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Conserved domains on  [gi|7262393|ref|NP_000024|]
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ATP-binding cassette sub-family D member 1 [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, ...
1-681 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: 1037.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393      1 MPVLSRPRPWRGNTLKRTAVLLALAAYGAHKVYPLVRQCLAPARGLQAPAGEPTQEASGV----AAAKAGMNRVFLQRLL 76
Cdd:TIGR00954   1 MAVLSKYRLLRSTSNNKTDKQDSPAAVGMNKVIELKRERAADRRGDKSGKEELTIVGKHStiegAKKKAHVNGVFLGKLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393     77 WLLRLLFPRVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFGWQLLQWLLIALPATFVNSAIRYLEG 156
Cdd:TIGR00954  81 FLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    157 QLALSFRSRLVAHAYRLYFSQQTYYRVSNMDGRLRNPDQSLTEDVVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSR 236
Cdd:TIGR00954 161 ELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTALGSV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    237 GAGTAWPSaiaglvVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQRSYQDLASQ 316
Cdd:TIGR00954 241 GPAGLFAY------LFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEH 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    317 INLILLERLWYVMLEQFLMKYVWSASGLLMVAVPIITATgysesdaeavKKAALEKKEEELVSErteaFTIARNLLTAAA 396
Cdd:TIGR00954 315 LNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKT----------HPAFLEMSEEELMQE----FYNNGRLLLKAA 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    397 DAIERIMSSYKEVTELAGYTARVHEMFQVFEDVQRCHFKRPRELEDAQAGSGtiGRSGVRVEGplkiRGQVVDVEQGIIC 476
Cdd:TIGR00954 381 DALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIESGREG--GRNSNLVPG----RGIVEYQDNGIKF 454
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    477 ENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSLRDQ 556
Cdd:TIGR00954 455 ENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQ 534
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    557 VIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVS 636
Cdd:TIGR00954 535 IIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 7262393    637 IDVEGKIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGGWKF 681
Cdd:TIGR00954 615 VDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
 
Name Accession Description Interval E-value
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
1-681 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: 1037.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393      1 MPVLSRPRPWRGNTLKRTAVLLALAAYGAHKVYPLVRQCLAPARGLQAPAGEPTQEASGV----AAAKAGMNRVFLQRLL 76
Cdd:TIGR00954   1 MAVLSKYRLLRSTSNNKTDKQDSPAAVGMNKVIELKRERAADRRGDKSGKEELTIVGKHStiegAKKKAHVNGVFLGKLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393     77 WLLRLLFPRVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFGWQLLQWLLIALPATFVNSAIRYLEG 156
Cdd:TIGR00954  81 FLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    157 QLALSFRSRLVAHAYRLYFSQQTYYRVSNMDGRLRNPDQSLTEDVVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSR 236
Cdd:TIGR00954 161 ELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTALGSV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    237 GAGTAWPSaiaglvVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQRSYQDLASQ 316
Cdd:TIGR00954 241 GPAGLFAY------LFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEH 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    317 INLILLERLWYVMLEQFLMKYVWSASGLLMVAVPIITATgysesdaeavKKAALEKKEEELVSErteaFTIARNLLTAAA 396
Cdd:TIGR00954 315 LNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKT----------HPAFLEMSEEELMQE----FYNNGRLLLKAA 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    397 DAIERIMSSYKEVTELAGYTARVHEMFQVFEDVQRCHFKRPRELEDAQAGSGtiGRSGVRVEGplkiRGQVVDVEQGIIC 476
Cdd:TIGR00954 381 DALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIESGREG--GRNSNLVPG----RGIVEYQDNGIKF 454
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    477 ENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSLRDQ 556
Cdd:TIGR00954 455 ENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQ 534
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    557 VIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVS 636
Cdd:TIGR00954 535 IIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 7262393    637 IDVEGKIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGGWKF 681
Cdd:TIGR00954 615 VDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
ABC_membrane_2 pfam06472
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ...
83-352 3.08e-121

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: 363.85  E-value: 3.08e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393     83 FPRVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFGWQLLQWLLIALPATFVNSAIRYLEGQLALSF 162
Cdd:pfam06472   6 FPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQRLALRF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    163 RSRLVAHAYRLYFSQQTYYRVSNMDGRLRNPDQSLTEDVVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSRGAgtaw 242
Cdd:pfam06472  86 RTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRGP---- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    243 psAIAGLVVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQRSYQDLASQINLILL 322
Cdd:pfam06472 162 --AILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILR 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 7262393    323 ERLWYVMLEQFLMKYVWSASGLLMVAVPII 352
Cdd:pfam06472 240 RRLWYGFIEDFVLKYTWSILGYVLVALPIF 269
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
122-688 2.54e-86

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 283.62  E-value: 2.54e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  122 IVRKDPRAFGWQLLQWLLIALPATFVNSAIRYLEGQLALSFRSRLVAHAYRLYFSQQTYYRVSNMDGRLRNPDQSLTEDV 201
Cdd:COG4178  55 LQARDAAAFWQQLGVFALLAAISILLAVYQTYLRQRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDI 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  202 VAFAASVAHLYSNLtkplLDVAVT--SYT-----LLRAARSRGAGTAWpsAIAGLVVF------LTANVLrAFspKFG-- 266
Cdd:COG4178 135 RLFTETTLSLSLGL----LSSVVTliSFIgilwsLSGSLTFTLGGYSI--TIPGYMVWaaliyaIIGTLL-TH--LIGrp 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  267 --ELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQRSYQDLASQINLILLerlWYVMLEQFLmkyvwSASGL 344
Cdd:COG4178 206 liRLNFEQQRREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVIANWRRLIR---RQRNLTFFT-----TGYGQ 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  345 LMVAVPI-ITATGYsesdaeavkkaalekkeeelvserteaftIARNL----LTAAADAIERIMSS-------YKEVTEL 412
Cdd:COG4178 278 LAVIFPIlVAAPRY-----------------------------FAGEItlggLMQAASAFGQVQGAlswfvdnYQSLAEW 328
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  413 AGYTARVHEMFQVFEDVQRchfkrpreledAQAGSGTIGRSGvrvegplkirgqvvdvEQGIICENIPIVTPSGEVVVAS 492
Cdd:COG4178 329 RATVDRLAGFEEALEAADA-----------LPEAASRIETSE----------------DGALALEDLTLRTPDGRPLLED 381
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSLRDQVIYPDSVEDmqrkgYS 572
Cdd:COG4178 382 LSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGTLREALLYPATAEA-----FS 456
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  573 EQDLEAILDVVHLHHILQR--EGGweamcDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDA 650
Cdd:COG4178 457 DAELREALEAVGLGHLAERldEEA-----DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE 531
                       570       580       590       600
                ....*....|....*....|....*....|....*....|
gi 7262393  651 --GIALLSITHRPSLWKYHTHLLQFDGEGGWKFEKLDSAA 688
Cdd:COG4178 532 lpGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPAEAPA 571
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
474-679 2.78e-83

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: 261.32  E-value: 2.78e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSL 553
Cdd:cd03223   1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  554 RDQVIYPdsvedmqrkgyseqdleaildvvhlhhilqreggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:cd03223  81 REQLIYP----------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 7262393  634 AVSIDVEGKIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGGW 679
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
486-659 4.21e-18

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 84.00  E-value: 4.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK-------PPP---QRMFYIPQRPYMSVGSLR 554
Cdd:PRK10247  19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPTSGTLLFEgedistlKPEiyrQQVSYCAQTPTLFGDTVY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   555 DQVIYPdsvEDMQRKGYSEQDLEAILDVVHL-HHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:PRK10247  99 DNLIFP---WQIRNQQPDPAIFLDDLERFALpDTILTKN---------IAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
                        170       180       190
                 ....*....|....*....|....*....|
gi 7262393   634 AVS----IDVEGKIFQAAKDAGIALLSITH 659
Cdd:PRK10247 167 ALDesnkHNVNEIIHRYVREQNIAVLWVTH 196
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
486-671 7.01e-10

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 59.17  E-value: 7.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRpymsvGSLRDQviYPDSVED 565
Cdd:NF040873   4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQR-----SEVPDS--LPLTVRD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   566 M------QRKG----YSEQD---LEAILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:NF040873  77 LvamgrwARRGlwrrLTRDDraaVDDALERVGLADLAGRQ---------LGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 7262393   633 SAVSIDVEGKIFQ---AAKDAGIALLSITHRPSLWKYHTHLL 671
Cdd:NF040873 148 TGLDAESRERIIAllaEEHARGATVVVVTHDLELVRRADPCV 189
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
502-663 7.58e-05

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 43.52  E-value: 7.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393     502 HLLITGPNGCGKSSLFRILGGlwptyggvLYKPPPQRMFYIpqrpymsvgslrdqviypdsvedmqrkgyseqDLEAILD 581
Cdd:smart00382   4 VILIVGPPGSGKTTLARALAR--------ELGPPGGGVIYI--------------------------------DGEDILE 43
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393     582 VVHLHHILQREGGWEAMcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDAGIALLSITHRP 661
Cdd:smart00382  44 EVLDQLLLIIVGGKKAS------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNL 117

                   ..
gi 7262393     662 SL 663
Cdd:smart00382 118 TV 119
 
Name Accession Description Interval E-value
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
1-681 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: 1037.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393      1 MPVLSRPRPWRGNTLKRTAVLLALAAYGAHKVYPLVRQCLAPARGLQAPAGEPTQEASGV----AAAKAGMNRVFLQRLL 76
Cdd:TIGR00954   1 MAVLSKYRLLRSTSNNKTDKQDSPAAVGMNKVIELKRERAADRRGDKSGKEELTIVGKHStiegAKKKAHVNGVFLGKLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393     77 WLLRLLFPRVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFGWQLLQWLLIALPATFVNSAIRYLEG 156
Cdd:TIGR00954  81 FLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    157 QLALSFRSRLVAHAYRLYFSQQTYYRVSNMDGRLRNPDQSLTEDVVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSR 236
Cdd:TIGR00954 161 ELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTALGSV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    237 GAGTAWPSaiaglvVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQRSYQDLASQ 316
Cdd:TIGR00954 241 GPAGLFAY------LFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEH 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    317 INLILLERLWYVMLEQFLMKYVWSASGLLMVAVPIITATgysesdaeavKKAALEKKEEELVSErteaFTIARNLLTAAA 396
Cdd:TIGR00954 315 LNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKT----------HPAFLEMSEEELMQE----FYNNGRLLLKAA 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    397 DAIERIMSSYKEVTELAGYTARVHEMFQVFEDVQRCHFKRPRELEDAQAGSGtiGRSGVRVEGplkiRGQVVDVEQGIIC 476
Cdd:TIGR00954 381 DALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIESGREG--GRNSNLVPG----RGIVEYQDNGIKF 454
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    477 ENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSLRDQ 556
Cdd:TIGR00954 455 ENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQ 534
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    557 VIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVS 636
Cdd:TIGR00954 535 IIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 7262393    637 IDVEGKIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGGWKF 681
Cdd:TIGR00954 615 VDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
ABC_membrane_2 pfam06472
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ...
83-352 3.08e-121

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: 363.85  E-value: 3.08e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393     83 FPRVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFGWQLLQWLLIALPATFVNSAIRYLEGQLALSF 162
Cdd:pfam06472   6 FPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQRLALRF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    163 RSRLVAHAYRLYFSQQTYYRVSNMDGRLRNPDQSLTEDVVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSRGAgtaw 242
Cdd:pfam06472  86 RTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRGP---- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    243 psAIAGLVVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQRSYQDLASQINLILL 322
Cdd:pfam06472 162 --AILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILR 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 7262393    323 ERLWYVMLEQFLMKYVWSASGLLMVAVPII 352
Cdd:pfam06472 240 RRLWYGFIEDFVLKYTWSILGYVLVALPIF 269
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
122-688 2.54e-86

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 283.62  E-value: 2.54e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  122 IVRKDPRAFGWQLLQWLLIALPATFVNSAIRYLEGQLALSFRSRLVAHAYRLYFSQQTYYRVSNMDGRLRNPDQSLTEDV 201
Cdd:COG4178  55 LQARDAAAFWQQLGVFALLAAISILLAVYQTYLRQRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDI 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  202 VAFAASVAHLYSNLtkplLDVAVT--SYT-----LLRAARSRGAGTAWpsAIAGLVVF------LTANVLrAFspKFG-- 266
Cdd:COG4178 135 RLFTETTLSLSLGL----LSSVVTliSFIgilwsLSGSLTFTLGGYSI--TIPGYMVWaaliyaIIGTLL-TH--LIGrp 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  267 --ELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQRSYQDLASQINLILLerlWYVMLEQFLmkyvwSASGL 344
Cdd:COG4178 206 liRLNFEQQRREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVIANWRRLIR---RQRNLTFFT-----TGYGQ 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  345 LMVAVPI-ITATGYsesdaeavkkaalekkeeelvserteaftIARNL----LTAAADAIERIMSS-------YKEVTEL 412
Cdd:COG4178 278 LAVIFPIlVAAPRY-----------------------------FAGEItlggLMQAASAFGQVQGAlswfvdnYQSLAEW 328
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  413 AGYTARVHEMFQVFEDVQRchfkrpreledAQAGSGTIGRSGvrvegplkirgqvvdvEQGIICENIPIVTPSGEVVVAS 492
Cdd:COG4178 329 RATVDRLAGFEEALEAADA-----------LPEAASRIETSE----------------DGALALEDLTLRTPDGRPLLED 381
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSLRDQVIYPDSVEDmqrkgYS 572
Cdd:COG4178 382 LSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGTLREALLYPATAEA-----FS 456
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  573 EQDLEAILDVVHLHHILQR--EGGweamcDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDA 650
Cdd:COG4178 457 DAELREALEAVGLGHLAERldEEA-----DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE 531
                       570       580       590       600
                ....*....|....*....|....*....|....*....|
gi 7262393  651 --GIALLSITHRPSLWKYHTHLLQFDGEGGWKFEKLDSAA 688
Cdd:COG4178 532 lpGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPAEAPA 571
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
474-679 2.78e-83

