 LGELWPLFGGRLTKperGKLFYVPQRPYMTLGTLRDQVIYPDGREDQKRKGI-------SDLVLKEYLDNVQLGhilerE 558
Cdd:TIGR00957  685 LAEMDKVEGHVHMK---GSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVleacallPDLEILPSGDRTEIG-----E 756
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 4506341     559 GGWDsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSH 612
Cdd:TIGR00957  757 KGVN--------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
437-599 2.31e-12

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: 67.42  E-value: 2.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  437 DNIIKFDHVPLATpNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-------LFGGRLTKPE----RGK 504
Cdd:COG1119   1 DPLLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItGDLPPtygndvrLFGERRGGEDvwelRKR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  505 LFYV-P--QRPYMTLGTLRDQVI---------YPDGREDQKRKGisdlvlKEYLDNVQLGHILEREggwdsvqdwMDVLS 572
Cdd:COG1119  80 IGLVsPalQLRFPRDETVLDVVLsgffdsiglYREPTDEQRERA------RELLELLGLAHLADRP---------FGTLS 144
                       170       180
                ....*....|....*....|....*..
gi 4506341  573 GGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTA 171
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
455-625 3.63e-12

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: 65.74  E-value: 3.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  455 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGGRLTKPE--RGKLFYVPQRPYMTLG--TLRDQVI 524
Cdd:cd03226  15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKessgsiLLNGKPIKAKerRKSIGYVMQDVDYQLFtdSVREELL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  525 Y----PDGREDQKRKGISDLVLKEYLDNvqlgHILEreggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSA 600
Cdd:cd03226  95 LglkeLDAGNEQAETVLKDLDLYALKER----HPLS--------------LSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
                       170       180
                ....*....|....*....|....*...
gi 4506341  601 V---SVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03226 157 LdykNMERVGELIRELAAQGKAVIVITH 184
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
440-598 6.62e-12

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: 63.62  E-value: 6.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATpNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQrpymtlgtl 519
Cdd:cd03221   1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4506341  520 rdqviypdgredqkrkgisdlvlkeyldnvqlghilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:cd03221  71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
454-600 1.10e-11

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: 64.47  E-value: 1.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  454 VLiRDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLfyvpqrpymtlgTLRDQVIYPDGRE-DQ 532
Cdd:cd03262  15 VL-KGIDLTVKKGEVVVIIGPSGSGKSTLLRCI--------NLLEEPDSGTI------------IIDGLKLTDDKKNiNE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  533 KRKGISdLVLKEY--------LDNVQLG-----------------HILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYH 587
Cdd:cd03262  74 LRQKVG-MVFQQFnlfphltvLENITLApikvkgmskaeaeeralELLEKVGLADKADAYPAQLSGGQQQRVAIARALAM 152
                       170
                ....*....|...
gi 4506341  588 KPQFAILDECTSA 600
Cdd:cd03262 153 NPKVMLFDEPTSA 165
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
452-625 1.17e-11

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: 65.05  E-value: 1.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  452 GDVLIRDLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWP------LFGGRLT--KPERGKLFYVPQR----PYMTLgt 518
Cdd:cd03299  11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLEtIAGFIKPdsgkilLNGKDITnlPPEKRDISYVPQNyalfPHMTV-- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  519 lRDQVIYPDGREDQKRKGISDLVlKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:cd03299  89 -YKNIAYGLKKRKVDKKEIERKV-LEIAEMLGIDHLLNRKPE---------TLSGGEQQRVAIARALVVNPKILLLDEPF 157
                       170       180       190
                ....*....|....*....|....*....|.
gi 4506341  599 SAVSVDVEGYIYSHCRKV----GITLFTVSH 625
Cdd:cd03299 158 SALDVRTKEKLREELKKIrkefGVTVLHVTH 188
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
428-626 1.32e-11

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: 64.36  E-value: 1.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  428 PGAGEIIIADNIIKFdhvplaTPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplFggRLTKPERGK--- 504
Cdd:cd03369   2 PEHGEIEVENLSVRY------APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILAL------F--RFLEAEEGKiei 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  505 ----------------LFYVPQRPYMTLGTLRdqviypdgredqkrkgiSDL-VLKEYlDNVQLGHILE-REGGwdsvqd 566
Cdd:cd03369  68 dgidistipledlrssLTIIPQDPTLFSGTIR-----------------SNLdPFDEY-SDEEIYGALRvSEGG------ 123
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4506341  567 wmDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRK--VGITLFTVSHR 626
Cdd:cd03369 124 --LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREefTNSTILTIAHR 183
PTZ00243 PTZ00243
ABC transporter; Provisional
454-653 1.34e-11

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 68.27  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    454 VLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWPlfggrltkpERgKLFYVPQRPYMTLGTLRDQVIY 525
Cdd:PTZ00243  674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLlsqfeiseGRVWA---------ER-SIAYVPQQAWIMNATVRGNILF 743
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    526 PDgREDQKRkgISDLVLKEYL--DNVQLGHILEREGGWDSVQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSV 603
Cdd:PTZ00243  744 FD-EEDAAR--LADAVRVSQLeaDLAQLGGGLETEIGEKGVN-----LSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4506341    604 DVEGYIYSHC---RKVGITLFTVSHRKSLWKHHEYYLHMdGRGNYEFKQITED 653
Cdd:PTZ00243  816 HVGERVVEECflgALAGKTRVLATHQVHVVPRADYVVAL-GDGRVEFSGSSAD 867
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
455-629 1.51e-11

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 64.59  E-value: 1.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  455 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVlgelwpLFGGRLTKPERGKlFYVPQRPYMTLGTLRDQvIYPDGREDQKr 534
Cdd:COG2401  45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRL------LAGALKGTPVAGC-VDVPDNQFGREASLIDA-IGRKGDFKDA- 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  535 kgisdlvlKEYLDNVQLGhilereggwdSVQDWM---DVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVeGYIYS 611
Cdd:COG2401 116 --------VELLNAVGLS----------DAVLWLrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT-AKRVA 176
                       170       180
                ....*....|....*....|...
gi 4506341  612 H-----CRKVGITLFTVSHRKSL 629
Cdd:COG2401 177 RnlqklARRAGITLVVATHHYDV 199
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
451-596 1.85e-11

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 64.04  E-value: 1.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSL-----------FRVLGELWpLFGGRLTK--PERGKLFYVPQR----PY 513
Cdd:COG4136  12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLlaaiagtlspaFSASGEVL-LNGRRLTAlpAEQRRIGILFQDdllfPH 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  514 MTLG-----TLRDQViypdGREDQKRKgisdlvLKEYLDNVQLGHILEReggwDSVQdwmdvLSGGEKQRMAMARLFYHK 588
Cdd:COG4136  91 LSVGenlafALPPTI----GRAQRRAR------VEQALEEAGLAGFADR----DPAT-----LSGGQRARVALLRALLAE 151

                ....*...
gi 4506341  589 PQFAILDE 596
Cdd:COG4136 152 PRALLLDE 159
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
454-625 2.17e-11

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 63.67  E-value: 2.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   454 VLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GelwplfggrLTKPERGKLFYVPQRpymtlgtLRDQviypdgREDQ 532
Cdd:PRK13538  15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILaG---------LARPDAGEVLWQGEP-------IRRQ------RDEY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   533 KRK--------GISDLV-----------LKEYLDNVQLGHILEREGgwdsVQDWMDV----LSGGEKQRMAMARLFYHKP 589
Cdd:PRK13538  73 HQDllylghqpGIKTELtalenlrfyqrLHGPGDDEALWEALAQVG----LAGFEDVpvrqLSAGQQRRVALARLWLTRA 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 4506341   590 QFAILDECTSAVSV----DVEGYIYSHCRKVGITLFTvSH 625
Cdd:PRK13538 149 PLWILDEPFTAIDKqgvaRLEALLAQHAEQGGMVILT-TH 187
cbiO PRK13640
energy-coupling factor transporter ATPase;
437-625 2.80e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 64.82  E-value: 2.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   437 DNIIKFDHVPLATPNGDV-LIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP---------LFGGRLTKPE---- 501
Cdd:PRK13640   3 DNIVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLInGLLLPddnpnskitVDGITLTAKTvwdi 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   502 RGKLFYVPQRP--YMTLGTLRDQVIYpdGREDqkrKGISDLVLKEYLDNVqlghiLEREGGWDSVQDWMDVLSGGEKQRM 579
Cdd:PRK13640  83 REKVGIVFQNPdnQFVGATVGDDVAF--GLEN---RAVPRPEMIKIVRDV-----LADVGMLDYIDSEPANLSGGQKQRV 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 4506341   580 AMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV----GITLFTVSH 625
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITH 202
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
428-642 3.06e-11

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 66.52  E-value: 3.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   428 PGAGEIIIADNIIKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--------- 498
Cdd:PRK13657 323 PGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgtdirtv 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   499 --KPERGKLFYVPQRPYMTLGTLRD--QViypdGREDQkrkgiSDLVLKEYLDNVQ-LGHILEREGGWDS-VQDWMDVLS 572
Cdd:PRK13657 403 trASLRRNIAVVFQDAGLFNRSIEDniRV----GRPDA-----TDEEMRAAAERAQaHDFIERKPDGYDTvVGERGRQLS 473
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   573 GGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEgyiyshcRKV---------GITLFTVSHRKSLWKHHEYYLHMD-GR 642
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVETE-------AKVkaaldelmkGRTTFIIAHRLSTVRNADRILVFDnGR 546
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
451-622 4.28e-11

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 62.76  E-value: 4.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTkpergklfyVPQRPYMTLGTLRDQVIYPDGRE 530
Cdd:TIGR01189  11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVR---------WNGTPLAEQRDEPHENILYLGHL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    531 DqkrkGI-SDLVLKEYLDNVQLGHILEREGGWDSVQDwMDV----------LSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:TIGR01189  82 P----GLkPELSALENLHFWAAIHGGAQRTIEDALAA-VGLtgfedlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTT 156
                         170       180
                  ....*....|....*....|....*..
gi 4506341    600 AVSVD----VEGYIYSHCRKVGITLFT 622
Cdd:TIGR01189 157 ALDKAgvalLAGLLRAHLARGGIVLLT 183
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
440-640 4.32e-11

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: 65.92  E-value: 4.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    440 IKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGRLTK-----PERGKLF 506
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLvgffqarsGEI--LLNGFSLKdidrhTLRQFIN 551
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    507 YVPQRPYMTLGTLRDQVIY---PDGREDQKRKGISDLVLKEYLDNVQLGH--ILEREGGwdsvqdwmdVLSGGEKQRMAM 581
Cdd:TIGR01193 552 YLPQEPYIFSGSILENLLLgakENVSQDEIWAACEIAEIKDDIENMPLGYqtELSEEGS---------SISGGQKQRIAL 622
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    582 ARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVG-ITLFTVSHRKSLWKHHEYYLHMD 640
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQdKTIIFVAHRLSVAKQSDKIIVLD 682
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
428-600 5.95e-11

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: 65.61  E-value: 5.95e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  428 PGAGEIIIADNIIKFDHVPLA-TPNGDVLiRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-------- 498
Cdd:COG5265 346 PDAPPLVVGGGEVRFENVSFGyDPERPIL-KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILidgqdird 424
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  499 -KPE--RGKLFYVPQRPYMTLGTLRDQVIYpdGREDqkrkgISDLVLKEYLDNVQLGHILER-EGGWDSVqdwmdV---- 570
Cdd:COG5265 425 vTQAslRAAIGIVPQDTVLFNDTIAYNIAY--GRPD-----ASEEEVEAAARAAQIHDFIESlPDGYDTR-----Vgerg 492
                       170       180       190
                ....*....|....*....|....*....|..
gi 4506341  571 --LSGGEKQRMAMARLFYHKPQFAILDECTSA 600
Cdd:COG5265 493 lkLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
458-625 6.36e-11