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: 261.32  E-value: 2.78e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSL 553
Cdd:cd03223   1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  554 RDQVIYPdsvedmqrkgyseqdleaildvvhlhhilqreggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:cd03223  81 REQLIYP----------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 7262393  634 AVSIDVEGKIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGGW 679
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
482-659 3.10e-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: 3.10e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  482 VTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLYK-------PPP---QRMFYIPQRPYMSV 550
Cdd:COG4619   8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGeIYLDgkplsamPPPewrRQVAYVPQEPALWG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  551 GSLRDQVIYPDSvedMQRKGYSEQDLEAILDVVHL-HHILQreggweamcdwKDV--LSGGEKQRIGMARMFYHRPKYAL 627
Cdd:COG4619  88 GTVRDNLPFPFQ---LRERKFDRERALELLERLGLpPDILD-----------KPVerLSGGERQRLALIRALLLQPDVLL 153
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 7262393  628 LDECTSAVSID----VEGKIFQAAKDAGIALLSITH 659
Cdd:COG4619 154 LDEPTSALDPEntrrVEELLREYLAEEGRAVLWVSH 189
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
474-663 9.22e-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: 106.00  E-value: 9.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVL---------YKPPP--QRMFYI 542
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdLDPASwrRQIAWV 416
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  543 PQRPYMSVGSLRDQViypdsveDMQRKGYSEQDLEAILDVVHLHHILQR-EGGWEAMcdwkdV------LSGGEKQRIGM 615
Cdd:COG4988 417 PQNPYLFAGTIRENL-------RLGRPDASDEELEAALEAAGLDEFVAAlPDGLDTP-----LgeggrgLSGGQAQRLAL 484
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 7262393  616 ARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHRPSL 663
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlaKGRTVILITHRLAL 534
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
484-663 2.85e-23

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: 97.07  E-value: 2.85e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY-------KPPP----QRMFYIPQRPYmsvgs 552
Cdd:cd03228  12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlrDLDLeslrKNIAYVPQDPF----- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  553 lrdqvIYPDSVEDmqrkgyseqdleaildvvhlhhilqreggweamcdwkDVLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:cd03228  87 -----LFSGTIRE-------------------------------------NILSGGQRQRIAIARALLRDPPILILDEAT 124
                       170       180       190
                ....*....|....*....|....*....|...
gi 7262393  633 SAVSIDVEGKIFQA--AKDAGIALLSITHRPSL 663
Cdd:cd03228 125 SALDPETEALILEAlrALAKGKTVIVIAHRLST 157
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
484-663 6.08e-22

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: 101.06  E-value: 6.08e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGvlykpppqRMFY--IPQRpYMSVGSLRDQV---- 557
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG--------RILIdgIDLR-QIDPASLRRQIgvvl 555
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  558 ----IYPDSVED---MQRKGYSEQDLEAILDVVHLHH-ILQREGGWEAMcdwkdV------LSGGEKQRIGMARMFYHRP 623
Cdd:COG2274 556 qdvfLFSGTIREnitLGDPDATDEEIIEAARLAGLHDfIEALPMGYDTV-----VgeggsnLSGGQRQRLAIARALLRNP 630
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 7262393  624 KYALLDECTSAVSIDVEGKIFQA--AKDAGIALLSITHRPSL 663
Cdd:COG2274 631 RILILDEATSALDAETEAIILENlrRLLKGRTVIIIAHRLST 672
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
92-662 2.13e-21

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 98.70  E-value: 2.13e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   92 GLLALHSAALVSRTFLSVYVARLDGRLARCIVR-KDPRAFGWQLLQWLLIALPATFVNSAIRYLEGQLALSF----RSRL 166
Cdd:COG1132  21 GLLILALLLLLLSALLELLLPLLLGRIIDALLAgGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVvadlRRDL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  167 VAHAYRL---YFSQQTYYRVSNMdgrlrnpdqsLTEDVVAFAASVAHLYSNLTKPLLDVAVTSYTLLRaarsrgagTAWP 243
Cdd:COG1132 101 FEHLLRLplsFFDRRRTGDLLSR----------LTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFV--------IDWR 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  244 SAIAGLVVF-LTANVLRAFSPKFGELVAEEARRKGELrymhSRVVANS----EEIAFYGGHEVELALLQRSYQDLASQin 318
Cdd:COG1132 163 LALIVLLVLpLLLLVLRLFGRRLRKLFRRVQEALAEL----NGRLQESlsgiRVVKAFGREERELERFREANEELRRA-- 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  319 lilleRLWYVMLEQFLMKYVWSASGLLMVAVPIITATGYSESDAEAvkkaalekkeEELVserteAFTiarNLLTAAADA 398
Cdd:COG1132 237 -----NLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTV----------GDLV-----AFI---LYLLRLFGP 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  399 IERIMSSYKEVTELAGYTARVHEMFQVFEDVQrchfkrprelEDAQAGSGTIGRSGVRVEGplkirgqvvdveqgiicen 478
Cdd:COG1132 294 LRQLANVLNQLQRALASAERIFELLDEPPEIP----------DPPGAVPLPPVRGEIEFEN------------------- 344
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  479 ipiVT---PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP------TYGGV---------LYKpppqRMF 540
Cdd:COG1132 345 ---VSfsyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDptsgriLIDGVdirdltlesLRR----QIG 417
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  541 YIPQRPYMSVGSLRDQVIYPdsvedmqRKGYSEQDLEAILDVVHLHHILQR-EGGWEAMcdwkdV------LSGGEKQRI 613
Cdd:COG1132 418 VVPQDTFLFSGTIRENIRYG-------RPDATDEEVEEAAKAAQAHEFIEAlPDGYDTV-----VgergvnLSGGQRQRI 485
                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|.
gi 7262393  614 GMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHRPS 662
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERlmKGRTTIVIAHRLS 536
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
474-663 5.68e-21

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 90.74  E-value: 5.68e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  474 IICENIPIVTPSGE-VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLykpppqrmfyIPQRPYMSVG 551
Cdd:cd03246   1 LEVENVSFRYPGAEpPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLrPTSGRVR----------LDGADISQWD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  552 S--LRDQViypdsvedmqrkGYSEQDLE----AILDvvhlhhilqreggweamcdwkDVLSGGEKQRIGMARMFYHRPKY 625
Cdd:cd03246  71 PneLGDHV------------GYLPQDDElfsgSIAE---------------------NILSGGQRQRLGLARALYGNPRI 117
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 7262393  626 ALLDECTSAVSIDVEGKIFQA---AKDAGIALLSITHRPSL 663
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPET 158
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
489-663 2.45e-20

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: 90.34  E-value: 2.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY------KPPP----QRMFYIPQRPYMSVGSLRDQV 557
Cdd:cd03245  19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkPTSGSVLLdgtdirQLDPadlrRNIGYVPQDVTLFYGTLRDNI 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  558 IYpdsvedmqrkGYSEQDLEAILDVVHLHHILQ-------------REGGweamcdwkDVLSGGEKQRIGMARMFYHRPK 624
Cdd:cd03245  99 TL----------GAPLADDERILRAAELAGVTDfvnkhpngldlqiGERG--------RGLSGGQRQAVALARALLNDPP 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 7262393  625 YALLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHRPSL 663
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQllGDKTLIIITHRPSL 201
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
485-671 8.01e-20

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: 88.30  E-value: 8.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  485 SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYkppPQRMFYIPQRPYMSVGSLRDQVIYpDSV 563
Cdd:cd03250  16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKLSGSVSV---PGSIAYVSQEPWIQNGTIRENILF-GKP 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  564 EDMQRkgyseqdLEAILDVVHLHHILQR-EGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEG 641
Cdd:cd03250  92 FDEER-------YEKVIKACALEPDLEIlPDGDLTEIGEKGInLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGR 164
                       170       180       190
                ....*....|....*....|....*....|....*
gi 7262393  642 KIFQ-----AAKDAGIALLsITHRPSLWKYHTHLL 671
Cdd:cd03250 165 HIFEncilgLLLNNKTRIL-VTHQLQLLPHADQIV 198
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
493-663 9.32e-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: 86.53  E-value: 9.32e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMFYIPQrpymsvgsLRDQVIYpdsvedmqrkgy 571
Cdd:cd00267  18 VSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLkPTSGEILIDGKDIAKLPLEE--------LRRRIGY------------ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  572 seqdleaildvvhlhhILQreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDA- 650
Cdd:cd00267  78 ----------------VPQ--------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELa 127
                       170
                ....*....|....*
gi 7262393  651 --GIALLSITHRPSL 663
Cdd:cd00267 128 eeGRTVIIVTHDPEL 142
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
493-633 1.94e-19

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: 85.39  E-value: 1.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    493 LNIRVEEGMHLLITGPNGCGKSSLFRIL-GGLWPTYGGVLY----------KPPPQRMFYIPQ----RPYMSVgslRDQV 557
Cdd:pfam00005   4 VSLTLNPGEILALVGPNGAGKSTLLKLIaGLLSPTEGTILLdgqdltdderKSLRKEIGYVFQdpqlFPRLTV---RENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7262393    558 IYPDSVEDMQRKGYSEQDLEAI--LDVVHLHHILQREGGweamcdwkDVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALekLGLGDLADRPVGERP--------GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
493-667 3.42e-19

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: 86.75  E-value: 3.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP----------QRMFYIPQRPymsvgslRDQVIYPd 561
Cdd:cd03225  20 ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLgPTSGEVLVDGKDltklslkelrRKVGLVFQNP-------DDQFFGP- 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  562 SVED-----MQRKGYSEQDLEAI----LDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:cd03225  92 TVEEevafgLENLGLPEEEIEERveeaLELVGLEGLRDRS---------PFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 7262393  633 SavSIDVEG-----KIFQAAKDAGIALLSITHRPSLWKYH 667
Cdd:cd03225 163 A--GLDPAGrrellELLKKLKAEGKTIIIVTHDLDLLLEL 200
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
485-676 3.02e-18

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: 84.12  E-value: 3.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  485 SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKPPPQRMF-----YIPQRPYMSvgslRDqvi 558
Cdd:cd03235  10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLKPTSGSIRVFGKPLEKErkrigYVPQRRSID----RD--- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  559 YPDSVED---MQR-------KGYSEQDLEAI---LDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKY 625
Cdd:cd03235  83 FPISVRDvvlMGLyghkglfRRLSKADKAKVdeaLERVGLSELADRQIG---------ELSGGQQQRVLLARALVQDPDL 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7262393  626 ALLDECTSAVsiDVEGK-----IFQAAKDAGIALLSITH-RPSLWKYHTHLLQFDGE 676
Cdd:cd03235 154 LLLDEPFAGV--DPKTQediyeLLRELRREGMTILVVTHdLGLVLEYFDRVLLLNRT 208
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
477-663 3.48e-18

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


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 88.56  E-value: 3.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    477 ENIPIVTPSGE-VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVL------YKPPPQRMF-----YIPQ 544
Cdd:TIGR01842 320 ENVTIVPPGGKkPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVrldgadLKQWDRETFgkhigYLPQ 399
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    545 RPYMSVGSLRDqviypdSVEDMQRKGYSEQDLEA-ILDVVHlHHILQREGGWE-AMCDWKDVLSGGEKQRIGMARMFYHR 622
Cdd:TIGR01842 400 DVELFPGTVAE------NIARFGENADPEKIIEAaKLAGVH-ELILRLPDGYDtVIGPGGATLSGGQRQRIALARALYGD 472
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 7262393    623 PKYALLDECTSavSIDVEGKI-----FQAAKDAGIALLSITHRPSL 663
Cdd:TIGR01842 473 PKLVVLDEPNS--NLDEEGEQalanaIKALKARGITVVVITHRPSL 516
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
474-666 3.81e-18

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: 83.69  E-value: 3.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  474 IICENIPIVTPSGEVVVASL---NIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGV------LYKPPP------- 536
Cdd:cd03255   1 IELKNLSKTYGGGGEKVQALkgvSLSIEKGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVrvdgtdISKLSEkelaafr 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  537 -QRMFYIPQR----PYMSVgslRDQVIYPDSVEDMQRKGYsEQDLEAILDVVHLHHILQReggweaMCDWkdvLSGGEKQ 611
Cdd:cd03255  81 rRHIGFVFQSfnllPDLTA---LENVELPLLLAGVPKKER-RERAEELLERVGLGDRLNH------YPSE---LSGGQQQ 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7262393  612 RIGMARMFYHRPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALLSITHRPSLWKY 666
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLdsetGKEVMELLRELNKEAGTTIVVVTHDPELAEY 206
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
486-659 4.21e-18