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: 62.23  E-value: 6.36e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  458 DLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTkpERGKLFYVPQRPYMTLGTLRD-QVIYPD--GRED--- 531
Cdd:cd03268  18 DISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT--FDGKSYQKNIEALRRIGALIEaPGFYPNltARENlrl 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  532 -QKRKGISDLVLKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTSAvsVDVEG--- 607
Cdd:cd03268  96 lARLLGIRKKRIDEVLDVVGLKDSAKKKVK---------GFSLGMKQRLGIALALLGNPDLLILDEPTNG--LDPDGike 164
                       170       180
                ....*....|....*....|.
gi 4506341  608 ---YIYSHcRKVGITLFTVSH 625
Cdd:cd03268 165 lreLILSL-RDQGITVLISSH 184
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
456-625 7.09e-11

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


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 62.74  E-value: 7.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWplFGGR----LTKPERGKLFyVPQR----PYMTLGT- 518
Cdd:cd03296  18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIaglerpdsGTIL--FGGEdatdVPVQERNVGF-VFQHyalfRHMTVFDn 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  519 ----LRDQVIYPDGREDQKRKGISDLvlkeyLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:cd03296  95 vafgLRVKPRSERPPEAEIRAKVHEL-----LKLVQLDWLADR---------YPAQLSGGQRQRVALARALAVEPKVLLL 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 4506341  595 DECTSAVSVDVEGYIYSHCRK----VGITLFTVSH 625
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRlhdeLHVTTVFVTH 195
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
440-598 8.28e-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: 62.21  E-value: 8.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATPNGDVLiRDLNFEVRSGANVLIcGPNGCGKSSLFRVLGELWPLFGGRLT--------KPE--RGKLFYVP 509
Cdd:cd03264   1 LQLENLTKRYGKKRAL-DGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRidgqdvlkQPQklRRRIGYLP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  510 Q--RPYMTLgTLRDQVIYpdgredQKR-KGISDLVLKEYLDNVqlghiLEREGGWDSVQDWMDVLSGGEKQRMAMARLFY 586
Cdd:cd03264  79 QefGVYPNF-TVREFLDY------IAWlKGIPSKEVKARVDEV-----LELVNLGDRAKKKIGSLSGGMRRRVGIAQALV 146
                       170
                ....*....|..
gi 4506341  587 HKPQFAILDECT 598
Cdd:cd03264 147 GDPSILIVDEPT 158
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
451-625 1.03e-10

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 61.48  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLfGGRLTKPERGKLFYVPQR-------PY-----MTLG 517
Cdd:NF040873   3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLaGVLRPT-SGTVRRAGGARVAYVPQRsevpdslPLtvrdlVAMG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   518 TLRDQVIY-PDGREDQkrkgisdLVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:NF040873  82 RWARRGLWrRLTRDDR-------AAVDDALERVGLADLAGRQ---------LGELSGGQRQRALLAQGLAQEADLLLLDE 145
                        170       180       190
                 ....*....|....*....|....*....|..
gi 4506341   597 CTSAVSVDVEGYIYSHCRKV---GITLFTVSH 625
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEharGATVVVVTH 177
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
456-641 1.09e-10

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: 61.96  E-value: 1.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  456 IRDLNFEVRSGANVLICGPNGCGKSSLF-RVLGELWPLFG--------------GRLTKPERGKLFYVPQRPYMTLGTLR 520
Cdd:cd03290  17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGkvhwsnknesepsfEATRSRNRYSVAYAAQKPWLLNATVE 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  521 DQVIYPDGREDQKRKGIS-------DLVLKEYLDNVQLGhilerEGGWDsvqdwmdvLSGGEKQRMAMARLFYHKPQFAI 593
Cdd:cd03290  97 ENITFGSPFNKQRYKAVTdacslqpDIDLLPFGDQTEIG-----ERGIN--------LSGGQRQRICVARALYQNTNIVF 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4506341  594 LDECTSAVSVdvegYIYSHCRKVGI---------TLFTVSHRKSLWKHHEYYLHM-DG 641
Cdd:cd03290 164 LDDPFSALDI----HLSDHLMQEGIlkflqddkrTLVLVTHKLQYLPHADWIIAMkDG 217
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
451-625 1.19e-10

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: 61.87  E-value: 1.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGR----LTKPERG--------KLFyvpq 510
Cdd:cd03300  11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIagfetptsGEI--LLDGKditnLPPHKRPvntvfqnyALF---- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  511 rPYMTLGtlrDQVIYPDGREDQKRKGISDLVlKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQ 590
Cdd:cd03300  85 -PHLTVF---ENIAFGLRLKKLPKAEIKERV-AEALDLVQLEGYANRK---------PSQLSGGQQQRVAIARALVNEPK 150
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 4506341  591 FAILDECTSAVSV----DVEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03300 151 VLLLDEPLGALDLklrkDMQLELKRLQKELGITFVFVTH 189
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
452-625 1.27e-10

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: 61.35  E-value: 1.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  452 GDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERG----------KLFYVPQRPYM--TLGTL 519
Cdd:cd03231  12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPldfqrdsiarGLLYLGHAPGIktTLSVL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  520 RD-QVIYPDGREDQkrkgisdlvLKEYLDNVQLGHILEREGGWdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:cd03231  92 ENlRFWHADHSDEQ---------VEEALARVGLNGFEDRPVAQ---------LSAGQQRRVALARLLLSGRPLWILDEPT 153
                       170       180       190
                ....*....|....*....|....*....|.
gi 4506341  599 SAV---SVD-VEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03231 154 TALdkaGVArFAEAMAGHCARGGMVVLTTHQ 184
PLN03130 PLN03130
ABC transporter C family member; Provisional
458-615 1.45e-10

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 64.76  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    458 DLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFGGRLTKpeRGKLFYVPQRPYMTLGTLRDQVIYpdGRE-DQKR- 534
Cdd:PLN03130  635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI--RGTVAYVPQVSWIFNATVRDNILF--GSPfDPERy 710
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    535 -KGISDLVLKEYLDNVQLGHILE-REGGWDsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSH 612
Cdd:PLN03130  711 eRAIDVTALQHDLDLLPGGDLTEiGERGVN--------ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDK 782

                  ...
gi 4506341    613 CRK 615
Cdd:PLN03130  783 CIK 785
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
458-625 1.92e-10

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


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 62.82  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    458 DLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL---------------TKPERGKLFYVPQR----PYMTLgt 518
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfdsrkgifLPPEKRRIGYVFQEarlfPHLSV-- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    519 lRDQVIYPDGREDQKRKGISDLVLKEYLDnvqLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:TIGR02142  93 -RGNLRYGMKRARPSERRISFERVIELLG---IGHLLGRLPG---------RLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 4506341    599 SAVSV----DVEGYIYSHCRKVGITLFTVSH 625
Cdd:TIGR02142 160 AALDDprkyEILPYLERLHAEFGIPILYVSH 190
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
452-596 8.24e-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: 59.19  E-value: 8.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  452 GDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL---------TKPERGKLFYVPQR----PYMtlgT 518
Cdd:cd03301  12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtdLPPKDRDIAMVFQNyalyPHM---T 88
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4506341  519 LRDQVIYPDGREDQKRKGISDLVlKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:cd03301  89 VYDNIAFGLKLRKVPKDEIDERV-REVAELLQIEHLLDRK---------PKQLSGGQRQRVALGRAIVREPKVFLMDE 156
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
449-613 8.65e-10

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: 8.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341     449 TPNGDV-------------LIRDLNFEVRSGANVLICGPNGCGKSSLFRV-LGELWPLFGgrlTKPERGKLFYVPQRPYM 514
Cdd:TIGR01271  422 QPNGDDglffsnfslyvtpVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMiMGELEPSEG---KIKHSGRISFSPQTSWI 498
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341     515 TLGTLRDQVIYPDGREDQKRKGI-------SDLVLKEYLDNVQLGhilerEGGWdsvqdwmdVLSGGEKQRMAMARLFYH 587
Cdd:TIGR01271  499 MPGTIKDNIIFGLSYDEYRYTSVikacqleEDIALFPEKDKTVLG-----EGGI--------TLSGGQRARISLARAVYK 565
                          170       180
                   ....*....|....*....|....*.
gi 4506341     588 KPQFAILDECTSAVSVDVEGYIYSHC 613
Cdd:TIGR01271  566 DADLYLLDSPFTHLDVVTEKEIFESC 591
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
437-613 1.06e-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: 59.87  E-value: 1.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  437 DNIIKFDHVPL-ATPngdvLIRDLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFGgrlTKPERGKLFYVPQRPYM 514
Cdd:cd03291  37 DNNLFFSNLCLvGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELEPSEG---KIKHSGRISFSSQFSWI 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  515 TLGTLRDQVIYPDGREDQKRKGI-------SDLVLKEYLDNVQLGhilerEGGWdsvqdwmdVLSGGEKQRMAMARLFYH 587
Cdd:cd03291 110 MPGTIKENIIFGVSYDEYRYKSVvkacqleEDITKFPEKDNTVLG-----EGGI--------TLSGGQRARISLARAVYK 176
                       170       180
                ....*....|....*....|....*.
gi 4506341  588 KPQFAILDECTSAVSVDVEGYIYSHC 613
Cdd:cd03291 177 DADLYLLDSPFGYLDVFTEKEIFESC 202
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
440-599 1.06e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 59.62  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   440 IKFDHVPLATPNGDVL-IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWplfggrltKPERGKLF-YVPQRPYMTLG 517
Cdd:PRK13632   8 IKVENVSFSYPNSENNaLKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL--------KPQSGEIKiDGITISKENLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   518 TLRDQV--IY--PD--------------GREDQK--RKGISDLVLkEYLDNVQLGHILEREGgwdsvqdwmDVLSGGEKQ 577
Cdd:PRK13632  80 EIRKKIgiIFqnPDnqfigatveddiafGLENKKvpPKKMKDIID-DLAKKVGMEDYLDKEP---------QNLSGGQKQ 149
                        170       180
                 ....*....|....*....|..
gi 4506341   578 RMAMARLFYHKPQFAILDECTS 599
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTS 171
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
454-596 1.11e-09

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 60.50  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   454 VLIRDLNFEVRSGANVLICGPNGCGKSSLFRvlgelwpLFGGrLTKPERGKLFY---------VPQR------------P 512
Cdd:PRK11432  20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLR-------LVAG-LEKPTEGQIFIdgedvthrsIQQRdicmvfqsyalfP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   513 YMTLGtlrDQVIYPDGREDQKRKGISDLVlKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFA 592
Cdd:PRK11432  92 HMSLG---ENVGYGLKMLGVPKEERKQRV-KEALELVDLAGFEDR---------YVDQISGGQQQRVALARALILKPKVL 158

                 ....
gi 4506341   593 ILDE 596
Cdd:PRK11432 159 LFDE 162
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
457-626 1.71e-09

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: 57.05  E-value: 1.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  457 RDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplFGgrLTKPERGKLFyvpqrpymtlgtLRDQVIYPDGREDQKRKG 536
Cdd:cd03216  17 DGVSLSVRRGEVHALLGENGAGKSTLMKIL------SG--LYKPDSGEIL------------VDGKEVSFASPRDARRAG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  537 ISdLVlkeyldnvqlgHilereggwdsvQdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV 616
Cdd:cd03216  77 IA-MV-----------Y-----------Q-----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL 128
                       170
                ....*....|...
gi 4506341  617 ---GITLFTVSHR 626
Cdd:cd03216 129 raqGVAVIFISHR 141
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
436-599 2.01e-09