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 84.00  E-value: 4.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK-------PPP---QRMFYIPQRPYMSVGSLR 554
Cdd:PRK10247  19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPTSGTLLFEgedistlKPEiyrQQVSYCAQTPTLFGDTVY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   555 DQVIYPdsvEDMQRKGYSEQDLEAILDVVHL-HHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:PRK10247  99 DNLIFP---WQIRNQQPDPAIFLDDLERFALpDTILTKN---------IAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
                        170       180       190
                 ....*....|....*....|....*....|
gi 7262393   634 AVS----IDVEGKIFQAAKDAGIALLSITH 659
Cdd:PRK10247 167 ALDesnkHNVNEIIHRYVREQNIAVLWVTH 196
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
486-661 2.74e-17

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: 80.99  E-value: 2.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLYK---------PPPQRMFYIPQRPymsvgslrd 555
Cdd:COG4133  14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGeVLWNgepirdareDYRRRLAYLGHAD--------- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  556 qVIYPD-SVED-------MQRKGYSEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:COG4133  85 -GLKPElTVREnlrfwaaLYGLRADREAIDEALEAVGLAGLADLPVR---------QLSAGQKRRVALARLLLSPAPLWL 154
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 7262393  628 LDECTSAvsIDVEGK-----IFQAAKDAGIALLSITHRP 661
Cdd:COG4133 155 LDEPFTA--LDAAGVallaeLIAAHLARGGAVLLTTHQP 191
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
484-662 3.68e-17

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: 85.59  E-value: 3.68e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP------TYGGVLYKPPP-----QRMFYIPQRPYMSVGS 552
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDpqsgsiTLGGVDLRDLDeddlrRRIAVVPQRPHLFDTT 424
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  553 LRD--QVIYPDSvedmqrkgySEQDLEAILDVVHLHHILQR-EGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALL 628
Cdd:COG4987 425 LREnlRLARPDA---------TDEELWAALERVGLGDWLAAlPDGLDTWLGEGGRrLSGGERRRLALARALLRDAPILLL 495
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 7262393  629 DECTSAVSIDVEGKI----FQAAKDAgiALLSITHRPS 662
Cdd:COG4987 496 DEPTEGLDAATEQALladlLEALAGR--TVLLITHRLA 531
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
477-659 5.95e-17

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: 79.99  E-value: 5.95e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  477 ENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY--KPPPQRMFYipQRPYMSVGSL 553
Cdd:cd03226   3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLngKPIKAKERR--KSIGYVMQDV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  554 RDQvIYPDSVED-----MQRKGYSEQDLEAILDVVHLHhilqreggweamcDWKDV----LSGGEKQRIGMARMFYHRPK 624
Cdd:cd03226  81 DYQ-LFTDSVREelllgLKELDAGNEQAETVLKDLDLY-------------ALKERhplsLSGGQKQRLAIAAALLSGKD 146
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 7262393  625 YALLDECTSAV---SIDVEGKIFQAAKDAGIALLSITH 659
Cdd:cd03226 147 LLIFDEPTSGLdykNMERVGELIRELAAQGKAVIVITH 184
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
474-663 7.86e-17

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: 84.26  E-value: 7.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGV-------LYKPPP----QRMFYI 542
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSiavngvpLADADAdswrDQIAWV 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    543 PQRPYMSVGSLRDQVIypdsvedMQRKGYSEQDLEAILDVVHLHHILQ-REGGWEAMCDWKDV-LSGGEKQRIGMARMFY 620
Cdd:TIGR02857 402 PQHPFLFAGTIAENIR-------LARPDASDAEIREALERAGLDEFVAaLPQGLDTPIGEGGAgLSGGQAQRLALARAFL 474
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 7262393    621 HRPKYALLDECTSAVSIDVEGKIFQAAKDA--GIALLSITHRPSL 663
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLAL 519
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
486-663 1.00e-16

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: 78.63  E-value: 1.00e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYkpppqrmfyipqrpymsvgsLRDQviypdSVED 565
Cdd:cd03214  11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL--------------------LDGK-----DLAS 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  566 MQRK------GYSEQdleaILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAV---- 635
Cdd:cd03214  66 LSPKelarkiAYVPQ----ALELLGLAHLADRP---------FNELSGGERQRVLLARALAQEPPILLLDEPTSHLdiah 132
                       170       180
                ....*....|....*....|....*...
gi 7262393  636 SIDVEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:cd03214 133 QIELLELLRRLARERGKTVVMVLHDLNL 160
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
474-662 1.56e-16

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: 79.58  E-value: 1.56e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP----------QRMFYI 542
Cdd:cd03254   3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYdPQKGQILIDGIDirdisrkslrSMIGVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  543 PQRPYMSVGSLRDQVIYPDSVEDmqrkgysEQDLEAILDVVHLHH-ILQREGGWEA-MCDWKDVLSGGEKQRIGMARMFY 620
Cdd:cd03254  83 LQDTFLFSGTIMENIRLGRPNAT-------DEEVIEAAKEAGAHDfIMKLPNGYDTvLGENGGNLSQGERQLLAIARAML 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 7262393  621 HRPKYALLDECTSavSIDVEG-KIFQAAKDA---GIALLSITHRPS 662
Cdd:cd03254 156 RDPKILILDEATS--NIDTETeKLIQEALEKlmkGRTSIIIAHRLS 199
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
486-663 2.20e-16

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 79.70  E-value: 2.20e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY---KP----PP----QRMFYIPQRPYMSVGSlr 554
Cdd:COG1120  13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDlaslSRrelaRRIAYVPQEPPAPFGL-- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  555 dqviypdSVED---MQRKGY-------SEQDLEAI---LDVVHLHHILQReggweamcDWkDVLSGGEKQRIGMARMFYH 621
Cdd:COG1120  91 -------TVRElvaLGRYPHlglfgrpSAEDREAVeeaLERTGLEHLADR--------PV-DELSGGERQRVLIARALAQ 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 7262393  622 RPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:COG1120 155 EPPLLLLDEPTSHLdlahQLEVLELLRRLARERGRTVVMVLHDLNL 200
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
484-663 4.03e-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: 78.14  E-value: 4.03e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK---PPPQRMFYIPQRpymsVGSL----RD 555
Cdd:COG1122  11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLkPTSGEVLVDgkdITKKNLRELRRK----VGLVfqnpDD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  556 QVIYPdSVED-----MQRKGYSEQDLEA----ILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYA 626
Cdd:COG1122  87 QLFAP-TVEEdvafgPENLGLPREEIRErveeALELVGLEHLADRP---------PHELSGGQKQRVAIAGVLAMEPEVL 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 7262393  627 LLDECTSavSIDVEGK-----IFQAAKDAGIALLSITHRPSL 663
Cdd:COG1122 157 VLDEPTA--GLDPRGRrelleLLKRLNKEGKTVIIVTHDLDL 196
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
477-663 5.55e-16

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: 81.72  E-value: 5.55e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  477 ENIPIVTP-SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGV-------LYKPPPQR----MFYIPQ 544
Cdd:COG4618 334 ENLTVVPPgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSvrldgadLSQWDREElgrhIGYLPQ 413
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  545 rpymsvgslrDQVIYPDSVED----MQrkgysEQDLEAILD---VVHLHHILQR----------EGGweamcdwkDVLSG 607
Cdd:COG4618 414 ----------DVELFDGTIAEniarFG-----DADPEKVVAaakLAGVHEMILRlpdgydtrigEGG--------ARLSG 470
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7262393  608 GEKQRIGMARMFYHRPKYALLDECTSavSIDVEG-----KIFQAAKDAGIALLSITHRPSL 663
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNS--NLDDEGeaalaAAIRALKARGATVVVITHRPSL 529
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
486-659 6.04e-16

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 78.21  E-value: 6.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYG-----GVLYKPPPQRMFYIPQRPYMSVGslrdqviY 559
Cdd:COG1121  18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILGLLPPTSGtvrlfGKPPRRARRRIGYVPQRAEVDWD-------F 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  560 PDSVED---MQR-------KGYSEQDLEAI---LDVVHLHHILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRP 623
Cdd:COG1121  91 PITVRDvvlMGRygrrglfRRPSRADREAVdeaLERVGLEDLADRpigE------------LSGGQQQRVLLARALAQDP 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 7262393  624 KYALLDECTSAVsiDVEG-----KIFQAAKDAGIALLSITH 659
Cdd:COG1121 159 DLLLLDEPFAGV--DAATeealyELLRELRREGKTILVVTH 197
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
483-630 6.79e-16

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 78.21  E-value: 6.79e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  483 TPSGEV-VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY-----KPPPQRMFYIPQR----PYMSVg 551
Cdd:COG1116  19 TGGGGVtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEkPTSGEVLVdgkpvTGPGPDRGVVFQEpallPWLTV- 97
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7262393  552 slRDQVIYPDSVEDMQRKgYSEQDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:COG1116  98 --LDNVALGLELRGVPKA-ERRERARELLELVGLAGFEDA---------YPHQLSGGMRQRVAIARALANDPEVLLMDE 164
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
488-630 8.16e-16

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: 77.13  E-value: 8.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLY-----KPPPQRMFYIPQR----PYMSVgslRDQV 557
Cdd:cd03293  18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLeRPTSGEVLVdgepvTGPGPDRGYVFQQdallPWLTV---LDNV 94
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7262393  558 IYPDSVEDMQRKGySEQDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:cd03293  95 ALGLELQGVPKAE-ARERAEELLELVGLSGFENA---------YPHQLSGGMRQRVALARALAVDPDVLLLDE 157
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
489-659 1.31e-15

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: 76.84  E-value: 1.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW------PTYGGVLYKPPP------------QRMFYIPQRPYMSV 550
Cdd:cd03260  15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgaPDEGEVLLDGKDiydldvdvlelrRRVGMVFQKPNPFP 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  551 GSLRDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLhhilqreggWEAMCDWKDV--LSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03260  95 GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAAL---------WDEVKDRLHAlgLSGGQQQRLCLARALANEPEVLLL 165
                       170       180       190
                ....*....|....*....|....*....|....*
gi 7262393  629 DECTSAVSI----DVEGKIFQAAKDAGIALlsITH 659
Cdd:cd03260 166 DEPTSALDPistaKIEELIAELKKEYTIVI--VTH 198
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
486-659 3.47e-15

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: 75.45  E-value: 3.47e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYK-------PPPQRMF-YIPQR----PYMSVgs 552
Cdd:cd03299  11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLEtIAGFIKPDSGKILLNgkditnlPPEKRDIsYVPQNyalfPHMTV-- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  553 lRDQVIYPDSVEDMQRKGYSEQDLEaILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:cd03299  89 -YKNIAYGLKKRKVDKKEIERKVLE-IAEMLGIDHLLNRKPE---------TLSGGEQQRVAIARALVVNPKILLLDEPF 157
                       170       180       190
                ....*....|....*....|....*....|.
gi 7262393  633 SAVSIDVEGKIFQAAKDA----GIALLSITH 659
Cdd:cd03299 158 SALDVRTKEKLREELKKIrkefGVTVLHVTH 188
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
484-663 3.69e-15

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 75.47  E-value: 3.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  484 PSGEVVVASL---NIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYK-------PPPQR-MF------YIPQR 545
Cdd:COG1136  15 GTGEGEVTALrgvSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVLIDgqdisslSERELaRLrrrhigFVFQF 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  546 ----PYMSVgslRDQVIYPDSVEDMQRKGySEQDLEAILDVVHLHHILQR---EggweamcdwkdvLSGGEKQRIGMARM 618
Cdd:COG1136  95 fnllPELTA---LENVALPLLLAGVSRKE-RRERARELLERVGLGDRLDHrpsQ------------LSGGQQQRVAIARA 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 7262393  619 FYHRPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:COG1136 159 LVNRPKLILADEPTGNLdsktGEEVLELLRELNRELGTTIVMVTHDPEL 207
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
486-659 1.43e-14

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: 73.81  E-value: 1.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYK-------PPPQRMF-YIPQR----PYMSVGs 552
Cdd:cd03300  12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFeTPTSGEILLDgkditnlPPHKRPVnTVFQNyalfPHLTVF- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  553 lrDQVIYPdsvedMQRKGYSEQDLEA----ILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03300  91 --ENIAFG-----LRLKKLPKAEIKErvaeALDLVQLEGYANRK---------PSQLSGGQQQRVAIARALVNEPKVLLL 154
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 7262393  629 DECTSAV------SIDVEGKIFQaaKDAGIALLSITH 659
Cdd:cd03300 155 DEPLGALdlklrkDMQLELKRLQ--KELGITFVFVTH 189
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
505-662 3.00e-14