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 58.87  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   436 ADNIIKFDHVPLATPNGDVL-IRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGRLTKPE-----RG 503
Cdd:PRK13635   2 KEEIIRVEHISFRYPDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLnGLLLPeagtiTVGGMVLSEEtvwdvRR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   504 KLFYVPQRP--YMTLGTLRDQVIYpdGREDQkrkGI--SDLV--LKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQ 577
Cdd:PRK13635  82 QVGMVFQNPdnQFVGATVQDDVAF--GLENI---GVprEEMVerVDQALRQVGMEDFLNREPH---------RLSGGQKQ 147
                        170       180
                 ....*....|....*....|..
gi 4506341   578 RMAMARLFYHKPQFAILDECTS 599
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATS 169
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
434-625 3.35e-09

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: 57.38  E-value: 3.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  434 IIADNIIKfdhvplaTPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT----------KPERG 503
Cdd:cd03265   1 IEVENLVK-------KYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvaghdvvrepREVRR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  504 KLFYVPQRPymtlgTLRDQVIypdGRED----QKRKGISDLVLKEYLDNVqlghiLEREGGWDSVQDWMDVLSGGEKQRM 579
Cdd:cd03265  74 RIGIVFQDL-----SVDDELT---GWENlyihARLYGVPGAERRERIDEL-----LDFVGLLEAADRLVKTYSGGMRRRL 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 4506341  580 AMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV----GITLFTVSH 625
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkeefGMTILLTTH 190
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
426-628 3.44e-09

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: 58.00  E-value: 3.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  426 LIPGAGEIIIADNIIKFDHvplatpNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT------- 498
Cdd:cd03288  13 LVGLGGEIKIHDLCVRYEN------NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVidgidis 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  499 ----KPERGKLFYVPQRPYMTLGTLRDQViypdgreDQKRKgISDLVLKEYLDNVQLGHILER-EGGWDS-VQDWMDVLS 572
Cdd:cd03288  87 klplHTLRSRLSIILQDPILFSGSIRFNL-------DPECK-CTDDRLWEALEIAQLKNMVKSlPGGLDAvVTEGGENFS 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4506341  573 GGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIyshcRKVGITLF------TVSHRKS 628
Cdd:cd03288 159 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENIL----QKVVMTAFadrtvvTIAHRVS 216
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
451-642 3.47e-09

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: 57.15  E-value: 3.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL----------GELwpLFGGR----LTKPERGK--LFYVPQRPYm 514
Cdd:cd03217  11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghpkyevteGEI--LFKGEditdLPPEERARlgIFLAFQYPP- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  515 tlgtlrdqviypdgredqkrkGISDLVLKEYLDNVQLGhilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:cd03217  88 ---------------------EIPGVKNADFLRYVNEG------------------FSGGEKKRNEILQLLLLEPDLAIL 128
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4506341  595 DECTSAVSVD----VEGYIySHCRKVGITLFTVSHRKSLWKHHE---YYLHMDGR 642
Cdd:cd03217 129 DEPDSGLDIDalrlVAEVI-NKLREEGKSVLIITHYQRLLDYIKpdrVHVLYDGR 182
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
440-628 3.90e-09

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 59.73  E-value: 3.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   440 IKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLtkpergklfYVPQRPymtLGTL 519
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI---------RLDGRP---LSSL 408
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   520 RDQVIypdgredqkRKGIS-----DLVLKE-YLDNVQLGHILEREGGWD---SVQ--DWM---------------DVLSG 573
Cdd:PRK10790 409 SHSVL---------RQGVAmvqqdPVVLADtFLANVTLGRDISEEQVWQaleTVQlaELArslpdglytplgeqgNNLSV 479
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 4506341   574 GEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV--GITLFTVSHRKS 628
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLS 536
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
451-625 3.97e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 57.75  E-value: 3.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--------------------KPERGKLFYVPQ 510
Cdd:PRK14246  21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKvdgkvlyfgkdifqidaiklRKEVGMVFQQPN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   511 rPYMTLgTLRDQVIYPDGREDQKRKGISDLVLKEYLDNVQLghilereggWDSVQDWMDV----LSGGEKQRMAMARLFY 586
Cdd:PRK14246 101 -PFPHL-SIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGL---------WKEVYDRLNSpasqLSGGQQQRLTIARALA 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 4506341   587 HKPQFAILDECTSAVSV----DVEGYIYSHCRKVGITLftVSH 625
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIvnsqAIEKLITELKNEIAIVI--VSH 210
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
458-600 4.01e-09

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: 57.30  E-value: 4.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  458 DLNFEVrSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL---------------TKPERGKLFYVPQR----PYMTLgt 518
Cdd:cd03297  16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrkkinLPPQQRKIGLVFQQyalfPHLNV-- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  519 lRDQVIYPDGREDQKRKGISdlvLKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:cd03297  93 -RENLAFGLKRKRNREDRIS---VDELLDLLGLDHLLNR---------YPAQLSGGEKQRVALARALAAQPELLLLDEPF 159

                ..
gi 4506341  599 SA 600
Cdd:cd03297 160 SA 161
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
456-625 4.43e-09

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 58.81  E-value: 4.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   456 IRDLNFEVRSGANVLICGPNGCGKSSLFRvlgelwpLFGGrLTKPERGKLF-------YVP--QR------------PYM 514
Cdd:PRK09452  30 ISNLDLTINNGEFLTLLGPSGCGKTTVLR-------LIAG-FETPDSGRIMldgqditHVPaeNRhvntvfqsyalfPHM 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   515 TLgtlRDQVIYpdGREDQKR--KGISDLVLkEYLDNVQLGHILEREggwdsVQDwmdvLSGGEKQRMAMARLFYHKPQFA 592
Cdd:PRK09452 102 TV---FENVAF--GLRMQKTpaAEITPRVM-EALRMVQLEEFAQRK-----PHQ----LSGGQQQRVAIARAVVNKPKVL 166
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4506341   593 ILDECTSAVSVDVEGYIYSHC----RKVGITLFTVSH 625
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELkalqRKLGITFVFVTH 203
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
405-606 4.58e-09

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: 59.18  E-value: 4.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    405 KYERTMVSQQEKGIEGVQV-IPLIPGAGEIII-ADNIIK-FDHvplatpngDVLIRDLNFEVRSGANVLICGPNGCGKSS 481
Cdd:TIGR03719 292 RYEELLSQEFQKRNETAEIyIPPGPRLGDKVIeAENLTKaFGD--------KLLIDDLSFKLPPGGIVGVIGPNGAGKST 363
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    482 LFRVL-GELWPlFGGRLTKPERGKLFYVpqrpymtlgtlrdqviypdgreDQKRKGISD--LVLKEY---LDNVQLG--H 553
Cdd:TIGR03719 364 LFRMItGQEQP-DSGTIEIGETVKLAYV----------------------DQSRDALDPnkTVWEEIsggLDIIKLGkrE 420
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    554 ILERE-------GGWDSvQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSavSVDVE 606
Cdd:TIGR03719 421 IPSRAyvgrfnfKGSDQ-QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTN--DLDVE 477
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
456-625 4.74e-09

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: 57.09  E-value: 4.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGEL-WPLFGGRLTK--------PERGKLFyvpQR----PYMTLgtlRDQ 522
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEgkqitepgPDRMVVF---QNysllPWLTV---REN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    523 V------IYPDGREDQKRKgisdlVLKEYLDNVQLGHILEREGGWdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:TIGR01184  75 IalavdrVLPDLSKSERRA-----IVEEHIALVGLTEAADKRPGQ---------LSGGMKQRVAIARALSIRPKVLLLDE 140
                         170       180       190
                  ....*....|....*....|....*....|...
gi 4506341    597 CTSAVSVDVEGYIYSH----CRKVGITLFTVSH 625
Cdd:TIGR01184 141 PFGALDALTRGNLQEElmqiWEEHRVTVLMVTH 173
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
456-596 4.95e-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: 57.06  E-value: 4.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGR-------LTK------PERGkLFYVPQR----PYMT--- 515
Cdd:cd03224  16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSirfdgrdITGlppherARAG-IGYVPEGrrifPELTvee 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  516 ---LGTLRDqviyPDGREDQKRKGISDL--VLKEyldnvqlghILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQ 590
Cdd:cd03224  95 nllLGAYAR----RRAKRKARLERVYELfpRLKE---------RRKQLAG---------TLSGGEQQMLAIARALMSRPK 152

                ....*.
gi 4506341  591 FAILDE 596
Cdd:cd03224 153 LLLLDE 158
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
458-600 6.11e-09

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 57.02  E-value: 6.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   458 DLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG----------------RLTKPERGKLFyvpQR----PYMT-- 515
Cdd:PRK09493  19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivdglkvndpkvdeRLIRQEAGMVF---QQfylfPHLTal 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   516 ----LGTLRdqvIYPDGREDQKRKGisdlvlKEYLDNVQLGhilEREGGWDSVqdwmdvLSGGEKQRMAMARLFYHKPQF 591
Cdd:PRK09493  96 envmFGPLR---VRGASKEEAEKQA------RELLAKVGLA---ERAHHYPSE------LSGGQQQRVAIARALAVKPKL 157

                 ....*....
gi 4506341   592 AILDECTSA 600
Cdd:PRK09493 158 MLFDEPTSA 166
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
452-625 7.72e-09

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 58.12  E-value: 7.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   452 GDVLI-RDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGRL------TKPERGKLF-----Yvpqr 511
Cdd:PRK11000  14 GDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIagleditsGDL--FIGEKRmndvppAERGVGMVFqsyalY---- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   512 PYMTLGtlrDQVIY------PDGREDQKRkgisdlvLKEYLDNVQLGHILEREGgwdsvqdwmDVLSGGEKQRMAMARLF 585
Cdd:PRK11000  88 PHLSVA---ENMSFglklagAKKEEINQR-------VNQVAEVLQLAHLLDRKP---------KALSGGQRQRVAIGRTL 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 4506341   586 YHKPQFAILDECTS----AVSVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:PRK11000 149 VAEPSVFLLDEPLSnldaALRVQMRIEISRLHKRLGRTMIYVTH 192
PLN03073 PLN03073
ABC transporter F family; Provisional
439-629 1.13e-08

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 58.33  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   439 IIKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGRLTKPE-RGKLFYVPQRPYMTL 516
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIsGELQPSSGTVFRSAKvRMAVFSQHHVDGLDL 587
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   517 GT---LRDQVIYPdGREDQKrkgisdlvLKEYLDNVQLGHILEREGgwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAI 593
Cdd:PLN03073 588 SSnplLYMMRCFP-GVPEQK--------LRAHLGSFGVTGNLALQP--------MYTLSGGQKSRVAFAKITFKKPHILL 650
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 4506341   594 LDECTSAVSVD-VEGYIYshcrkvGITLF-----TVSHRKSL 629
Cdd:PLN03073 651 LDEPSNHLDLDaVEALIQ------GLVLFqggvlMVSHDEHL 686
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
448-596 1.30e-08

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 56.23  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  448 ATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL----------GELwpLFGGR----LTKPERGK--LFYVPQR 511
Cdd:COG0396   8 VSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghpkyevtsGSI--LLDGEdileLSPDERARagIFLAFQY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  512 PY----MTLGTL--------RDQVIypDGREDQKRkgisdlvLKEYLDNVQLGH-ILER---EGgwdsvqdwmdvLSGGE 575
Cdd:COG0396  86 PVeipgVSVSNFlrtalnarRGEEL--SAREFLKL-------LKEKMKELGLDEdFLDRyvnEG-----------FSGGE 145
                       170       180
                ....*....|....*....|.
gi 4506341  576 KQRMAMARLFYHKPQFAILDE 596
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDE 166
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
456-626 1.30e-08

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: 55.75  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLF---------------YVPQR----PYMtl 516
Cdd:cd03269  16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMI--------LGIILPDSGEVLfdgkpldiaarnrigYLPEErglyPKM-- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  517 gTLRDQVIYPDGREDQKRKGISDLVLkEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDE 596
Cdd:cd03269  86 -KVIDQLVYLAQLKGLKKEEARRRID-EWLERLELSEYANKR---------VEELSKGNQQKVQFIAAVIHDPELLILDE 154
                       170       180       190
                ....*....|....*....|....*....|...
gi 4506341  597 CTSA---VSVDVEGYIYSHCRKVGITLFTVSHR 626
Cdd:cd03269 155 PFSGldpVNVELLKDVIRELARAGKTVILSTHQ 187
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
455-599 1.32e-08

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 55.74  E-value: 1.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  455 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVL---GELWPLFGGRLT---KPERGKLF-----YVPQR----PYMTL--- 516
Cdd:cd03234  22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILfngQPRKPDQFqkcvaYVRQDdillPGLTVret 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  517 ----GTLRDQVIYPDGredQKRKGISDLVLKEyLDNVQLGHILereggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFA 592
Cdd:cd03234 102 ltytAILRLPRKSSDA---IRKKRVEDVLLRD-LALTRIGGNL------------VKGISGGERRRVSIAVQLLWDPKVL 165

                ....*..
gi 4506341  593 ILDECTS 599
Cdd:cd03234 166 ILDEPTS 172
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
450-604 1.49e-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: 54.63  E-value: 1.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  450 PNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFG---------GRLTKPERGKLFYVPQRPYMTLGTL 519
Cdd:cd03247  12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLtGDLKPQQGeitldgvpvSDLEKALSSLISVLNQRPYLFDTTL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  520 RDQViypdGREdqkrkgisdlvlkeyldnvqlghilereggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFAILDECTs 599
Cdd:cd03247  92 RNNL----GRR----------------------------------------FSGGERQRLALARILLQDAPIVLLDEPT- 126

                ....*
gi 4506341  600 aVSVD 604
Cdd:cd03247 127 -VGLD 130
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
452-625 1.61e-08

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 57.03  E-value: 1.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  452 GDVL-IRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGGRL---TKPERGKLFYVPQR----PYMT 515
Cdd:COG3842  16 GDVTaLDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagfetpdsGRI--LLDGRDvtgLPPEKRNVGMVFQDyalfPHLT 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  516 LgtlRDQVIYPDGREDQKRKGISDLVlKEYLDNVQLGHILER---EggwdsvqdwmdvLSGGEKQRMAMARLFYHKPQFA 592
Cdd:COG3842  94 V---AENVAFGLRMRGVPKAEIRARV-AELLELVGLEGLADRyphQ------------LSGGQQQRVALARALAPEPRVL 157
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 4506341  593 ILDECTSA------VSVDVEgyIYSHCRKVGITLFTVSH 625
Cdd:COG3842 158 LLDEPLSAldaklrEEMREE--LRRLQRELGITFIYVTH 194
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
437-625 1.89e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 56.01  E-value: 1.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   437 DNIIKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGRLTKPERGKLFYVPQ 510
Cdd:PRK13636   3 DYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLnGILKPssgriLFDGKPIDYSRKGLMKLRE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   511 RPYMTLGTLRDQVIYPDGREDQKRkGISDLVLKEylDNVQ--LGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHK 588
Cdd:PRK13636  83 SVGMVFQDPDNQLFSASVYQDVSF-GAVNLKLPE--DEVRkrVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 4506341   589 PQFAILDECTSAVS----VDVEGYIYSHCRKVGITLFTVSH 625
Cdd:PRK13636 160 PKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATH 200
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
437-625 2.22e-08

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 55.56  E-value: 2.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   437 DNIIKFDHVPLATPnGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWP------LFGGRLTKPERGKLF---- 506
Cdd:PRK10575   9 DTTFALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPpsegeiLLDAQPLESWSSKAFarkv 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   507 -YVPQR-PYMTLGTLRDQVI---YP-------DGREDQKRkgisdlvLKEYLDNVQLGHILEReggwdsvqdWMDVLSGG 574
Cdd:PRK10575  88 aYLPQQlPAAEGMTVRELVAigrYPwhgalgrFGAADREK-------VEEAISLVGLKPLAHR---------LVDSLSGG 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4506341   575 EKQRMAMARLFYHKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALdiahQVDVLALVHRLSQERGLTVIAVLH 206
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
458-625 2.60e-08

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 55.02  E-value: 2.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   458 DLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRL----------TKPE-------RGKLFYVPQR----PYMT- 515
Cdd:PRK11124  20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdfsKTPSdkairelRRNVGMVFQQynlwPHLTv 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   516 -----------LGTLRDQVIypdgreDQKRKGISDLVLKEYLDNVQLgHilereggwdsvqdwmdvLSGGEKQRMAMARL 584
Cdd:PRK11124 100 qqnlieapcrvLGLSKDQAL------ARAEKLLERLRLKPYADRFPL-H-----------------LSGGQQQRVAIARA 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 4506341   585 FYHKPQFAILDECTSAVSVDVEGYIYSHCRKV---GITLFTVSH 625
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELaetGITQVIVTH 199
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
452-598 2.64e-08

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 56.82  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   452 GDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLfGGRLTKPERGKLFYVPQRPY------MTLGTLRDQVI 524
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLvGELEPD-SGTVKWSENANIGYYAQDHAydfendLTLFDWMSQWR 409
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4506341   525 YPdGREDQKRKGIsdlvlkeyldnvqLGHILereGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:PRK15064 410 QE-GDDEQAVRGT-------------LGRLL---FSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
433-625 2.72e-08

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 55.28  E-value: 2.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   433 IIIADNIIKfdhvplaTPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT-------------K 499
Cdd:PRK10895   3 TLTAKNLAK-------AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllplhaR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   500 PERGkLFYVPQRP--YMTLGTLRDQVIYPDGREDQKRKGISDLVlKEYLDNVQLGHILEREGgwdsvqdwmDVLSGGEKQ 577
Cdd:PRK10895  76 ARRG-IGYLPQEAsiFRRLSVYDNLMAVLQIRDDLSAEQREDRA-NELMEEFHIEHLRDSMG---------QSLSGGERR 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4506341   578 RMAMARLFYHKPQFAILDECTSAVS----VDVEGyIYSHCRKVGITLFTVSH 625
Cdd:PRK10895 145 RVEIARALAANPKFILLDEPFAGVDpisvIDIKR-IIEHLRDSGLGVLITDH 195
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
452-599 2.91e-08

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 55.30  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   452 GDV-LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFggrltkPE---RGKLFYVPQRPY-MTLGTLRD--QVI 524
Cdd:PRK14247  14 GQVeVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELY------PEarvSGEVYLDGQDIFkMDVIELRRrvQMV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   525 YpdgredQKRKGISDLVLKEyldNVQLG------------------HILEREGGWDSVQDWMDV----LSGGEKQRMAMA 582
Cdd:PRK14247  88 F------QIPNPIPNLSIFE---NVALGlklnrlvkskkelqervrWALEKAQLWDEVKDRLDApagkLSGGQQQRLCIA 158
                        170
                 ....*....|....*..
gi 4506341   583 RLFYHKPQFAILDECTS 599
Cdd:PRK14247 159 RALAFQPEVLLADEPTA 175
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
439-635 3.30e-08

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 54.50  E-value: 3.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   439 IIKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWplFGG----RLTKPE----R 502
Cdd:PRK10908   1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLIcgierpsaGKIW--FSGhditRLKNREvpflR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   503 GKLFYVPQRPYMTLG-TLRDQVIYP-----DGREDQKRKgisdlvLKEYLDNVQLghilereggWDSVQDWMDVLSGGEK 576
Cdd:PRK10908  79 RQIGMIFQDHHLLMDrTVYDNVAIPliiagASGDDIRRR------VSAALDKVGL---------LDKAKNFPIQLSGGEQ 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4506341   577 QRMAMARLFYHKPQFAILDECT----SAVSVDVEgYIYSHCRKVGITLFTVSHRKSLWKHHEY 635
Cdd:PRK10908 144 QRVGIARAVVNKPAVLLADEPTgnldDALSEGIL-RLFEEFNRVGVTVLMATHDIGLISRRSY 205
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
452-596 3.62e-08

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: 54.60  E-value: 3.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  452 GDVLI-RDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------KPE----RGkLFYVPQR----PY 513
Cdd:COG0410  14 GGIHVlHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgeditglPPHriarLG-IGYVPEGrrifPS 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  514 MT------LG--TLRDQviyPDGREDQKRkgISDL--VLKEYLDnvqlghileREGGwdsvqdwmdVLSGGEKQRMAMAR 583
Cdd:COG0410  93 LTveenllLGayARRDR---AEVRADLER--VYELfpRLKERRR---------QRAG---------TLSGGEQQMLAIGR 149
                       170
                ....*....|...
gi 4506341  584 LFYHKPQFAILDE 596
Cdd:COG0410 150 ALMSRPKLLLLDE 162
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
456-596 3.76e-08

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: 54.75  E-value: 3.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGR-LT--KPER------GKLFYVPqRPYMTLgTLR 520
Cdd:cd03219  16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsGFLRPtsgsvLFDGEdITglPPHEiarlgiGRTFQIP-RLFPEL-TVL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  521 DQVIYpdGREDQKRKGISDLVLK-----------EYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKP 589
Cdd:cd03219  94 ENVMV--AAQARTGSGLLLARARreereareraeELLERVGLADLADRPAG---------ELSYGQQRRLEIARALATDP 162

                ....*..
gi 4506341  590 QFAILDE 596
Cdd:cd03219 163 KLLLLDE 169
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
450-626 3.94e-08

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: 56.88  E-value: 3.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341     450 PNGDVLIRDLNFEVRSGANVLICGPNGCGKSS----LFRVL----GELwPLFGGRLTK----PERGKLFYVPQRPYMTLG 517
Cdd:TIGR00957 1296 EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINesaeGEI-IIDGLNIAKiglhDLRFKITIIPQDPVLFSG 1374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341     518 TLRDQVIYPDGREDQKRKGISDLV-LKEYLDNVQLGHILE-REGGwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:TIGR00957 1375 SLRMNLDPFSQYSDEEVWWALELAhLKTFVSALPDKLDHEcAEGG--------ENLSVGQRQLVCLARALLRKTKILVLD 1446
                          170       180       190
                   ....*....|....*....|....*....|...
gi 4506341     596 ECTSAVSVDVEGYIYSHCRKV--GITLFTVSHR 626
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRTQfeDCTVLTIAHR 1479
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
408-628 3.96e-08