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: 72.33  E-value: 3.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  505 ITGPNGCGKSSLFRILGGLWPTYGGVLY--------------KPPPQRMF-YIPQR----PYMSVgslRDQVIYpdsveD 565
Cdd:cd03297  28 IFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrkkinLPPQQRKIgLVFQQyalfPHLNV---RENLAF-----G 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  566 MQRKGYSE--QDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKI 643
Cdd:cd03297 100 LKRKRNREdrISVDELLDLLGLDHLLNR---------YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
                       170       180
                ....*....|....*....|...
gi 7262393  644 F----QAAKDAGIALLSITHRPS 662
Cdd:cd03297 171 LpelkQIKKNLNIPVIFVTHDLS 193
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
484-662 4.86e-14

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: 72.13  E-value: 4.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK--------PPPQR--MFYIPQRPYMSVGS 552
Cdd:cd03252  12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYvPENGRVLVDghdlaladPAWLRrqVGVVLQENVLFNRS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  553 LRDQVIYPDSVEDMQRKGYSeqdleAILDVVHlHHILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDEC 631
Cdd:cd03252  92 IRDNIALADPGMSMERVIEA-----AKLAGAH-DFISELPEGYDTIVGEQGAgLSGGQRQRIAIARALIHNPRILIFDEA 165
                       170       180       190
                ....*....|....*....|....*....|...
gi 7262393  632 TSAVSIDVEGKIFQAAKD--AGIALLSITHRPS 662
Cdd:cd03252 166 TSALDYESEHAIMRNMHDicAGRTVIIIAHRLS 198
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
484-659 5.43e-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: 70.91  E-value: 5.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRIL-GGLWPTYGGVLYKPPP------------QRMFYIPQRPymsv 550
Cdd:TIGR01166   2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLnGLLRPQSGAVLIDGEPldysrkgllerrQRVGLVFQDP---- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    551 gslRDQVIYPDSVEDM----QRKGYSEQDLEAI----LDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHR 622
Cdd:TIGR01166  78 ---DDQLFAADVDQDVafgpLNLGLSEAEVERRvreaLTAVGASGLRERP---------THCLSGGEKKRVAIAGAVAMR 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 7262393    623 PKYALLDECTSAVsiDVEG-----KIFQAAKDAGIALLSITH 659
Cdd:TIGR01166 146 PDVLLLDEPTAGL--DPAGreqmlAILRRLRAEGMTVVISTH 185
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
486-662 5.55e-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: 71.40  E-value: 5.55e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLY------KPPPQR-----MFyipQR----PYMS 549
Cdd:cd03259  12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLeRPDSGEILIdgrdvtGVPPERrnigmVF---QDyalfPHLT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  550 VgslRDQVIYPdsvedMQRKGYSEQDLEA----ILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKY 625
Cdd:cd03259  89 V---AENIAFG-----LKLRGVPKAEIRArvreLLELVGLEGLLNR---------YPHELSGGQQQRVALARALAREPSL 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 7262393  626 ALLDECTSAvsIDVE------GKIFQAAKDAGIALLSITHRPS 662
Cdd:cd03259 152 LLLDEPLSA--LDAKlreelrEELKELQRELGITTIYVTHDQE 192
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
493-662 8.34e-14

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: 71.80  E-value: 8.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVL--------YKPPPQR--MFYIPQRPYMSVGSLRDQVIYPD 561
Cdd:cd03249  22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYdPTSGEILldgvdirdLNLRWLRsqIGLVSQEPVLFDGTIAENIRYGK 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  562 svedmqRKGYSEQDLEAILDVVHLHHILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVE 640
Cdd:cd03249 102 ------PDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSqLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
                       170       180
                ....*....|....*....|....*
gi 7262393  641 gKIFQAAKD---AGIALLSITHRPS 662
Cdd:cd03249 176 -KLVQEALDramKGRTTIVIAHRLS 199
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
486-661 9.05e-14

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 70.67  E-value: 9.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLYKP-------PPQRMFYIPQR----PYMSVGsl 553
Cdd:PRK13539  14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtIKLDGgdiddpdVAEACHYLGHRnamkPALTVA-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   554 rdqviypDSVEDMQR-KGYSEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMAR-MFYHRPKYaLLDEC 631
Cdd:PRK13539  92 -------ENLEFWAAfLGGEELDIAAALEAVGLAPLAHLPFG---------YLSAGQKRRVALARlLVSNRPIW-ILDEP 154
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 7262393   632 TSAvsIDVEGK-----IFQA-AKDAGIALLSiTHRP 661
Cdd:PRK13539 155 TAA--LDAAAValfaeLIRAhLAQGGIVIAA-THIP 187
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
489-659 1.07e-13

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: 71.37  E-value: 1.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP------TYGGVLYKPPPQRMFY-----IPQRPYMSV---GSLR 554
Cdd:COG1124  20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERpwsgevTFDGRPVTRRRRKAFRrrvqmVFQDPYASLhprHTVD 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  555 DQVIYPDSVedmQRKGYSEQDLEAILDVVHLH-HILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:COG1124 100 RILAEPLRI---HGLPDREERIAELLEQVGLPpSFLDRyphQ------------LSGGQRQRVAIARALILEPELLLLDE 164
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 7262393  631 CTSAVsiDVegkIFQAA---------KDAGIALLSITH 659
Cdd:COG1124 165 PTSAL--DV---SVQAEilnllkdlrEERGLTYLFVSH 197
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
494-630 1.29e-13

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 73.95  E-value: 1.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  494 NIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVG-SLRDQVI--YPDSVEDMQRK- 569
Cdd:COG0488  18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDlTVLDTVLdgDAELRALEAELe 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  570 ------GYSEQDLEAIldvVHLHHILQREGGWEA--------------MCDW-KDV--LSGGEKQRIGMARMFYHRPKYA 626
Cdd:COG0488  98 eleaklAEPDEDLERL---AELQEEFEALGGWEAearaeeilsglgfpEEDLdRPVseLSGGWRRRVALARALLSEPDLL 174

                ....
gi 7262393  627 LLDE 630
Cdd:COG0488 175 LLDE 178
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
488-659 1.37e-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: 69.35  E-value: 1.37e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  488 VVVASLNIRVEEG--MHLLitGPNGCGKSSLFRILGGLW-PTYGGVLY--KPPP-------QRMFYIPQRPYmsvgslrd 555
Cdd:cd03230  14 TALDDISLTVEKGeiYGLL--GPNGAGKTTLIKIILGLLkPDSGEIKVlgKDIKkepeevkRRIGYLPEEPS-------- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  556 qvIYPD-SVEDmqrkgyseqdleaildvvHLHhilqreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSA 634
Cdd:cd03230  84 --LYENlTVRE------------------NLK------------------LSGGMKQRLALAQALLHDPELLILDEPTSG 125
                       170       180       190
                ....*....|....*....|....*....|
gi 7262393  635 vsIDVEG-----KIFQAAKDAGIALLSITH 659
Cdd:cd03230 126 --LDPESrrefwELLRELKKEGKTILLSSH 153
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
493-659 1.94e-13

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: 70.57  E-value: 1.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYK------PPPQRMFYIPQR---PYMSVgslRDQV-IYPD 561
Cdd:TIGR01184   4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEgkqitePGPDRMVVFQNYsllPWLTV---RENIaLAVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    562 SVEDMQRKGYSEQDLEAILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSI---- 637
Cdd:TIGR01184  81 RVLPDLSKSERRAIVEEHIALVGLTEAADKR---------PGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrg 151
                         170       180
                  ....*....|....*....|..
gi 7262393    638 DVEGKIFQAAKDAGIALLSITH 659
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTH 173
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
474-664 2.31e-13

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 73.40  E-value: 2.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  474 IICENIPIVTPSGEV-VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGV----------LYKPPPQ----R 538
Cdd:COG1123   5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIsgevlldgrdLLELSEAlrgrR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  539 MFYIPQRPYMSVGSLR--DQVIYPDSVEDMQRKGYSEQDLEAiLDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMA 616
Cdd:COG1123  85 IGMVFQDPMTQLNPVTvgDQIAEALENLGLSRAEARARVLEL-LEAVGLERRLDR---------YPHQLSGGQRQRVAIA 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 7262393  617 RMFYHRPKYALLDECTSA----VSIDVEGKIFQAAKDAGIALLSITHRPSLW 664
Cdd:COG1123 155 MALALDPDLLIADEPTTAldvtTQAEILDLLRELQRERGTTVLLITHDLGVV 206
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
488-659 3.00e-13

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 70.09  E-value: 3.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY--KPPP-------QRMFYIPQRPYMsvgslrdqv 557
Cdd:COG1131  14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLrPTSGEVRVlgEDVArdpaevrRRIGYVPQEPAL--------- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  558 iYPD-SVEDM---------QRKGYSEQDLEAILDVVHLHHILQREGGWeamcdwkdvLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:COG1131  85 -YPDlTVRENlrffarlygLPRKEARERIDELLELFGLTDAADRKVGT---------LSGGMKQRLGLALALLHDPELLI 154
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 7262393  628 LDECTSAVsiDVEG-----KIFQAAKDAGIA-LLSiTH 659
Cdd:COG1131 155 LDEPTSGL--DPEArrelwELLRELAAEGKTvLLS-TH 189
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
474-662 3.62e-13

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: 69.57  E-value: 3.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVL--------YKPPPQR--MFYI 542
Cdd:cd03253   1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYdVSSGSILidgqdireVTLDSLRraIGVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  543 PQrpymsvgslrDQVIYPDSVEDMQRKG---YSEQDLEAILDVVHLHH-ILQREGGWEAMCDWKDV-LSGGEKQRIGMAR 617
Cdd:cd03253  81 PQ----------DTVLFNDTIGYNIRYGrpdATDEEVIEAAKAAQIHDkIMRFPDGYDTIVGERGLkLSGGEKQRVAIAR 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 7262393  618 MFYHRPKYALLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHRPS 662
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDvsKGRTTIVIAHRLS 197
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
480-659 6.19e-13

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 71.86  E-value: 6.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  480 PIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY-------------KPPPQRMFYIPQR 545
Cdd:COG1123 271 PVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLrPTSGSILFdgkdltklsrrslRELRRRVQMVFQD 350
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  546 PY------MSVGslrDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLH-HILQR---EggweamcdwkdvLSGGEKQRIGM 615
Cdd:COG1123 351 PYsslnprMTVG---DIIAEPLRLHGLLSRAERRERVAELLERVGLPpDLADRyphE------------LSGGQRQRVAI 415
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7262393  616 ARMFYHRPKYALLDECTSA--VSIdvegkifQA---------AKDAGIALLSITH 659
Cdd:COG1123 416 ARALALEPKLLILDEPTSAldVSV-------QAqilnllrdlQRELGLTYLFISH 463
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
486-661 6.36e-13

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: 69.34  E-value: 6.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLY----KPPPQRMFYIpqRPYMSV--GSLRDQVI 558
Cdd:COG1119  15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRlfgeRRGGEDVWEL--RKRIGLvsPALQLRFP 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  559 YPDSVEDMQRKG----------YSEQDLE---AILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKY 625
Cdd:COG1119  93 RDETVLDVVLSGffdsiglyrePTDEQRErarELLELLGLAHLADRPFG---------TLSQGEQRRVLIARALVKDPEL 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 7262393  626 ALLDECTSavSIDVEGK------IFQAAKDAGIALLSITHRP 661
Cdd:COG1119 164 LILDEPTA--GLDLGARelllalLDKLAAEGAPTLVLVTHHV 203
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
489-659 6.47e-13

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 69.37  E-value: 6.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSvgslrdqVIYPDSVED--M 566
Cdd:PRK09544  19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLD-------TTLPLTVNRflR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   567 QRKGYSEQDLEAILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVsiDVEGK---- 642
Cdd:PRK09544  92 LRPGTKKEDILPALKRVQAGHLIDAP---------MQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV--DVNGQvaly 160
                        170
                 ....*....|....*....
gi 7262393   643 --IFQAAKDAGIALLSITH 659
Cdd:PRK09544 161 dlIDQLRRELDCAVLMVSH 179
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
461-678 6.86e-13

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 68.94  E-value: 6.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  461 LKIRGQVVDVEQGIICENIPIVTPSGEVVVaslnirveegmhllITGPNGCGKSSLFRILGGLwPTY----GGVLYK--- 533
Cdd:COG0396   1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHA--------------IMGPNGSGKSTLAKVLMGH-PKYevtsGSILLDged 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  534 ----PPPQR----MFYIPQRP------------YMSVGSLRDQVIypdSVEDMQRKgyseqdLEAILDVVHL-HHILQR- 591
Cdd:COG0396  66 ilelSPDERaragIFLAFQYPveipgvsvsnflRTALNARRGEEL---SAREFLKL------LKEKMKELGLdEDFLDRy 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  592 --EGgweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID---VEGKIFQAAKDAGIALLSITHRPSLWKY 666
Cdd:COG0396 137 vnEG-----------FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDalrIVAEGVNKLRSPDRGILIITHYQRILDY 205
                       250       260
                ....*....|....*....|
gi 7262393  667 ----HTHLLqFDG----EGG 678
Cdd:COG0396 206 ikpdFVHVL-VDGrivkSGG 224
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
486-659 1.13e-12

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: 68.35  E-value: 1.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLY------KPPP---QRMFYIPQRPYMSVG-SLR 554
Cdd:COG4555  13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGlLKPDSGSILIdgedvrKEPRearRQIGVLPDERGLYDRlTVR 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  555 DQV-----IYPDSVEDMQRKG--YSEQ-DLEAILDvvhlhhilQREGGweamcdwkdvLSGGEKQRIGMARMFYHRPKYA 626
Cdd:COG4555  93 ENIryfaeLYGLFDEELKKRIeeLIELlGLEEFLD--------RRVGE----------LSTGMKKKVALARALVHDPKVL 154
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 7262393  627 LLDECTSAvsIDVEG-----KIFQAAKDAGIALLSITH 659
Cdd:COG4555 155 LLDEPTNG--LDVMArrllrEILRALKKEGKTVLFSSH 190
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
505-675 1.52e-12

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: 67.50  E-value: 1.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  505 ITGPNGCGKSSLFRILGGLWPTYGGVLY---KPPPQ--------RMFYIPQRPYMSVGSLRDQVIYpdsveDMQRKgySE 573
Cdd:cd03248  45 LVGPSGSGKSTVVALLENFYQPQGGQVLldgKPISQyehkylhsKVSLVGQEPVLFARSLQDNIAY-----GLQSC--SF 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  574 QDLEAILDVVHLHHILQR--EGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKD-- 649
Cdd:cd03248 118 ECVKEAAQKAHAHSFISElaSGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDwp 197
                       170       180
                ....*....|....*....|....*.
gi 7262393  650 AGIALLSITHRPSLWKYHTHLLQFDG 675
Cdd:cd03248 198 ERRTVLVIAHRLSTVERADQILVLDG 223
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
484-660 1.71e-12

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: 67.52  E-value: 1.71e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSS----LFRILgglwPTYGGVLY-------KPPP----QRMFYIPQRPYM 548
Cdd:cd03244  14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILidgvdisKIGLhdlrSRISIIPQDPVL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  549 SVGSLRDQvIYPDSVedmqrkgYSEQDLEAILDVVHL-HHILQREGGWEAM-CDWKDVLSGGEKQRIGMARMFYHRPKYA 626
Cdd:cd03244  90 FSGTIRSN-LDPFGE-------YSDEELWQALERVGLkEFVESLPGGLDTVvEEGGENLSVGQRQLLCLARALLRKSKIL 161
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 7262393  627 LLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHR 660
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIREafKDCTVLTIAHR 197
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
486-666 1.89e-12

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: 66.78  E-value: 1.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLwPTY----GGVLYK-------PPPQR----MFYIPQRPYMSV 550
Cdd:cd03217  12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYevteGEILFKgeditdlPPEERarlgIFLAFQYPPEIP 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  551 GSlrdqviypdSVEDMQRkgyseqdleailDVvhlhhilqREGgweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:cd03217  91 GV---------KNADFLR------------YV--------NEG-----------FSGGEKKRNEILQLLLLEPDLAILDE 130
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 7262393  631 CTSAVSID---VEGKIFQAAKDAGIALLSITHRPSLWKY 666
Cdd:cd03217 131 PDSGLDIDalrLVAEVINKLREEGKSVLIITHYQRLLDY 169
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
488-660 2.88e-12

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: 66.54  E-value: 2.88e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVL---YKP----PPQRMFYIPQR----PYMSVgslRDQ 556
Cdd:cd03269  14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdGKPldiaARNRIGYLPEErglyPKMKV---IDQ 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  557 VIYPDSVEDMQRKgYSEQDLEAILDVVHL-HHILQReggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTSA- 634
Cdd:cd03269  91 LVYLAQLKGLKKE-EARRRIDEWLERLELsEYANKR----------VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGl 159
                       170       180
                ....*....|....*....|....*...
gi 7262393  635 --VSIDVEGKIFQAAKDAGIALLSITHR 660
Cdd:cd03269 160 dpVNVELLKDVIRELARAGKTVILSTHQ 187
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
488-660 3.00e-12

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: 67.08  E-value: 3.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  488 VVVASLNIRVEEG-MHLLItGPNGCGKSSLFRILGG-LWPTYGGVLYK-------PPPQ-------RMFYIPqRPY--MS 549
Cdd:cd03219  14 VALDDVSFSVRPGeIHGLI-GPNGAGKTTLFNLISGfLRPTSGSVLFDgeditglPPHEiarlgigRTFQIP-RLFpeLT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  550 V------GSLRDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRP 623
Cdd:cd03219  92 VlenvmvAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAG---------ELSYGQQRRLEIARALATDP 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 7262393  624 KYALLDECTSAVS---IDVEGKIFQAAKDAGIALLSITHR 660
Cdd:cd03219 163 KLLLLDEPAAGLNpeeTEELAELIRELRERGITVLLVEHD 202
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
489-660 3.90e-12

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 69.47  E-value: 3.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP----------QRMFYIPQRPYMSVGSLRD-- 555
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWdPQQGEILLNGQPiadyseaalrQAISVVSQRVHLFSATLRDnl 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   556 QVIYPDSvedmqrkgySEQDLEAILDVVHLHHILQREGGWEA-MCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSA 634
Cdd:PRK11160 435 LLAAPNA---------SDEALIEVLQQVGLEKLLEDDKGLNAwLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
                        170       180
                 ....*....|....*....|....*...
gi 7262393   635 VSIDVEGKIFQAAKD--AGIALLSITHR 660
Cdd:PRK11160 506 LDAETERQILELLAEhaQNKTVLMITHR 533
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
489-659 4.51e-12

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: 66.38  E-value: 4.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK-----PPPQRMF--------YIPQRPY------M 548
Cdd:cd03257  20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLkPTSGSIIFDgkdllKLSRRLRkirrkeiqMVFQDPMsslnprM 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  549 SVGslrDQVIYPDSVEDMQRKgYSEQDLEAILDVVHLH---HILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHR 622
Cdd:cd03257 100 TIG---EQIAEPLRIHGKLSK-KEARKEAVLLLLVGVGlpeEVLNRyphE------------LSGGQRQRVAIARALALN 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 7262393  623 PKYALLDECTSAVSIDVEGKIFQAAKDA----GIALLSITH 659
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLqeelGLTLLFITH 204
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
489-659 9.05e-12

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: 64.93  E-value: 9.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK-PPPQRMFYIPQRpymsVGSLRD-QVIYPD--SV 563
Cdd:cd03268  15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIkPDSGEITFDgKSYQKNIEALRR----IGALIEaPGFYPNltAR 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  564 EDMQRK----GYSEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAvsIDV 639
Cdd:cd03268  91 ENLRLLarllGIRKKRIDEVLDVVGLKDSAKKKVK---------GFSLGMKQRLGIALALLGNPDLLILDEPTNG--LDP 159
                       170       180
                ....*....|....*....|....*
gi 7262393  640 EG-----KIFQAAKDAGIALLSITH 659
Cdd:cd03268 160 DGikelrELILSLRDQGITVLISSH 184
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
474-663 9.22e-12

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 65.07  E-value: 9.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLY------KPPPQRMfyipqrP 546
Cdd:COG2884   2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKlLYGEERPTSGQVLVngqdlsRLKRREI------P 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  547 YM--SVGslrdqVIYPD-------SVED-----MQRKGYSEQDL----EAILDVVHLHHILqreggwEAMCDwkdVLSGG 608
Cdd:COG2884  76 YLrrRIG-----VVFQDfrllpdrTVYEnvalpLRVTGKSRKEIrrrvREVLDLVGLSDKA------KALPH---ELSGG 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7262393  609 EKQRIGMARMFYHRPKYALLDECT----SAVSIDVEgKIFQAAKDAGIALLSITHRPSL 663
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTgnldPETSWEIM-ELLEEINRRGTTVLIATHDLEL 199
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
489-663 1.24e-11

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 68.21  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMF---YI-------PQRPYMSVGSLRDQV 557
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPTGGQVLLDGVPLVQYdhhYLhrqvalvGQEPVLFSGSVRENI 575
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    558 IYpdsvedmqrkGYSEQDLEAILDVVHLHH----ILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:TIGR00958 576 AY----------GLTDTPDEEIMAAAKAANahdfIMEFPNGYDTEVGEKGSqLSGGQKQRIAIARALVRKPRVLILDEAT 645
                         170       180       190
                  ....*....|....*....|....*....|.
gi 7262393    633 SAVSIDVEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:TIGR00958 646 SALDAECEQLLQESRSRASRTVLLIAHRLST 676
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
489-655 1.28e-11

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: 64.76  E-value: 1.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLY-------KPPPQR----MFYIPQrpymsvgslrDQ 556
Cdd:cd03224  15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsIRFdgrditgLPPHERaragIGYVPE----------GR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  557 VIYPD-SVED-------MQRKGYSEQDLEAILDVV-HLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:cd03224  85 RIFPElTVEEnlllgayARRRAKRKARLERVYELFpRLKERRKQLAG---------TLSGGEQQMLAIARALMSRPKLLL 155
                       170       180       190
                ....*....|....*....|....*....|.
gi 7262393  628 LDECTSAVSIDVEGKIFQAA---KDAGIALL 655
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIrelRDEGVTIL 186
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
486-634 1.50e-11

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 66.89  E-value: 1.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYK-------PPPQR----------MFyipqrPY 547
Cdd:PRK09452  26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFeTPDSGRIMLDgqdithvPAENRhvntvfqsyaLF-----PH 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   548 MSVgslRDQVIYPdsvEDMQRKGYSEQD---LEAiLDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPK 624
Cdd:PRK09452 101 MTV---FENVAFG---LRMQKTPAAEITprvMEA-LRMVQLEEFAQRK---------PHQLSGGQQQRVAIARAVVNKPK 164
                        170
                 ....*....|
gi 7262393   625 YALLDECTSA 634
Cdd:PRK09452 165 VLLLDESLSA 174
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
486-630 1.70e-11

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 66.78  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVL-------YKPPPQR----MFyipQR----PYMS 549
Cdd:PRK11607  31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMldgvdlsHVPPYQRpinmMF---QSyalfPHMT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   550 VgslrDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:PRK11607 108 V----EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRK---------PHQLSGGQRQRVALARSLAKRPKLLLLD 174

                 .
gi 7262393   630 E 630
Cdd:PRK11607 175 E 175
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
484-661 1.91e-11

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: 67.00  E-value: 1.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG--VLYKPPPQ---------RMFYIPQRPYMSVGS 552
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGevTLDGVPVSsldqdevrrRVSVCAQDAHLFDTT 424
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    553 LRDQVIypdsvedMQRKGYSEQDLEAILDVVHLHHILQR--EGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:TIGR02868 425 VRENLR-------LARPDATDEELWAALERVGLADWLRAlpDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDE 497
                         170       180       190
                  ....*....|....*....|....*....|...
gi 7262393    631 CTSAVSIDVEGKIFQ--AAKDAGIALLSITHRP 661
Cdd:TIGR02868 498 PTEHLDAETADELLEdlLAALSGRTVVLITHHL 530
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
486-630 2.03e-11

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 66.25  E-value: 2.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG--------VLYKPPPQRMF-YIPQR----PYMSVgs 552
Cdd:COG3839  15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGeiliggrdVTDLPPKDRNIaMVFQSyalyPHMTV-- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  553 lRDQVIYPdsvedMQRKGYSEQDLEA----ILDVVHLHHILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRPKY 625
Cdd:COG3839  93 -YENIAFP-----LKLRKVPKAEIDRrvreAAELLGLEDLLDRkpkQ------------LSGGQRQRVALGRALVREPKV 154

                ....*
gi 7262393  626 ALLDE 630
Cdd:COG3839 155 FLLDE 159
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
474-643 2.67e-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: 63.75  E-value: 2.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  474 IICENIPIVTPSGeVVVASLNIRVEEGMHLLItGPNGCGKSSLFRILGGLW-PTYGGVL---YKPPPQRMF------YIP 543
Cdd:cd03264   1 LQLENLTKRYGKK-RALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTpPSSGTIRidgQDVLKQPQKlrrrigYLP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  544 QR----PYMSVgslRDQVIYPDSVEDMQRKGySEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMF 619
Cdd:cd03264  79 QEfgvyPNFTV---REFLDYIAWLKGIPSKE-VKARVDEVLELVNLGDRAKKKIG---------SLSGGMRRRVGIAQAL 145
                       170       180
                ....*....|....*....|....
gi 7262393  620 YHRPKYALLDECTsaVSIDVEGKI 643
Cdd:cd03264 146 VGDPSILIVDEPT--AGLDPEERI 167
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
486-659 3.48e-11

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 63.27  E-value: 3.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWP--TYGGVLY--------KPPPQR-MFYIPQR----PYMS 549
Cdd:COG4136  13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPafSASGEVLlngrrltaLPAEQRrIGILFQDdllfPHLS 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  550 VG-----SLrdqviyPDSVEDMQRKgyseQDLEAILDVVHLHHILQReggweamcdwkDV--LSGGEKQRIGMARMFYHR 622
Cdd:COG4136  93 VGenlafAL------PPTIGRAQRR----ARVEQALEEAGLAGFADR-----------DPatLSGGQRARVALLRALLAE 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 7262393  623 PKYALLDECTS----AVSIDVEGKIFQAAKDAGIALLSITH 659
Cdd:COG4136 152 PRALLLDEPFSkldaALRAQFREFVFEQIRQRGIPALLVTH 192
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
486-630 5.35e-11