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 56.26  E-value: 3.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   408 RTMVSQQEKGIEGVQVIPLIPGAgeiiIADNIIKFdHVPLATPngDVLiRDLNFEVRSGANVLICGPNGCGKSSLFRVL- 486
Cdd:PRK10789 291 RAMLAEAPVVKDGSEPVPEGRGE----LDVNIRQF-TYPQTDH--PAL-ENVNFTLKPGQMLGICGPTGSGKSTLLSLIq 362
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   487 -------GEL----WPLFGGRLTKpERGKLFYVPQRPYMTLGTLRDQVIYpdGREDQKRKGISDLVlkeYLDNVQlGHIL 555
Cdd:PRK10789 363 rhfdvseGDIrfhdIPLTKLQLDS-WRSRLAVVSQTPFLFSDTVANNIAL--GRPDATQQEIEHVA---RLASVH-DDIL 435
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4506341   556 EREGGWDS-VQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGI--TLFTVSHRKS 628
Cdd:PRK10789 436 RLPQGYDTeVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEgrTVIISAHRLS 511
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
450-604 5.99e-08

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 55.71  E-value: 5.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    450 PNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWPLFGGrltkpergKLFYVPQRPYM--TLgTL 519
Cdd:TIGR03719  15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkdfnGEARPQPGI--------KVGYLPQEPQLdpTK-TV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    520 RDQVIypDGREDQKRkgisdlVLKEYlDNV-------------------QLGHILEREGGWD---SVQDWMD-------- 569
Cdd:TIGR03719  86 RENVE--EGVAEIKD------ALDRF-NEIsakyaepdadfdklaaeqaELQEIIDAADAWDldsQLEIAMDalrcppwd 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 4506341    570 ----VLSGGEKQRMAMARLFYHKPQFAILDECTS---AVSVD 604
Cdd:TIGR03719 157 advtKLSGGERRRVALCRLLLSKPDMLLLDEPTNhldAESVA 198
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
452-596 6.23e-08

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 54.73  E-value: 6.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  452 GDVL-IRDLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWP------LFGGRLTKPERGKLFYVPQ----RPYMTLGtl 519
Cdd:COG4152  12 GDKTaVDDVSFTVPKGEIFGLLGPNGAGKTTTIRiILGILAPdsgevlWDGEPLDPEDRRRIGYLPEerglYPKMKVG-- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  520 rDQVIY------PDGREDQKRkgisdlvLKEYLDNVQLGhilEREGgwDSVQDwmdvLSGGEKQRMAMARLFYHKPQFAI 593
Cdd:COG4152  90 -EQLVYlarlkgLSKAEAKRR-------ADEWLERLGLG---DRAN--KKVEE----LSKGNQQKVQLIAALLHDPELLI 152

                ...
gi 4506341  594 LDE 596
Cdd:COG4152 153 LDE 155
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
449-603 6.32e-08

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


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 54.67  E-value: 6.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  449 TPNGDV-LIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-----------GELwpLFGGR----LTKPE----RGK-LFY 507
Cdd:COG0444  13 TRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlgllpppgitsGEI--LFDGEdllkLSEKElrkiRGReIQM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  508 VPQRPYMTLG---TLRDQVIYP------DGREDQKRKGIsdlvlkEYLDNVQLghilereggwDSVQDWMDV----LSGG 574
Cdd:COG0444  91 IFQDPMTSLNpvmTVGDQIAEPlrihggLSKAEARERAI------ELLERVGL----------PDPERRLDRypheLSGG 154
                       170       180       190
                ....*....|....*....|....*....|....*
gi 4506341  575 EKQR----MAMArlfyHKPQFAILDECTSA--VSV 603
Cdd:COG0444 155 MRQRvmiaRALA----LEPKLLIADEPTTAldVTI 185
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
440-633 7.77e-08

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


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 53.18  E-value: 7.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  440 IKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFG-----GRLTKPERGKlfyvpQRPY 513
Cdd:cd03292   1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIyKEELPTSGtirvnGQDVSDLRGR-----AIPY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  514 M--TLGT-LRD-----------------QVIYPDGREDQKRkgisdlvLKEYLDNVQLGHilereggwdSVQDWMDVLSG 573
Cdd:cd03292  76 LrrKIGVvFQDfrllpdrnvyenvafalEVTGVPPREIRKR-------VPAALELVGLSH---------KHRALPAELSG 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4506341  574 GEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV---GITLFTVSHRKSLWKHH 633
Cdd:cd03292 140 GEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInkaGTTVVVATHAKELVDTT 202
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
455-625 9.42e-08

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 53.89  E-value: 9.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   455 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGrlTKPErGKLFYVPQRPY---MTLGTLRDQV-------- 523
Cdd:PRK14258  22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESE--VRVE-GRVEFFNQNIYerrVNLNRLRRQVsmvhpkpn 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   524 IYPDGREDQKRKGISdlvLKEYLDNVQLGHILEREGG----WDSVQDWMDV----LSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:PRK14258  99 LFPMSVYDNVAYGVK---IVGWRPKLEIDDIVESALKdadlWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMD 175
                        170       180       190
                 ....*....|....*....|....*....|....
gi 4506341   596 E-CTS---AVSVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:PRK14258 176 EpCFGldpIASMKVESLIQSLRLRSELTMVIVSH 209
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
452-606 1.16e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 54.96  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   452 GDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRV-LGELWPLfGGRL---TKPE-------RGKLfyVPQRpymtlgTLR 520
Cdd:PRK11147 331 GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQAD-SGRIhcgTKLEvayfdqhRAEL--DPEK------TVM 401
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   521 DQViyPDGREDQKRKGISDLVLKeYLdnvqlghilereggwdsvQDWM----------DVLSGGEKQRMAMARLFYHKPQ 590
Cdd:PRK11147 402 DNL--AEGKQEVMVNGRPRHVLG-YL------------------QDFLfhpkramtpvKALSGGERNRLLLARLFLKPSN 460
                        170
                 ....*....|....*.
gi 4506341   591 FAILDECTSavSVDVE 606
Cdd:PRK11147 461 LLILDEPTN--DLDVE 474
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
473-601 1.18e-07

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 53.24  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   473 GPNGCGKSSLFRVL---GELWP--------------LFGGRLTKPE-RGKLFYVPQRPYMTLGTLRDQVIYpdgreDQKR 534
Cdd:PRK14239  38 GPSGSGKSTLLRSInrmNDLNPevtitgsivynghnIYSPRTDTVDlRKEIGMVFQQPNPFPMSIYENVVY-----GLRL 112
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506341   535 KGISDlvlKEYLDNVqLGHILEREGGWDSVQDWMD----VLSGGEKQRMAMARLFYHKPQFAILDECTSAV 601
Cdd:PRK14239 113 KGIKD---KQVLDEA-VEKSLKGASIWDEVKDRLHdsalGLSGGQQQRVCIARVLATSPKIILLDEPTSAL 179
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
458-583 1.33e-07

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 53.95  E-value: 1.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  458 DLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---------------KPERGKLFYVPQ--R--PYMT-LG 517
Cdd:COG4148  17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsargiflPPHRRRIGYVFQeaRlfPHLSvRG 96
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4506341  518 TLRdqviYPDGREDQKRKGISdlvLKEYLDNVQLGHILEReggwdsvqdWMDVLSGGEKQRMAMAR 583
Cdd:COG4148  97 NLL----YGRKRAPRAERRIS---FDEVVELLGIGHLLDR---------RPATLSGGERQRVAIGR 146
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
434-605 1.69e-07

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 53.93  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   434 IIADNIIK-FDHVPLATpngdvlirDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELwpLFGG----RLTKP 500
Cdd:PRK10851   3 IEIANIKKsFGRTQVLN--------DISLDIPSGQMVALLGPSGSGKTTLLRIIaglehqtsGHI--RFHGtdvsRLHAR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   501 ER--GKLF--YVPQRpYMTLGtlrDQVIY-----PDgREDQKRKGISDLVLKeYLDNVQLGHILEReggwdsvqdWMDVL 571
Cdd:PRK10851  73 DRkvGFVFqhYALFR-HMTVF---DNIAFgltvlPR-RERPNAAAIKAKVTQ-LLEMVQLAHLADR---------YPAQL 137
                        170       180       190
                 ....*....|....*....|....*....|....
gi 4506341   572 SGGEKQRMAMARLFYHKPQFAILDECTSAVSVDV 605
Cdd:PRK10851 138 SGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
405-584 1.99e-07

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 53.97  E-value: 1.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   405 KYERtMVSQQEKGIEGVQ--VIPLIPGAGEIII-ADNIIK-FdhvplatpnGD-VLIRDLNFEVRSGANVLICGPNGCGK 479
Cdd:PRK11819 294 RYEE-LLSEEYQKRNETNeiFIPPGPRLGDKVIeAENLSKsF---------GDrLLIDDLSFSLPPGGIVGIIGPNGAGK 363
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   480 SSLFRVLGELWPLFGGRLTKPERGKLFYVpqrpymtlgtlrdqviypdgreDQKRKGISD-----LVLKEYLDNVQLGhi 554
Cdd:PRK11819 364 STLFKMITGQEQPDSGTIKIGETVKLAYV----------------------DQSRDALDPnktvwEEISGGLDIIKVG-- 419
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 4506341   555 lERE------------GGWDSvQDWMDVLSGGEKQRMAMARL 584
Cdd:PRK11819 420 -NREipsrayvgrfnfKGGDQ-QKKVGVLSGGERNRLHLAKT 459
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
434-596 2.29e-07

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: 52.16  E-value: 2.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  434 IIADNIIKFdhvplatPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTK-P--ER 502
Cdd:cd03218   1 LRAENLSKR-------YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIvglvkpdsGKIL-LDGQDITKlPmhKR 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  503 GKL--FYVPQRPYMTLG-TLRDQV-----IYPDGREDQKRKgisdlvLKEYLDNVQLGHILEREGgwdsvqdwmDVLSGG 574
Cdd:cd03218  73 ARLgiGYLPQEASIFRKlTVEENIlavleIRGLSKKEREEK------LEELLEEFHITHLRKSKA---------SSLSGG 137
                       170       180
                ....*....|....*....|..
gi 4506341  575 EKQRMAMARLFYHKPQFAILDE 596
Cdd:cd03218 138 ERRRVEIARALATNPKFLLLDE 159
PLN03232 PLN03232
ABC transporter C family member; Provisional
381-626 2.36e-07

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 54.21  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    381 MTRLAGFTARITELMQ-VLKDLNhgKYERTMVSqqekgIEGVQVIPLIPGAGEIIIADN----------IIKFDHVPLA- 448
Cdd:PLN03232 1172 MGLLLSYTLNITTLLSgVLRQAS--KAENSLNS-----VERVGNYIDLPSEATAIIENNrpvsgwpsrgSIKFEDVHLRy 1244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    449 TPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPE-----------RGKLFYVPQRPYMTLG 517
Cdd:PLN03232 1245 RPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltdlRRVLSIIPQSPVLFSG 1324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    518 TLRDQV-IYPDGREDQKRKGISDLVLKEYLDNVQLGHILE-REGGwdsvqdwmDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:PLN03232 1325 TVRFNIdPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEvSEGG--------ENFSVGQRQLLSLARALLRRSKILVLD 1396
                         250       260       270
                  ....*....|....*....|....*....|...
gi 4506341    596 ECTSAVSVDVEGYIYSHCRK--VGITLFTVSHR 626
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIREefKSCTMLVIAHR 1429
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
444-609 2.74e-07