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 65.05  E-value: 5.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   486 GEVVVAS-LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKpPPQRMFYIP--QRpymSVGSL-RDQVIYP- 560
Cdd:PRK11000  14 GDVVISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRMNDVPpaER---GVGMVfQSYALYPh 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7262393   561 -DSVEDMQ--------RKGYSEQDLEAILDVVHLHHILQREGgweamcdwKDvLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:PRK11000  90 lSVAENMSfglklagaKKEEINQRVNQVAEVLQLAHLLDRKP--------KA-LSGGQRQRVAIGRTLVAEPSVFLLDE 159
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
487-663 6.22e-11

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 62.67  E-value: 6.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  487 EVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLwptyggvLYKPPPQRMFYIPQRPYMSVGSLRDQVI----YPDS 562
Cdd:COG2401  43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA-------LKGTPVAGCVDVPDNQFGREASLIDAIGrkgdFKDA 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  563 VEDMQRKGYSEqdleAILdvvhlhhilqreggweamcdWK---DVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID- 638
Cdd:COG2401 116 VELLNAVGLSD----AVL--------------------WLrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQt 171
                       170       180
                ....*....|....*....|....*...
gi 7262393  639 ---VEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:COG2401 172 akrVARNLQKLARRAGITLVVATHHYDV 199
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
486-660 6.48e-11

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


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 61.29  E-value: 6.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYkpppqrmfyipqrpymsvgsLRDQVIYPDSVED 565
Cdd:cd03216  12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL--------------------VDGKEVSFASPRD 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  566 MQRKGYSeqdleaildVVHlhhilQreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVS---IDVEGK 642
Cdd:cd03216  72 ARRAGIA---------MVY-----Q--------------LSVGERQMVEIARALARNARLLILDEPTAALTpaeVERLFK 123
                       170
                ....*....|....*...
gi 7262393  643 IFQAAKDAGIALLSITHR 660
Cdd:cd03216 124 VIRRLRAQGVAVIFISHR 141
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
486-643 1.35e-10

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: 64.76  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP----------QRMFYIPQRPYMSVGSLR 554
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFqARSGEILLNGFSlkdidrhtlrQFINYLPQEPYIFSGSIL 565
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    555 DQVIypdsvedMQ-RKGYSEQDLEAILDVVHLH-HILQREGGWEA-MCDWKDVLSGGEKQRIGMARMFYHRPKYALLDEC 631
Cdd:TIGR01193 566 ENLL-------LGaKENVSQDEIWAACEIAEIKdDIENMPLGYQTeLSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
                         170
                  ....*....|..
gi 7262393    632 TSAVSIDVEGKI 643
Cdd:TIGR01193 639 TSNLDTITEKKI 650
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
488-630 1.37e-10

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 61.50  E-value: 1.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY--------KPPPQR---MFYipQR----PYMSVgs 552
Cdd:cd03301  14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdLPPKDRdiaMVF--QNyalyPHMTV-- 89
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7262393  553 lRDQVIYPDSVEDMQRKGYSEQDLEAIlDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:cd03301  90 -YDNIAFGLKLRKVPKDEIDERVREVA-ELLQIEHLLDRK---------PKQLSGGQRQRVALGRAIVREPKVFLMDE 156
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
486-659 1.66e-10

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 63.19  E-value: 1.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG--------VLYKPPPQRMF-YIPQR----PYMSVgs 552
Cdd:COG3842  17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGrilldgrdVTGLPPEKRNVgMVFQDyalfPHLTV-- 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  553 lRDQVIYPdsvedMQRKGYSEQDLEA----ILDVVHLHHILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRPKY 625
Cdd:COG3842  95 -AENVAFG-----LRMRGVPKAEIRArvaeLLELVGLEGLADRyphQ------------LSGGQQQRVALARALAPEPRV 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 7262393  626 ALLDECTSAvsIDVEGK------IFQAAKDAGIALLSITH 659
Cdd:COG3842 157 LLLDEPLSA--LDAKLReemreeLRRLQRELGITFIYVTH 194
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
488-659 1.80e-10

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 61.68  E-value: 1.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLY----------KPPPQRMFYipqrpymsvgsLRDQ 556
Cdd:COG4778  25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKcIYGNYLPDSGSILVrhdggwvdlaQASPREILA-----------LRRR 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  557 VIypdsvedmqrkGYSEQDLEAI-----LDVVH--LhhilqREGGW---EAMCDWKDVL-----------------SGGE 609
Cdd:COG4778  94 TI-----------GYVSQFLRVIprvsaLDVVAepL-----LERGVdreEARARARELLarlnlperlwdlppatfSGGE 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7262393  610 KQRIGMARMFYHRPKYALLDECTSavSIDVEGK-----IFQAAKDAGIALLSITH 659
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTA--SLDAANRavvveLIEEAKARGTAIIGIFH 210
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
489-659 2.27e-10

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 61.62  E-value: 2.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYKPPP-------QRMFYIPQR--PYMSVgslrdqvi 558
Cdd:PRK11247  27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLeTPSAGELLAGTAPlaearedTRLMFQDARllPWKKV-------- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   559 yPDSVEDMQRKGYSEQDLEAiLDVVHLHhilQREGGWEAmcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAVS-- 636
Cdd:PRK11247  99 -IDNVGLGLKGQWRDAALQA-LAAVGLA---DRANEWPA------ALSGGQKQRVALARALIHRPGLLLLDEPLGALDal 167
                        170       180
                 ....*....|....*....|....*
gi 7262393   637 --IDVEGKIFQAAKDAGIALLSITH 659
Cdd:PRK11247 168 trIEMQDLIESLWQQHGFTVLLVTH 192
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
482-646 2.78e-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: 64.16  E-value: 2.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393     482 VTPsgevVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKpppQRMFYIPQRPYMSVGSLRDQVIYP 560
Cdd:TIGR01271  438 VTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPSEGKIKHS---GRISFSPQTSWIMPGTIKDNIIFG 510
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393     561 DSVEDMQRKGYSE--QDLEAILDVVHLHHILQREGGWeamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID 638
Cdd:TIGR01271  511 LSYDEYRYTSVIKacQLEEDIALFPEKDKTVLGEGGI--------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582

                   ....*...
gi 7262393     639 VEGKIFQA 646
Cdd:TIGR01271  583 TEKEIFES 590
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
484-660 2.89e-10

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: 60.02  E-value: 2.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP---------QRMFYIPQRPYMSVGSL 553
Cdd:cd03247  12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLkPQQGEITLDGVPvsdlekalsSLISVLNQRPYLFDTTL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  554 RDQVIYPdsvedmqrkgyseqdleaildvvhlhhilqreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTs 633
Cdd:cd03247  92 RNNLGRR--------------------------------------------FSGGERQRLALARILLQDAPIVLLDEPT- 126
                       170       180       190
                ....*....|....*....|....*....|...
gi 7262393  634 aVSIDVEGK------IFQAAKDAgiALLSITHR 660
Cdd:cd03247 127 -VGLDPITErqllslIFEVLKDK--TLIWITHH 156
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
492-645 4.43e-10

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 63.43  E-value: 4.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393     492 SLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKpppQRMFYIPQRPYMSVGSLRDQVIYPDSVEDmqrkG 570
Cdd:TIGR00957  656 GITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHVHMK---GSVAYVPQQAWIQNDSLRENILFGKALNE----K 728
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7262393     571 YSEQDLEAILDVVHLHHIlqrEGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQ 645
Cdd:TIGR00957  729 YYQQVLEACALLPDLEIL---PSGDRTEIGEKGVnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
483-662 5.40e-10

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: 60.32  E-value: 5.40e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  483 TPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRmfyipqrpYMSVGSLRDQV---- 557
Cdd:cd03251  11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYdVDSGRILIDGHDVR--------DYTLASLRRQIglvs 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  558 ----IYPDSVEDMQRKGYSEQDLEAILDVVHLHH----ILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03251  83 qdvfLFNDTVAENIAYGRPGATREEVEEAARAANahefIMELPEGYDTVIGERGVkLSGGQRQRIAIARALLKDPPILIL 162
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 7262393  629 DECTSAVSIDVEgKIFQAAKD---AGIALLSITHRPS 662
Cdd:cd03251 163 DEATSALDTESE-RLVQAALErlmKNRTTFVIAHRLS 198
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
486-659 6.33e-10

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: 58.74  E-value: 6.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLY------------KPPPQRMFYIPQR----PYM 548
Cdd:cd03229  12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLeEPDSGSILIdgedltdledelPPLRRRIGMVFQDfalfPHL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  549 SVgslRDQVIYPdsvedmqrkgyseqdleaildvvhlhhilqreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03229  92 TV---LENIALG--------------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
                       170       180       190
                ....*....|....*....|....*....|....*
gi 7262393  629 DECTSA----VSIDVEGKIFQAAKDAGIALLSITH 659
Cdd:cd03229 125 DEPTSAldpiTRREVRALLKSLQAQLGITVVLVTH 159
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
486-661 6.89e-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: 59.43  E-value: 6.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMfyipQRPymsvgSLRDQVIYPDSVE 564
Cdd:cd03231  12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSpPLAGRVLLNGGPLDF----QRD-----SIARGLLYLGHAP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  565 DMQRKgyseqdLEAILDVVHLHHILQREGGWEAMCD-----WKDV----LSGGEKQRIGMARMFYHRPKYALLDECTSAV 635
Cdd:cd03231  83 GIKTT------LSVLENLRFWHADHSDEQVEEALARvglngFEDRpvaqLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
                       170       180       190
                ....*....|....*....|....*....|
gi 7262393  636 SIDVEGKIFQA----AKDAGIALLSiTHRP 661
Cdd:cd03231 157 DKAGVARFAEAmaghCARGGMVVLT-THQD 185
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
486-671 7.01e-10

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 59.17  E-value: 7.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRpymsvGSLRDQviYPDSVED 565
Cdd:NF040873   4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQR-----SEVPDS--LPLTVRD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   566 M------QRKG----YSEQD---LEAILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:NF040873  77 LvamgrwARRGlwrrLTRDDraaVDDALERVGLADLAGRQ---------LGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 7262393   633 SAVSIDVEGKIFQ---AAKDAGIALLSITHRPSLWKYHTHLL 671
Cdd:NF040873 148 TGLDAESRERIIAllaEEHARGATVVVVTHDLELVRRADPCV 189
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
489-646 9.90e-10

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: 60.26  E-value: 9.90e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  489 VVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKpppQRMFYIPQRPYMSVGSLRDQVIYPDSVEDMQ 567
Cdd:cd03291  52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELEPSEGKIKHS---GRISFSSQFSWIMPGTIKENIIFGVSYDEYR 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  568 RKGYSE--QDLEAILDVVHLHHILQREGGWeamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQ 645
Cdd:cd03291 129 YKSVVKacQLEEDITKFPEKDNTVLGEGGI--------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFE 200

                .
gi 7262393  646 A 646
Cdd:cd03291 201 S 201
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
474-660 1.08e-09

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 61.78  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYG-----GV-LYKPPP----QRMFYIP 543
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGslkinGIeLRELDPeswrKHLSWVG 429
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   544 QRPYMSVGSLRDQVIypdsvedMQRKGYSEQDLEAILDVVHLHHILQR-EGGWE-AMCDWKDVLSGGEKQRIGMARMFYH 621
Cdd:PRK11174 430 QNPQLPHGTLRDNVL-------LGNPDASDEQLQQALENAWVSEFLPLlPQGLDtPIGDQAAGLSVGQAQRLALARALLQ 502
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 7262393   622 RPKYALLDECTSAVSIDVEGKIFQAAKDA--GIALLSITHR 660
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQ 543
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
484-660 1.11e-09

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 58.96  E-value: 1.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSL----FRILGglwPTYG-----GVLYKPPP-----QRMFYIPQRPYMS 549
Cdd:cd03369  18 PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLilalFRFLE---AEEGkieidGIDISTIPledlrSSLTIIPQDPTLF 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  550 VGSLRDQViypdSVEDMqrkgYSEQDLEAILDVvhlhhilqREGGweamcdwkDVLSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:cd03369  95 SGTIRSNL----DPFDE----YSDEEIYGALRV--------SEGG--------LNLSQGQRQLLCLARALLKRPRVLVLD 150
                       170       180       190
                ....*....|....*....|....*....|...
gi 7262393  630 ECTSAVSIDVEGKIFQAAKD--AGIALLSITHR 660
Cdd:cd03369 151 EATASIDYATDALIQKTIREefTNSTILTIAHR 183
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
489-659 1.21e-09

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 59.74  E-value: 1.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLY--KP----PPQRMFYI----PQRPYMSvgslrdqv 557
Cdd:COG4559  16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSSGEVRLngRPlaawSPWELARRravlPQHSSLA-------- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  558 iYPDSVED---MQRKGYS------EQDLEAILDVVHLHHILQReggweamcDWKDvLSGGEKQRIGMAR-------MFYH 621
Cdd:COG4559  88 -FPFTVEEvvaLGRAPHGssaaqdRQIVREALALVGLAHLAGR--------SYQT-LSGGEQQRVQLARvlaqlwePVDG 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 7262393  622 RPKYALLDECTSAVSIDVEGKIFQAAKD---AGIALLSITH 659
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQlarRGGGVVAVLH 198
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
486-659 1.21e-09