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 52.80  E-value: 2.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   444 HVPLATPNGDVL-IRDLNFEVRSGANVLICGPNGCGKS-SLFRVLGELWP--------LFGGR--LTKPER--GKL---- 505
Cdd:PRK09473  19 RVTFSTPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngriggsaTFNGReiLNLPEKelNKLraeq 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   506 ----FYVPQ---RPYMTLGTLRDQVIypdgredQKRKGISDLVLKE----YLDNVQLGHILEReggwdsvqdwMDV---- 570
Cdd:PRK09473  99 ismiFQDPMtslNPYMRVGEQLMEVL-------MLHKGMSKAEAFEesvrMLDAVKMPEARKR----------MKMyphe 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 4506341   571 LSGGEKQR--MAMARLFyhKPQFAILDECTSAVSVDVEGYI 609
Cdd:PRK09473 162 FSGGMRQRvmIAMALLC--RPKLLIADEPTTALDVTVQAQI 200
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
463-599 4.73e-07

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 51.60  E-value: 4.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  463 VRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGRLTKPE--------RG-------------------KLFYVPQRPYM 514
Cdd:cd03236  23 PREGQVLGLVGPNGIGKSTALKILaGKLKPNLGKFDDPPDwdeildefRGselqnyftkllegdvkvivKPQYVDLIPKA 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  515 TLGTLRDQVIYPDGREdqkrkgisdlVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:cd03236 103 VKGKVGELLKKKDERG----------KLDELVDQLELRHVLDRN---------IDQLSGGELQRVAIAAALARDADFYFF 163

                ....*
gi 4506341  595 DECTS 599
Cdd:cd03236 164 DEPSS 168
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
440-625 7.47e-07

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 51.04  E-value: 7.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   440 IKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---KPERGKL-----FYVPQR 511
Cdd:PRK15056   7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgQPTRQALqknlvAYVPQS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   512 P------------------YMTLGTLRdqviYPDGREDQkrkgisdlVLKEYLDNVQLGHILEREGGwdsvqdwmdVLSG 573
Cdd:PRK15056  87 EevdwsfpvlvedvvmmgrYGHMGWLR----RAKKRDRQ--------IVTAALARVDMVEFRHRQIG---------ELSG 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4506341   574 GEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV---GITLFTVSH 625
Cdd:PRK15056 146 GQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrdeGKTMLVSTH 200
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
450-599 9.62e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 50.85  E-value: 9.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   450 PNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGRLTKPE------------RGKLFYVPQRPymtl 516
Cdd:PRK13639  12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFnGILKPTSGEVLIKGEpikydkksllevRKTVGIVFQNP---- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   517 gtlRDQVIYPDGREDQKRkGISDLVLKEylDNVQ--LGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:PRK13639  88 ---DDQLFAPTVEEDVAF-GPLNLGLSK--EEVEkrVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161

                 ....*
gi 4506341   595 DECTS 599
Cdd:PRK13639 162 DEPTS 166
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
387-611 1.20e-06

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 51.56  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   387 FTARITeLMQVLKDLNH--GKYERTMVS----------QQEKGIegvqviplipGAGEIIIADNIIKFDHVPLATPNGDV 454
Cdd:PRK11176 288 FSSMIA-LMRPLKSLTNvnAQFQRGMAAcqtlfaildlEQEKDE----------GKRVIERAKGDIEFRNVTFTYPGKEV 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   455 L-IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTkpergkLFYVPQRPYmTLGTLRDQV--------IY 525
Cdd:PRK11176 357 PaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIL------LDGHDLRDY-TLASLRNQValvsqnvhLF 429
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   526 PD--------GREDQ-KRKGISDLVLKEYldnvQLGHILEREGGWDSVQDWMDV-LSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:PRK11176 430 NDtianniayARTEQySREQIEEAARMAY----AMDFINKMDNGLDTVIGENGVlLSGGQRQRIAIARALLRDSPILILD 505
                        250
                 ....*....|....*.
gi 4506341   596 ECTSAVSVDVEGYIYS 611
Cdd:PRK11176 506 EATSALDTESERAIQA 521
ycf16 CHL00131
sulfate ABC transporter protein; Validated
448-604 1.22e-06

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 50.41  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   448 ATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL----------GELwpLFGGR----LTKPERGKL--FYVPQR 511
Cdd:CHL00131  15 ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpaykileGDI--LFKGEsildLEPEERAHLgiFLAFQY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   512 PYMTLGT-----LRdqVIYPDGREDQKRKGISDL----VLKEYLDNVQLG-HILER---EGgwdsvqdwmdvLSGGEKQR 578
Cdd:CHL00131  93 PIEIPGVsnadfLR--LAYNSKRKFQGLPELDPLefleIINEKLKLVGMDpSFLSRnvnEG-----------FSGGEKKR 159
                        170       180
                 ....*....|....*....|....*....
gi 4506341   579 ---MAMARLfyhKPQFAILDECTSAVSVD 604
Cdd:CHL00131 160 neiLQMALL---DSELAILDETDSGLDID 185
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
463-599 1.45e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 51.35  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   463 VRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGRLTKPE--------RG-------------------KLFYVPQRPYM 514
Cdd:PRK13409  96 PKEGKVTGILGPNGIGKTTAVKILsGELIPNLGDYEEEPSwdevlkrfRGtelqnyfkklyngeikvvhKPQYVDLIPKV 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   515 TLGTLRDQVIYPDGREdqkrkgisdlVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:PRK13409 176 FKGKVRELLKKVDERG----------KLDEVVERLGLENILDRD---------ISELSGGELQRVAIAAALLRDADFYFF 236

                 ....*
gi 4506341   595 DECTS 599
Cdd:PRK13409 237 DEPTS 241
cbiO PRK13650
energy-coupling factor transporter ATPase;
456-625 1.48e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 50.12  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWP-------LFGGRLTKPE----RGKLFYVPQRP--YMTLGTLRDQ 522
Cdd:PRK13650  23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEaesgqiiIDGDLLTEENvwdiRHKIGMVFQNPdnQFVGATVEDD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   523 VIYpdGREDqkrKGISdlvLKEYLDNVQlgHILEREGgwdsVQDWMDV----LSGGEKQRMAMARLFYHKPQFAILDECT 598
Cdd:PRK13650 103 VAF--GLEN---KGIP---HEEMKERVN--EALELVG----MQDFKEReparLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
                        170       180       190
                 ....*....|....*....|....*....|...
gi 4506341   599 SAvsVDVEG------YIYSHCRKVGITLFTVSH 625
Cdd:PRK13650 169 SM--LDPEGrlelikTIKGIRDDYQMTVISITH 199
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
456-615 1.68e-06

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 48.97  E-value: 1.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT---KPERGK---------LFYVPqrpymtlgtlrdqv 523
Cdd:cd03215  16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITldgKPVTRRsprdairagIAYVP-------------- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  524 iypdgrEDQKRKGisdLVLKEYL-DNVQLGHILereggwdsvqdwmdvlSGGEKQRMAMARLFYHKPQFAILDECTsaVS 602
Cdd:cd03215  82 ------EDRKREG---LVLDLSVaENIALSSLL----------------SGGNQQKVVLARWLARDPRVLILDEPT--RG 134
                       170
                ....*....|....*
gi 4506341  603 VDVEG--YIYSHCRK 615
Cdd:cd03215 135 VDVGAkaEIYRLIRE 149
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
455-599 2.08e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 49.46  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   455 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPL------------FGGRLTKP---------ERGKLFYVPQR-P 512
Cdd:PRK14267  19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearvegevrlFGRNIYSPdvdpievrrEVGMVFQYPNPfP 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   513 YMTlgtlrdqvIYPDGREDQKRKGIsdLVLKEYLDNVqLGHILEREGGWDSVQDWMD----VLSGGEKQRMAMARLFYHK 588
Cdd:PRK14267  99 HLT--------IYDNVAIGVKLNGL--VKSKKELDER-VEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMK 167
                        170
                 ....*....|.
gi 4506341   589 PQFAILDECTS 599
Cdd:PRK14267 168 PKILLMDEPTA 178
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
456-625 2.09e-06

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 51.01  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--------------KPERGKLFYVPQRPYMTLG---T 518
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqridtlspgklQALRRDIQFIFQDPYASLDprqT 419
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   519 LRDQVIYP-------DGREDQKRkgisdlvLKEYLDNVQLghilEREGGWDSVQDWmdvlSGGEKQRMAMARLFYHKPQF 591
Cdd:PRK10261 420 VGDSIMEPlrvhgllPGKAAAAR-------VAWLLERVGL----LPEHAWRYPHEF----SGGQRQRICIARALALNPKV 484
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 4506341   592 AILDECTSAVSVDVEGYIYSHC----RKVGITLFTVSH 625
Cdd:PRK10261 485 IIADEAVSALDVSIRGQIINLLldlqRDFGIAYLFISH 522
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
454-603 3.65e-06

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


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 48.52  E-value: 3.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  454 VLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT--------KPE--RGKLFYVP--QRPYMTLgTLRD 521
Cdd:cd03266  19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATvdgfdvvkEPAeaRRRLGFVSdsTGLYDRL-TARE 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  522 QVIYPDGREDQKRKGISDLVlKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTSAV 601
Cdd:cd03266  98 NLEYFAGLYGLKGDELTARL-EELADRLGMEELLDRRVG---------GFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167

                ..
gi 4506341  602 SV 603
Cdd:cd03266 168 DV 169
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
439-625 5.12e-06

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: 48.35  E-value: 5.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  439 IIKFDHVP---LATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWpLFGGRLTKPERGKLfy 507
Cdd:cd03258   1 MIELKNVSkvfGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInglerptsGSVL-VDGTDLTLLSGKEL-- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  508 VPQRPYMTL----------GTLRDQVIYP-----DGREDQKRKgisdlvLKEYLDNVQLGhilereggwDSVQDWMDVLS 572
Cdd:cd03258  78 RKARRRIGMifqhfnllssRTVFENVALPleiagVPKAEIEER------VLELLELVGLE---------DKADAYPAQLS 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4506341  573 GGEKQRMAMARLFYHKPQFAILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03258 143 GGQKQRVGIARALANNPKVLLCDEATSALdpetTQSILALLRDINRELGLTIVLITH 199
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
455-599 9.47e-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: 9.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  455 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplfGGRLTKPERGKLFYVPQRPyMTLGTLRDQVIYPDgREDQKr 534
Cdd:cd03213  24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNAL-------AGRRTGLGVSGEVLINGRP-LDKRSFRKIIGYVP-QDDIL- 93
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4506341  535 kgISDLVLKEYLDNVQLghilereggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:cd03213  94 --HPTLTVRETLMFAAK----------------LRGLSGGERKRVSIALELVSNPSLLFLDEPTS 140
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
418-599 1.00e-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: 49.14  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341     418 IEGVQVIPLIPGAGEIIIADNIIKFdhvplaTPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFG--- 494
Cdd:TIGR01271 1203 IENPHAQKCWPSGGQMDVQGLTAKY------TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGeiq 1276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341     495 ------GRLTKPERGKLF-YVPQRPYMTLGTLRDQVIYPDGREDQKRKGISDLV-LKEYLDNV--QLGHILErEGGWdsv 564
Cdd:TIGR01271 1277 idgvswNSVTLQTWRKAFgVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVgLKSVIEQFpdKLDFVLV-DGGY--- 1352
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 4506341     565 qdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTS 599
Cdd:TIGR01271 1353 -----VLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
456-498 1.07e-05

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: 47.14  E-value: 1.07e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 4506341  456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT 498
Cdd:cd03220  38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
cbiO PRK13642
energy-coupling factor transporter ATPase;
459-625 1.36e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 47.40  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   459 LNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGG-------RLTKPE----RGKLFYVPQRP--YMTLGTLRDQVIY 525
Cdd:PRK13642  26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvkidgeLLTAENvwnlRRKIGMVFQNPdnQFVGATVEDDVAF 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   526 pdGREDQkrkGISDLVLKEYLDNVQLG-HILE---REGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTSAV 601
Cdd:PRK13642 106 --GMENQ---GIPREEMIKRVDEALLAvNMLDfktREPA---------RLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
                        170       180
                 ....*....|....*....|....*...
gi 4506341   602 S----VDVEGYIYSHCRKVGITLFTVSH 625
Cdd:PRK13642 172 DptgrQEIMRVIHEIKEKYQLTVLSITH 199
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
466-604 1.59e-05

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 47.81  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   466 GANVLICGPNGCGKSSLFRVL--------GELWPLFGGRLtkperGklfYVPQRPYMTLG-TLRDQVIypDGREDQKRKg 536
Cdd:PRK11819  33 GAKIGVLGLNGAGKSTLLRIMagvdkefeGEARPAPGIKV-----G---YLPQEPQLDPEkTVRENVE--EGVAEVKAA- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   537 isdlvLKEYlDNV-------------------QLGHILEREGGWDS---VQDWMD------------VLSGGEKQRMAMA 582
Cdd:PRK11819 102 -----LDRF-NEIyaayaepdadfdalaaeqgELQEIIDAADAWDLdsqLEIAMDalrcppwdakvtKLSGGERRRVALC 175
                        170       180
                 ....*....|....*....|....*
gi 4506341   583 RLFYHKPQFAILDECTS---AVSVD 604
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNhldAESVA 200
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
457-625 1.75e-05

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 46.90  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   457 RDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLF--------YVPQRPYMTLGTLRDQVIYPdg 528
Cdd:PRK10253  24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTL--------SRLMTPAHGHVWldgehiqhYASKEVARRIGLLAQNATTP-- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   529 redqkrkgiSDLVLKEYLDNVQLGH----ILEREGGWDSVQDWM-------------DVLSGGEKQRMAMARLFYHKPQF 591
Cdd:PRK10253  94 ---------GDITVQELVARGRYPHqplfTRWRKEDEEAVTKAMqatgithladqsvDTLSGGQRQRAWIAMVLAQETAI 164
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 4506341   592 AILDECTSAV----SVDVEGYIYSHCRKVGITLFTVSH 625
Cdd:PRK10253 165 MLLDEPTTWLdishQIDLLELLSELNREKGYTLAAVLH 202
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
473-601 1.94e-05

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 46.70  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   473 GPNGCGKSSLFRV---LGELWPLF---------GGRLTKPE------RGKLFYVPQRPYMTLGTLRDQVIYpdGREDQKR 534
Cdd:PRK14243  43 GPSGCGKSTILRCfnrLNDLIPGFrvegkvtfhGKNLYAPDvdpvevRRRIGMVFQKPNPFPKSIYDNIAY--GARINGY 120
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506341   535 KGISDLVLKEYLDNVQLghilereggWDSVQDWMD----VLSGGEKQRMAMARLFYHKPQFAILDECTSAV 601
Cdd:PRK14243 121 KGDMDELVERSLRQAAL---------WDEVKDKLKqsglSLSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
455-637 1.97e-05

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 46.10  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   455 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWplfggrltKPERGKLFYVPQ----------------------RP 512
Cdd:PRK13540  16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLL--------NPEKGEILFERQsikkdlctyqkqlcfvghrsgiNP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   513 YMTLgtlRDQVIYpDGREDQKRKGISDLVLKeyldnVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFA 592
Cdd:PRK13540  88 YLTL---RENCLY-DIHFSPGAVGITELCRL-----FSLEHLIDYPCG---------LLSSGQKRQVALLRLWMSKAKLW 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4506341   593 ILDEctSAVSVD------VEGYIYSHCRKVGITLFTVSHRKSLWK--HHEYYL 637
Cdd:PRK13540 150 LLDE--PLVALDelslltIITKIQEHRAKGGAVLLTSHQDLPLNKadYEEYHL 200
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
456-610 2.13e-05

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 47.69  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRpymtlgTLRDQVIYPDgrEDQKRK 535
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD------GLANGIVYIS--EDRKRD 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   536 GisdLVL----KE--------YLDN--VQLGHILEREggwdSVQDWMDV--------------LSGGEKQRMAMARLFYH 587
Cdd:PRK10762 340 G---LVLgmsvKEnmsltalrYFSRagGSLKHADEQQ----AVSDFIRLfniktpsmeqaiglLSGGNQQKVAIARGLMT 412
                        170       180
                 ....*....|....*....|...
gi 4506341   588 KPQFAILDECTSAVSVDVEGYIY 610
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIY 435
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
437-625 2.18e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 46.67  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   437 DNIIKFDHVPLATpNGD--VLIRDLNFEVRSGANVLICGPNGCGKSSLFRvlgelwpLFGGrLTKPERGKLFYvpqrpym 514
Cdd:PRK13648   5 NSIIVFKNVSFQY-QSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAK-------LMIG-IEKVKSGEIFY------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   515 tlgtlRDQVIYPDGREDQkRKGISdLVLK-----------EY-----LDNVQLGH---------ILEREGGWDSVQDWMD 569
Cdd:PRK13648  69 -----NNQAITDDNFEKL-RKHIG-IVFQnpdnqfvgsivKYdvafgLENHAVPYdemhrrvseALKQVDMLERADYEPN 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   570 VLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV----GITLFTVSH 625
Cdd:PRK13648 142 ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITH 201
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
462-606 2.29e-05

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 46.25  E-value: 2.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  462 EVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGRLTkpERGKLFYVPQrpYMTL---GTLRDQViypdgREDQKRKGI 537
Cdd:cd03237  21 SISESEVIGILGPNGIGKTTFIKMLaGVLKPDEGDIEI--ELDTVSYKPQ--YIKAdyeGTVRDLL-----SSITKDFYT 91
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4506341  538 SDLVLKEYLDNVQLGHILEREggwdsVQDwmdvLSGGEKQRMAMARLFYHKPQFAILDEcTSAvSVDVE 606
Cdd:cd03237  92 HPYFKTEIAKPLQIEQILDRE-----VPE----LSGGELQRVAIAACLSKDADIYLLDE-PSA-YLDVE 149
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
454-609 2.33e-05

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 47.39  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   454 VLIRDLNFEVRSGANVLICGPNGCGKSS----LFRVL---GELW----PL--FGGRLTKPERGKLFYVPQRPYMTLGT-L 519
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInsqGEIWfdgqPLhnLNRRQLLPVRHRIQVVFQDPNSSLNPrL 379
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   520 RDQVIYPDG------------REDQKRKgisdlVLKEY-LDNvqlghilereggwDSVQDWMDVLSGGEKQRMAMARLFY 586
Cdd:PRK15134 380 NVLQIIEEGlrvhqptlsaaqREQQVIA-----VMEEVgLDP-------------ETRHRYPAEFSGGQRQRIAIARALI 441
                        170       180
                 ....*....|....*....|...
gi 4506341   587 HKPQFAILDECTSAVSVDVEGYI 609
Cdd:PRK15134 442 LKPSLIILDEPTSSLDKTVQAQI 464
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
457-504 3.26e-05

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 45.84  E-value: 3.26e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 4506341  457 RDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGK 504
Cdd:COG1134  43 KDVSFEVERGESVGIIGRNGAGKSTLLKLI--------AGILEPTSGR 82
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
435-606 3.64e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 46.73  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   435 IADNIIKFD-HVPLATPNGDVLIR--DL-----NF-------EVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGGRLT 498
Cdd:PRK13409 319 IRPEPIEFEeRPPRDESERETLVEypDLtkklgDFsleveggEIYEGEVIGIVGPNGIGKTTFAKLLaGVLKPDEGEVDP 398
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   499 KPergKLFYVPQrpYMTlgtlRDQviypDGREDQKRKGISDLVLKEYLDN-----VQLGHILEREggwdsvqdwMDVLSG 573
Cdd:PRK13409 399 EL---KISYKPQ--YIK----PDY----DGTVEDLLRSITDDLGSSYYKSeiikpLQLERLLDKN---------VKDLSG 456
                        170       180       190
                 ....*....|....*....|....*....|...
gi 4506341   574 GEKQRMAMARLFYHKPQFAILDEcTSAvSVDVE 606
Cdd:PRK13409 457 GELQRVAIAACLSRDADLYLLDE-PSA-HLDVE 487
PLN03130 PLN03130
ABC transporter C family member; Provisional
440-626 4.47e-05

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 47.04  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    440 IKFDHVPLA-TPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVlgelwpLFggRLTKPERGK-------------- 504
Cdd:PLN03130 1238 IKFEDVVLRyRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNA------LF--RIVELERGRilidgcdiskfglm 1309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    505 -----LFYVPQRPYMTLGTLRDQViypDGREDQkrkgiSDLVLKEYLDNVQLGHILEREG-GWDS-VQDWMDVLSGGEKQ 577
Cdd:PLN03130 1310 dlrkvLGIIPQAPVLFSGTVRFNL---DPFNEH-----NDADLWESLERAHLKDVIRRNSlGLDAeVSEAGENFSVGQRQ 1381
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 4506341    578 RMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRK--VGITLFTVSHR 626
Cdd:PLN03130 1382 LLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREefKSCTMLIIAHR 1432
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
571-626 7.43e-05

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 46.18  E-value: 7.43e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    571 LSGGEKQRMAMARLFYHKPQFAILDECTSAVSVD----VEGYIYSHCRKVGITLFTVSHR 626
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAHR 1418
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
431-596 7.95e-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: 44.85  E-value: 7.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  431 GEIIIADNIIKFdhvplaTPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFG---------GRLTKPE 501
Cdd:cd03289   1 GQMTVKDLTAKY------TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGdiqidgvswNSVPLQK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  502 RGKLF-YVPQRPYMTLGTLRdQVIYPDGR-EDQKRKGISDLV-LKEYLDNV--QLGHILErEGGWdsvqdwmdVLSGGEK 576
Cdd:cd03289  75 WRKAFgVIPQKVFIFSGTFR-KNLDPYGKwSDEEIWKVAEEVgLKSVIEQFpgQLDFVLV-DGGC--------VLSHGHK 144
                       170       180
                ....*....|....*....|
gi 4506341  577 QRMAMARLFYHKPQFAILDE 596
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDE 164
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
455-599 8.04e-05

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 44.62  E-value: 8.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   455 LIRDLNFEVRSGANVLICGPNGCGKSSLFRVLgelwplfgGRLTKPERGKLFY-------------------VPQRPYMT 515
Cdd:PRK11231  17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCF--------ARLLTPQSGTVFLgdkpismlssrqlarrlalLPQHHLTP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   516 LG-TLRDQVIYpdGR------------EDQKRkgisdlvLKEYLDNVQLGHILEReggwdSVQDwmdvLSGGEKQRMAMA 582
Cdd:PRK11231  89 EGiTVRELVAY--GRspwlslwgrlsaEDNAR-------VNQAMEQTRINHLADR-----RLTD----LSGGQRQRAFLA 150
                        170
                 ....*....|....*..
gi 4506341   583 RLFYHKPQFAILDECTS 599
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTT 167
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
456-596 9.14e-05