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: 58.70  E-value: 1.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-------VLYKPPP------QRMFYIPQR----PYM 548
Cdd:cd03262  12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtiiidglKLTDDKKninelrQKVGMVFQQfnlfPHL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  549 SVgsLRDQVIYPdsvedMQRKGYSEQDLEAILdvvhlHHILQREGgweaMCDWKDV----LSGGEKQRIGMARMFYHRPK 624
Cdd:cd03262  92 TV--LENITLAP-----IKVKGMSKAEAEERA-----LELLEKVG----LADKADAypaqLSGGQQQRVAIARALAMNPK 155
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 7262393  625 YALLDECTSA----VSIDVEGKIFQAAKDaGIALLSITH 659
Cdd:cd03262 156 VMLFDEPTSAldpeLVGEVLDVMKDLAEE-GMTMVVVTH 193
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
489-660 1.40e-09

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: 59.09  E-value: 1.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK-------PPPQR----MFYIPQRPymSVgsLRDQ 556
Cdd:cd03218  15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGKILLDgqditklPMHKRarlgIGYLPQEA--SI--FRKL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  557 viypdSVED-------MQRKGYSEQD--LEAILDVVHLHHILQREGgweamcdwkDVLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:cd03218  91 -----TVEEnilavleIRGLSKKEREekLEELLEEFHITHLRKSKA---------SSLSGGERRRVEIARALATNPKFLL 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 7262393  628 LDECTSAVS----IDVEgKIFQAAKDAGI----------ALLSITHR 660
Cdd:cd03218 157 LDEPFAGVDpiavQDIQ-KIIKILKDRGIgvlitdhnvrETLSITDR 202
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
485-669 1.90e-09

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: 58.50  E-value: 1.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  485 SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLF-RILGGLWPTYGGVLY--KPPPQRMF------------YIPQRPYMS 549
Cdd:cd03290  12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWsnKNESEPSFeatrsrnrysvaYAAQKPWLL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  550 VGSLRDQVIYPDSVEDMQRKGYSEQ-DLEAILDVvhLHHILQREGGWEAMCdwkdvLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03290  92 NATVEENITFGSPFNKQRYKAVTDAcSLQPDIDL--LPFGDQTEIGERGIN-----LSGGQRQRICVARALYQNTNIVFL 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 7262393  629 DECTSAVSIDVEGKIFQAA-----KDAGIALLSITHRpslWKYHTH 669
Cdd:cd03290 165 DDPFSALDIHLSDHLMQEGilkflQDDKRTLVLVTHK---LQYLPH 207
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
505-632 3.03e-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: 60.33  E-value: 3.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    505 ITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPY------------MSVGSLRDQV--------IYPDSVE 564
Cdd:TIGR03719  36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQldptktvrenveEGVAEIKDALdrfneisaKYAEPDA 115
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7262393    565 DMQRKGYSEQDLEAILDVVHLHHILQR-EGGWEAM-C---DWK-DVLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:TIGR03719 116 DFDKLAAEQAELQEIIDAADAWDLDSQlEIAMDALrCppwDADvTKLSGGERRRVALCRLLLSKPDMLLLDEPT 189
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
486-661 4.67e-09

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: 56.98  E-value: 4.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKP---------PPQRMFYIPQRPYMSvGSLrd 555
Cdd:TIGR01189  12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLrPDSGEVRWNGtplaeqrdePHENILYLGHLPGLK-PEL-- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    556 qviypdSVEDMQR-----KGYSEQDLEAILDVVHLHHILQREGGWeamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:TIGR01189  89 ------SALENLHfwaaiHGGAQRTIEDALAAVGLTGFEDLPAAQ---------LSAGQQRRLALARLWLSRRPLWILDE 153
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 7262393    631 CTsaVSIDVEG-KIFQAAKDA-----GIALLSiTHRP 661
Cdd:TIGR01189 154 PT--TALDKAGvALLAGLLRAhlargGIVLLT-THQD 187
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
497-659 7.73e-09

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 57.33  E-value: 7.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   497 VEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLykpppqRMFYIPQRPyMSVGSLRDQV--IY--PD------SVED- 565
Cdd:PRK13635  30 VYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI------TVGGMVLSE-ETVWDVRRQVgmVFqnPDnqfvgaTVQDd 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   566 ----MQRKGYSEQDL----EAILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVS- 636
Cdd:PRK13635 103 vafgLENIGVPREEMvervDQALRQVGMEDFLNRE---------PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDp 173
                        170       180
                 ....*....|....*....|....*.
gi 7262393   637 ---IDVEGKIFQAAKDAGIALLSITH 659
Cdd:PRK13635 174 rgrREVLETVRQLKEQKGITVLSITH 199
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
486-659 1.18e-08

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 56.44  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGV------------LYKPPPQRMFYIPQRP------- 546
Cdd:PRK10895  15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddedisllpLHARARRGIGYLPQEAsifrrls 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   547 ----YMSVGSLRDqviypdSVEDMQRKGYSEQDLEAIldvvHLHHILQREGgweamcdwkDVLSGGEKQRIGMARMFYHR 622
Cdd:PRK10895  95 vydnLMAVLQIRD------DLSAEQREDRANELMEEF----HIEHLRDSMG---------QSLSGGERRRVEIARALAAN 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 7262393   623 PKYALLDECTSAVS----IDVEgKIFQAAKDAGIALLSITH 659
Cdd:PRK10895 156 PKFILLDEPFAGVDpisvIDIK-RIIEHLRDSGLGVLITDH 195
cbiO PRK13650
energy-coupling factor transporter ATPase;
497-659 1.38e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 56.66  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   497 VEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY----KPPPQRMFYIPQRPYMSVGSLRDQVIYPdSVED-----MQ 567
Cdd:PRK13650  30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIidgdLLTEENVWDIRHKIGMVFQNPDNQFVGA-TVEDdvafgLE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   568 RKGYSEQDLeaildVVHLHHILQREGgweaMCDWKDV----LSGGEKQRIGMARMFYHRPKYALLDECTSAvsIDVEGK- 642
Cdd:PRK13650 109 NKGIPHEEM-----KERVNEALELVG----MQDFKEReparLSGGQKQRVAIAGAVAMRPKIIILDEATSM--LDPEGRl 177
                        170       180
                 ....*....|....*....|..
gi 7262393   643 -----IFQAAKDAGIALLSITH 659
Cdd:PRK13650 178 eliktIKGIRDDYQMTVISITH 199
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
505-662 1.81e-08

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: 57.04  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    505 ITGPNGCGKSSLFRILGGLWPTYGGVLY--------------KPPPQRMF-YIPQR----PYMSVgslRDQVIYPDSVED 565
Cdd:TIGR02142  28 IFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtlfdsrkgifLPPEKRRIgYVFQEarlfPHLSV---RGNLRYGMKRAR 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    566 MQRKGYSEqdlEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIF- 644
Cdd:TIGR02142 105 PSERRISF---ERVIELLGIGHLLGRLPG---------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILp 172
                         170       180
                  ....*....|....*....|.
gi 7262393    645 ---QAAKDAGIALLSITHRPS 662
Cdd:TIGR02142 173 yleRLHAEFGIPILYVSHSLQ 193
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
474-659 1.92e-08

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: 53.61  E-value: 1.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  474 IICENIPIvTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQrpymsvgsl 553
Cdd:cd03221   1 IELENLSK-TYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  554 rdqviypdsvedmqrkgyseqdleaildvvhlhhilqreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:cd03221  71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
                       170       180
                ....*....|....*....|....*...
gi 7262393  634 avSIDVEGKIF--QAAKDAGIALLSITH 659
Cdd:cd03221 100 --HLDLESIEAleEALKEYPGTVILVSH 125
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
488-659 2.04e-08

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: 55.82  E-value: 2.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  488 VVVASLNIRVEEG-MHLLItGPNGCGKSSLFRILGGLW-PTYGGVLYK-------PPPQ-------RMFYIPQ-RPYMSV 550
Cdd:COG0411  18 VAVDDVSLEVERGeIVGLI-GPNGAGKTTLFNLITGFYrPTSGRILFDgrditglPPHRiarlgiaRTFQNPRlFPELTV 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  551 -------GSLRDQVIYPDSVEDMQRKGYSEQDL----EAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMF 619
Cdd:COG0411  97 lenvlvaAHARLGRGLLAALLRLPRARREEREAreraEELLERVGLADRADEPAG---------NLSYGQQRRLEIARAL 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 7262393  620 YHRPKYALLDECTSAVSI----DVEGKIFQAAKDAGIALLSITH 659
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPeeteELAELIRRLRDERGITILLIEH 211
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
474-669 2.16e-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: 55.11  E-value: 2.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKPPPQRMFYIPQRPYM--SV 550
Cdd:cd03292   1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKlIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrKI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  551 GS-------LRDQVIYPDSVEDMQRKGYSEQDLE----AILDVV---HLHHILQREggweamcdwkdvLSGGEKQRIGMA 616
Cdd:cd03292  81 GVvfqdfrlLPDRNVYENVAFALEVTGVPPREIRkrvpAALELVglsHKHRALPAE------------LSGGEQQRVAIA 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7262393  617 RMFYHRPKYALLDECTSAVSIDVEGKI---FQAAKDAGIALLSITHRPSLWKYHTH 669
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEImnlLKKINKAGTTVVVATHAKELVDTTRH 204
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
474-663 2.22e-08

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: 55.65  E-value: 2.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPqrmfyIPQRPYMSVGS 552
Cdd:cd03256   1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVePTSGSVLIDGTD-----INKLKGKALRQ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  553 LRDQV---------IYPDSVedMQ----------------RKGYSEQDLE---AILDVVHL-HHILQReggweamcdwKD 603
Cdd:cd03256  76 LRRQIgmifqqfnlIERLSV--LEnvlsgrlgrrstwrslFGLFPKEEKQralAALERVGLlDKAYQR----------AD 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7262393  604 VLSGGEKQRIGMARMFYHRPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLHQVDL 207
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
488-642 2.29e-08

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: 55.20  E-value: 2.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY---------KPPPQRMFYIPQrpymsvgslrDQV 557
Cdd:cd03263  16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELrPTSGTAYIngysirtdrKAARQSLGYCPQ----------FDA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  558 IYPD-SVEDMQR-----KGYSEQdlEAILDVVHLHHILQREggweamcDWKDV----LSGGEKQRIGMARMFYHRPKYAL 627
Cdd:cd03263  86 LFDElTVREHLRfyarlKGLPKS--EIKEEVELLLRVLGLT-------DKANKrartLSGGMKRKLSLAIALIGGPSVLL 156
                       170
                ....*....|....*
gi 7262393  628 LDECTSavSIDVEGK 642
Cdd:cd03263 157 LDEPTS--GLDPASR 169
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
484-659 2.70e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 55.85  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLYKPPP------------QRMFYIPQRPymsv 550
Cdd:PRK13639  12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPTSGEVLIKGEPikydkksllevrKTVGIVFQNP---- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   551 gslRDQVIYPDSVEDMQ----RKGYSEQDLEAildvvHLHHILQREGgweaMCDWKDV----LSGGEKQRIGMARMFYHR 622
Cdd:PRK13639  88 ---DDQLFAPTVEEDVAfgplNLGLSKEEVEK-----RVKEALKAVG----MEGFENKpphhLSGGQKKRVAIAGILAMK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 7262393   623 PKYALLDECTSAVSIDVEGKIFQAAKD---AGIALLSITH 659
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDlnkEGITIIISTH 195
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
488-676 4.34e-08

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 54.99  E-value: 4.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSLRDQVIYPDSV---E 564
Cdd:PRK10253  21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDItvqE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   565 DMQRKGYSEQDLEAIL---DVVHLHHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAV----SI 637
Cdd:PRK10253 101 LVARGRYPHQPLFTRWrkeDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLdishQI 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 7262393   638 DVEGKIFQAAKDAGIALLSITHR-PSLWKYHTHLLQF-DGE 676
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALrEGK 221
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
488-659 4.77e-08

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 55.50  E-value: 4.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMFYIPQR------------PYMSVGslr 554
Cdd:PRK11432  20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEkPTEGQIFIDGEDVTHRSIQQRdicmvfqsyalfPHMSLG--- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   555 DQVIYPdsvEDMQRKGYSE--QDLEAILDVVHLhhilqreGGWEAMcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:PRK11432  97 ENVGYG---LKMLGVPKEErkQRVKEALELVDL-------AGFEDR--YVDQISGGQQQRVALARALILKPKVLLFDEPL 164
                        170       180       190
                 ....*....|....*....|....*....|.
gi 7262393   633 SAVSIDV----EGKIFQAAKDAGIALLSITH 659
Cdd:PRK11432 165 SNLDANLrrsmREKIRELQQQFNITSLYVTH 195
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
493-659 5.24e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 55.00  E-value: 5.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYG-----GVLYKpppqrmfyipqrpYMSVGSLRDQV--IY--PD- 561
Cdd:PRK13632  28 VSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQSGeikidGITIS-------------KENLKEIRKKIgiIFqnPDn 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   562 -----SVED-----MQRKGYSEQDLEAILD----VVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:PRK13632  95 qfigaTVEDdiafgLENKKVPPKKMKDIIDdlakKVGMEDYLDKE---------PQNLSGGQKQRVAIASVLALNPEIII 165
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 7262393   628 LDECTSAvsIDVEGK------IFQAAKDAGIALLSITH 659
Cdd:PRK13632 166 FDESTSM--LDPKGKreikkiMVDLRKTRKKTLISITH 201
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
481-634 7.15e-08