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: 44.64  E-value: 9.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGR-LT--KPER----G--------KLFyvpqrPYM 514
Cdd:COG0411  20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLItGFYRPtsgriLFDGRdITglPPHRiarlGiartfqnpRLF-----PEL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  515 T------------LGTLRDQVIYPDGREDQKRKGISDLVLkEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMA 582
Cdd:COG0411  95 TvlenvlvaaharLGRGLLAALLRLPRARREEREARERAE-ELLERVGLADRADEPAG---------NLSYGQQRRLEIA 164
                       170
                ....*....|....
gi 4506341  583 RLFYHKPQFAILDE 596
Cdd:COG0411 165 RALATEPKLLLLDE 178
cbiO PRK13643
energy-coupling factor transporter ATPase;
439-625 9.46e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 44.72  E-value: 9.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   439 IIKFDHVPLA-TPNGDVLIR---DLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWPLFGG--------------RLTK 499
Cdd:PRK13643   1 MIKFEKVNYTyQPNSPFASRalfDIDLEVKKGSYTALIGHTGSGKSTLLQHLnGLLQPTEGKvtvgdivvsstskqKEIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   500 PER---GKLFYVPQRPYMTLGTLRDQVIYPDGREDQKRKgiSDLVLKEYLDNVQLGHILEREGGWDsvqdwmdvLSGGEK 576
Cdd:PRK13643  81 PVRkkvGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEK--AEKIAAEKLEMVGLADEFWEKSPFE--------LSGGQM 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4506341   577 QRMAMARLFYHKPQFAILDECTSAVSVDVE---GYIYSHCRKVGITLFTVSH 625
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARiemMQLFESIHQSGQTVVLVTH 202
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
464-599 1.15e-04

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 45.16  E-value: 1.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  464 RSGANVLICGPNGCGKSSLFRVL-GELWPLFGGRLTKPE--------RG-------------------KLFYVPQRPYMT 515
Cdd:COG1245  97 KKGKVTGILGPNGIGKSTALKILsGELKPNLGDYDEEPSwdevlkrfRGtelqdyfkklangeikvahKPQYVDLIPKVF 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  516 LGTLRDQVIYPDGREdqkrkgisdlVLKEYLDNVQLGHILEREggwdsvqdwMDVLSGGEKQRMAMARLFYHKPQFAILD 595
Cdd:COG1245 177 KGTVRELLEKVDERG----------KLDELAEKLGLENILDRD---------ISELSGGELQRVAIAAALLRDADFYFFD 237

                ....
gi 4506341  596 ECTS 599
Cdd:COG1245 238 EPSS 241
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
458-603 1.19e-04

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 45.06  E-value: 1.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  458 DLNFEVRSGANVLICGPNGCGKSSLFRVL-------GELWplFGGR----LT----KPERGKLFYVPQRPY------MTL 516
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALlrlipseGEIR--FDGQdldgLSrralRPLRRRMQVVFQDPFgslsprMTV 381
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  517 GtlrdQVI-------YPDGREDQKRKGISDLvlkeyLDNVQL-GHILER---EggwdsvqdwmdvLSGGEKQRMAMARLF 585
Cdd:COG4172 382 G----QIIaeglrvhGPGLSAAERRARVAEA-----LEEVGLdPAARHRyphE------------FSGGQRQRIAIARAL 440
                       170       180
                ....*....|....*....|
gi 4506341  586 YHKPQFAILDECTSA--VSV 603
Cdd:COG4172 441 ILEPKLLVLDEPTSAldVSV 460
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
450-596 1.51e-04

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 44.45  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   450 PNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVL--------GELWplFGGRLT---KP-ERGkLFYVPQR----PY 513
Cdd:PRK11650  14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVagleritsGEIW--IGGRVVnelEPaDRD-IAMVFQNyalyPH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   514 MTL-----------GTLRDQViypdgredQKRkgisdlvLKEYLDNVQLGHILER---EggwdsvqdwmdvLSGGEKQRM 579
Cdd:PRK11650  91 MSVrenmayglkirGMPKAEI--------EER-------VAEAARILELEPLLDRkprE------------LSGGQRQRV 143
                        170
                 ....*....|....*..
gi 4506341   580 AMARLFYHKPQFAILDE 596
Cdd:PRK11650 144 AMGRAIVREPAVFLFDE 160
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
453-601 1.71e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 45.02  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    453 DVLI-RDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLT------------KPERGKLFYVPQRPYMTLGTL 519
Cdd:PTZ00265  397 DVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIindshnlkdinlKWWRSKIGVVSQDPLLFSNSI 476
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341    520 RDQVIYP-------------------------DGREDQKRKGISDLvlKEYLDNVQLGHILEREGGWDSVQDW--MDV-- 570
Cdd:PTZ00265  477 KNNIKYSlyslkdlealsnyynedgndsqenkNKRNSCRAKCAGDL--NDMSNTTDSNELIEMRKNYQTIKDSevVDVsk 554
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 4506341    571 -------------------------LSGGEKQRMAMARLFYHKPQFAILDECTSAV 601
Cdd:PTZ00265  555 kvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSL 610
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
451-628 1.90e-04

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 43.59  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   451 NGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTK------------------------------- 499
Cdd:PRK11264  14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqqkglirqlrqhvgfvfqn 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   500 ----PERGKLFYVPQRPYMTLGTLRDQVIyPDGREDQKRKGISdlvlkeyldnvqlghilereGGWDSvqdWMDVLSGGE 575
Cdd:PRK11264  94 fnlfPHRTVLENIIEGPVIVKGEPKEEAT-ARARELLAKVGLA--------------------GKETS---YPRRLSGGQ 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 4506341   576 KQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVG---ITLFTVSHRKS 628
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAqekRTMVIVTHEMS 205
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
571-638 4.26e-04

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 42.65  E-value: 4.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4506341   571 LSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKV---GITLFTVSHRKSLWKH---HEYYLH 638
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHvssHVIFLH 226
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
458-625 4.33e-04

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


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 42.10  E-value: 4.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  458 DLNFEVRSGANVLICGPNGCGKSSLFR-VLGELWPLFGGRL--------TKPERGKLFYVPQR----PYMTLGTLRDQVI 524
Cdd:cd03298  16 HFDLTFAQGEITAIVGPSGSGKSTLLNlIAGFETPQSGRVLingvdvtaAPPADRPVSMLFQEnnlfAHLTVEQNVGLGL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  525 YPDGR---EDQKRkgisdlvLKEYLDNVQLGHILEREGGwdsvqdwmdVLSGGEKQRMAMARLFYHKPQFAILDECTSAV 601
Cdd:cd03298  96 SPGLKltaEDRQA-------IEVALARVGLAGLEKRLPG---------ELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
                       170       180
                ....*....|....*....|....*...
gi 4506341  602 S----VDVEGYIYSHCRKVGITLFTVSH 625
Cdd:cd03298 160 DpalrAEMLDLVLDLHAETKMTVLMVTH 187
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
459-625 5.13e-04

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 42.23  E-value: 5.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   459 LNFEVRSGANVLICGPNGCGKSSLFRVLGELWP-----LFGGR----LTKPE----RGKL-------FYVPQRPYMTLGT 518
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPgsgsiQFAGQpleaWSAAElarhRAYLsqqqtppFAMPVFQYLTLHQ 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   519 lrdqviyPDG-REDQKRKGISDLVlkeylDNVQLGHILEReggwdSVQDwmdvLSGGEKQRMAMARLFYH-----KP--Q 590
Cdd:PRK03695  95 -------PDKtRTEAVASALNEVA-----EALGLDDKLGR-----SVNQ----LSGGEWQRVRLAAVVLQvwpdiNPagQ 153
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 4506341   591 FAILDECTSAVSVDVEGYIYSHCRKV---GITLFTVSH 625
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSELcqqGIAVVMSSH 191
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
459-642 5.56e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 42.39  E-value: 5.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   459 LNFEVRSGANVLicGPNGCGKSSLFRVLGELWP-----------LFGGRLTKPER---------GKLFyvpQRPYMTLGT 518
Cdd:PRK14271  42 MGFPARAVTSLM--GPTGSGKTTFLRTLNRMNDkvsgyrysgdvLLGGRSIFNYRdvlefrrrvGMLF---QRPNPFPMS 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   519 LRDQVIYpdGREDQKrkgisdLVLKEYLDNVQLGHILErEGGWDSVQDWMD----VLSGGEKQRMAMARLFYHKPQFAIL 594
Cdd:PRK14271 117 IMDNVLA--GVRAHK------LVPRKEFRGVAQARLTE-VGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLL 187
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4506341   595 DECTSAV----SVDVEGYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGR 642
Cdd:PRK14271 188 DEPTSALdpttTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGR 239
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
546-629 1.23e-03

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 40.92  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   546 LDNVQLGHILEREGGWDSVQDWMDVL----------------SGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYI 609
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLeqlglgkrldhlpaqlSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
                         90       100
                 ....*....|....*....|....
gi 4506341   610 ----YSHCRKVGITLFTVSHRKSL 629
Cdd:PRK10584 186 adllFSLNREHGTTLILVTHDLQL 209
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
456-602 1.37e-03

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: 40.57  E-value: 1.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVL-GELWP-----LFGGRLTKPERGKLF----YVPQ-RPYMTLGTLRDQV- 523
Cdd:cd03263  18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLtGELRPtsgtaYINGYSIRTDRKAARqslgYCPQfDALFDELTVREHLr 97
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4506341  524 IYpdGREDQKRKGISDLVLKEYLDNVQLGHILEREggwdsVQDwmdvLSGGEKQRMAMARLFYHKPQFAILDECTSAVS 602
Cdd:cd03263  98 FY--ARLKGLPKSEIKEEVELLLRVLGLTDKANKR-----ART----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
471-615 1.95e-03

ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213242 [Multi-domain]  Cd Length: 247  Bit Score: 40.25  E-value: 1.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  471 ICGPNGCGKSSL-----FrVLGE---------LWPL-FGGRLTKPergklfyVPQRPYMTLgtlrdQVIYPDGREDQKRK 535
Cdd:cd03275  27 IIGPNGSGKSNLmdaisF-VLGEksshlrsknLKDLiYRARVGKP-------DSNSAYVTA-----VYEDDDGEEKTFRR 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341  536 GISDLV-----------LKEYLDNVQLGHILER-------EGGWDSV----------QDwMDVLSGGEKQRMAMARLF-- 585
Cdd:cd03275  94 IITGGSssyringkvvsLKEYNEELEKINILVKarnflvfQGDVESIasknppgkrfRD-MDNLSGGEKTMAALALLFai 172
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4506341  586 --YHKPQFAILDECTSA---VSVD-VEGYIYSHCRK 615
Cdd:cd03275 173 hsYQPAPFFVLDEVDAAldnTNVGkVASYIREQAGP 208
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
456-601 2.12e-03

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 40.79  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   456 IRDLNFEVRSGANVLICGPNGCGKSSLFRVLGelwplfggRLTKPERGKLFYvpqrPYMTLGTLRDQVIypdgrEDQKRK 535
Cdd:PRK10070  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLN--------RLIEPTRGQVLI----DGVDIAKISDAEL-----REVRRK 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506341   536 GISdLVLKEY--------LDNVQLGHIL-------EREGGWDSVQD---------WMDVLSGGEKQRMAMARLFYHKPQF 591
Cdd:PRK10070 107 KIA-MVFQSFalmphmtvLDNTAFGMELaginaeeRREKALDALRQvglenyahsYPDELSGGMRQRVGLARALAINPDI 185
                        170
                 ....*....|
gi 4506341   592 AILDECTSAV 601
Cdd:PRK10070 186 LLMDEAFSAL 195
AAA_23 pfam13476
AAA domain;
456-483 5.19e-03

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 38.63  E-value: 5.19e-03
                          10        20
                  ....*....|....*....|....*...
gi 4506341    456 IRDLNFEVRSGANvLICGPNGCGKSSLF 483
Cdd:pfam13476   9 FRDQTIDFSKGLT-LITGPNGSGKTTIL 35
 
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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