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 54.57  E-value: 7.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  481 IVTPSGEVV-VASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP--------------QRMFYIPQ 544
Cdd:cd03294  30 ILKKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIePTSGKVLIDGQDiaamsrkelrelrrKKISMVFQ 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  545 R----PYMSVgslRDQVIYPDSVEDMQRKGYSEQDLEAiLDVVHLhhilqreGGWEAmcDWKDVLSGGEKQRIGMARMFY 620
Cdd:cd03294 110 SfallPHRTV---LENVAFGLEVQGVPRAEREERAAEA-LELVGL-------EGWEH--KYPDELSGGMQQRVGLARALA 176
                       170
                ....*....|....
gi 7262393  621 HRPKYALLDECTSA 634
Cdd:cd03294 177 VDPDILLMDEAFSA 190
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
487-661 7.72e-08

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 54.28  E-value: 7.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   487 EVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTY-------GGVLY-------------KPPPQRMFYIPQR- 545
Cdd:PRK14246  23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYdskikvdGKVLYfgkdifqidaiklRKEVGMVFQQPNPf 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   546 PYMSVgslRDQVIYPDSVEDMQRKgyseQDLEAILDvvhlhHILQREGGWEAMCDWKDV----LSGGEKQRIGMARMFYH 621
Cdd:PRK14246 103 PHLSI---YDNIAYPLKSHGIKEK----REIKKIVE-----ECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALAL 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 7262393   622 RPKYALLDECTSAVSI----DVEGKIFQAAKDAGIALLSitHRP 661
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIvnsqAIEKLITELKNEIAIVIVS--HNP 212
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
489-735 8.42e-08

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 54.04  E-value: 8.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMFYIPQRPYMSvgslRD-QVIYPDS---- 562
Cdd:TIGR02769  26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEkPAQGTVSFRGQDLYQLDRKQRRAFR----RDvQLVFQDSpsav 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    563 -------------VEDMQRKGYSEQD--LEAILDVVHLHHilqreggwEAMCDWKDVLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:TIGR02769 102 nprmtvrqiigepLRHLTSLDESEQKarIAELLDMVGLRS--------EDADKLPRQLSGGQLQRINIARALAVKPKLIV 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    628 LDECTSAVSIDVEGKIFQAAKD----AGIALLSITHRPSLWKYHthllqfdgeggwkfekldsAARLSLTEEKQRLEQQL 703
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKlqqaFGTAYLFITHDLRLVQSF-------------------CQRVAVMDKGQIVEECD 234
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 7262393    704 AGipkmqrrlQELC------QILGEAVAPAH-VPAPSPQ 735
Cdd:TIGR02769 235 VA--------QLLSfkhpagRNLQSAVLPEHpVRRSITT 265
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
492-630 9.81e-08

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: 53.50  E-value: 9.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  492 SLNIRVEEGMHLLitGPNGCGKSSLFRILGGL-WPTYGGVLY-------KPPPQRMF-YIPQR----PYMSVgslRDQVI 558
Cdd:cd03296  22 SLDIPSGELVALL--GPSGSGKTTLLRLIAGLeRPDSGTILFggedatdVPVQERNVgFVFQHyalfRHMTV---FDNVA 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  559 Y----------PDSVEdMQRKgyseqdLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03296  97 FglrvkprserPPEAE-IRAK------VHELLKLVQLDWLADR---------YPAQLSGGQRQRVALARALAVEPKVLLL 160

                ..
gi 7262393  629 DE 630
Cdd:cd03296 161 DE 162
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
483-659 3.16e-07

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: 51.81  E-value: 3.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  483 TPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLY-------------KPPPQRMFYIPQR-PY 547
Cdd:cd03258  14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPTSGSVLVdgtdltllsgkelRKARRRIGMIFQHfNL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  548 MSVGSLRDQVIYPDSVEDMQRKgYSEQDLEAILDVVHLHHilqREGGWEAMcdwkdvLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:cd03258  94 LSSRTVFENVALPLEIAGVPKA-EIEERVLELLELVGLED---KADAYPAQ------LSGGQKQRVGIARALANNPKVLL 163
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 7262393  628 LDECTSAVSIDVEGKIFQAAKDA----GIALLSITH 659
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDInrelGLTIVLITH 199
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
493-661 3.59e-07

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 51.34  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLYKPPP---------QRMFYIPQRPymsvGslrdqvIYPD- 561
Cdd:PRK13538  20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGeVLWQGEPirrqrdeyhQDLLYLGHQP----G------IKTEl 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   562 -SVEDMQ-----RKGYSEQDLEAILDVVHLHhilqregGWEamcdwkDV----LSGGEKQRIGMARMFYHRPKYALLDEC 631
Cdd:PRK13538  90 tALENLRfyqrlHGPGDDEALWEALAQVGLA-------GFE------DVpvrqLSAGQQRRVALARLWLTRAPLWILDEP 156
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 7262393   632 TSAvsIDVEG-KIFQA-----AKDAGIALLSiTHRP 661
Cdd:PRK13538 157 FTA--IDKQGvARLEAllaqhAEQGGMVILT-THQD 189
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
493-659 3.90e-07

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 52.05  E-value: 3.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGV----LYKPPPQRMFYIPQRpymsVGslrdqVIY--PD---- 561
Cdd:TIGR04520  21 VSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLlPTSGKVtvdgLDTLDEENLWEIRKK----VG-----MVFqnPDnqfv 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    562 --SVED-----MQRKGYSEQDLEAI----LDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:TIGR04520  92 gaTVEDdvafgLENLGVPREEMRKRvdeaLKLVGMEDFRDRE---------PHLLSGGQKQRVAIAGVLAMRPDIIILDE 162
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 7262393    631 CTSAvsIDVEGK------IFQAAKDAGIALLSITH 659
Cdd:TIGR04520 163 ATSM--LDPKGRkevletIRKLNKEEGITVISITH 195
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
488-659 4.00e-07

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 51.63  E-value: 4.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY------KPPPQRMFYIPQR-----------PYMSv 550
Cdd:PRK09493  15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdglkvNDPKVDERLIRQEagmvfqqfylfPHLT- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   551 gSLRDQVIYPDSVEDMQRKGYSEQDLEaildvvhlhhILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:PRK09493  94 -ALENVMFGPLRVRGASKEEAEKQARE----------LLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
                        170       180       190
                 ....*....|....*....|....*....|....
gi 7262393   631 CTSAvsIDVE-----GKIFQAAKDAGIALLSITH 659
Cdd:PRK09493 163 PTSA--LDPElrhevLKVMQDLAEEGMTMVIVTH 194
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
493-662 4.20e-07

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 53.29  E-value: 4.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLykpppqrmfyIPQRPYMSV--GSLR--------DQVIYPD 561
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYdVTSGRIL----------IDGQDIRDVtqASLRaaigivpqDTVLFND 446
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  562 SVED---MQRKGYSEQDLEAILDVVHLHH-ILQREGGWEAMcdwkdV------LSGGEKQRIGMARMFYHRPKYALLDEC 631
Cdd:COG5265 447 TIAYniaYGRPDASEEEVEAAARAAQIHDfIESLPDGYDTR-----VgerglkLSGGEKQRVAIARTLLKNPPILIFDEA 521
                       170       180       190
                ....*....|....*....|....*....|...
gi 7262393  632 TSAVSIDVEGKIFQAAKDA--GIALLSITHRPS 662
Cdd:COG5265 522 TSALDSRTERAIQAALREVarGRTTLVIAHRLS 554
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
461-671 4.71e-07

FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273907 [Multi-domain]  Cd Length: 243  Bit Score: 51.49  E-value: 4.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    461 LKIRGQVVDVEQGIICENIPIVTPSGEVVVaslnirveegmhllITGPNGCGKSSLFRILGGlWPTY----GGVLYK--- 533
Cdd:TIGR01978   1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHA--------------IMGPNGSGKSTLSKTIAG-HPSYevtsGTILFKgqd 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    534 ----PPPQR----MFYIPQRPYMSVGSlrdqviypdSVEDMQRKGY---SEQDLEAILDVVHLHHILQRE----GGWEAM 598
Cdd:TIGR01978  66 llelEPDERaragLFLAFQYPEEIPGV---------SNLEFLRSALnarRSARGEEPLDLLDFEKLLKEKlallDMDEEF 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    599 CDwKDV---LSGGEKQRIGMARMFYHRPKYALLDECTSAVSID-----VEGkiFQAAKDAGIALLSITHRPSLWKY---- 666
Cdd:TIGR01978 137 LN-RSVnegFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDalkivAEG--INRLREPDRSFLIITHYQRLLNYikpd 213

                  ....*
gi 7262393    667 HTHLL 671
Cdd:TIGR01978 214 YVHVL 218
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
507-632 5.36e-07

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 52.81  E-value: 5.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   507 GPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPY------------MSVGSLRDQV--------IYPDSVEDM 566
Cdd:PRK11819  40 GLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQldpektvrenveEGVAEVKAALdrfneiyaAYAEPDADF 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   567 QrKGYSEQ-DLEAILDvvhlhhilqREGGWE-------AM----C---DWK-DVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:PRK11819 120 D-ALAAEQgELQEIID---------AADAWDldsqleiAMdalrCppwDAKvTKLSGGERRRVALCRLLLEKPDMLLLDE 189

                 ..
gi 7262393   631 CT 632
Cdd:PRK11819 190 PT 191
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
489-659 6.34e-07

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 50.97  E-value: 6.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYKPPPqrmfyIPQRPYMSVGSLRDQ---VIY----- 559
Cdd:PRK11629  24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQP-----MSKLSSAAKAELRNQklgFIYqfhhl 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   560 -PD--SVED---------MQRKGYSEQDLEaILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:PRK11629  99 lPDftALENvamplligkKKPAEINSRALE-MLAAVGLEHRANHR---------PSELSGGERQRVAIARALVNNPRLVL 168
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 7262393   628 LDECTSAVSIDVEGKIFQAAKD----AGIALLSITH 659
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGElnrlQGTAFLVVTH 204
PLN03232 PLN03232
ABC transporter C family member; Provisional
460-646 1.04e-06

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 52.29  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    460 PLKIRGQVVDVEQGIICENIPIVTPSgevvVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTY-GGVLYKpppQ 537
Cdd:PLN03232  607 PLQPGAPAISIKNGYFSWDSKTSKPT----LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAEtSSVVIR---G 679
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    538 RMFYIPQRPYMSVGSLRDQVIYPDSVEdmqrkgySEQDLEAIlDVVHLHHILQREGGWeamcDWKDV------LSGGEKQ 611
Cdd:PLN03232  680 SVAYVPQVSWIFNATVRENILFGSDFE-------SERYWRAI-DVTALQHDLDLLPGR----DLTEIgergvnISGGQKQ 747
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 7262393    612 RIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQA 646
Cdd:PLN03232  748 RVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDS 782
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
240-662 1.10e-06

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: 52.03  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    240 TAWPSAIAGLVVF-LTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVElallQRSYqDLASQIN 318
Cdd:TIGR02203 152 YSWQLTLIVVVMLpVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYE----TRRF-DAVSNRN 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    319 LillerlwyvmleQFLMKYVwSASGLLMVAVPIITATGYSesdaeAVKKAALEkkeeELVSERTEAFTIArNLLTAAAda 398
Cdd:TIGR02203 227 R------------RLAMKMT-SAGSISSPITQLIASLALA-----VVLFIALF----QAQAGSLTAGDFT-AFITAMI-- 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    399 ieRIMSSYKEVTELAGytaRVHEMFQVFEDVqrchFKRPRELEDAQAGSGTIGRsgvrVEGPLKIRGqvVDVEQGiicen 478
Cdd:TIGR02203 282 --ALIRPLKSLTNVNA---PMQRGLAAAESL----FTLLDSPPEKDTGTRAIER----ARGDVEFRN--VTFRYP----- 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    479 ipivtPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLykpppqrMFYIPQRPYmSVGSLRDQV 557
Cdd:TIGR02203 342 -----GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYePDSGQIL-------LDGHDLADY-TLASLRRQV 408
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    558 --------IYPDSVED----MQRKGYSEQDLEAILDVVHLHHILQR--EGGWEAMCDWKDVLSGGEKQRIGMARMFYHRP 623
Cdd:TIGR02203 409 alvsqdvvLFNDTIANniayGRTEQADRAEIERALAAAYAQDFVDKlpLGLDTPIGENGVLLSGGQRQRLAIARALLKDA 488
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 7262393    624 KYALLDECTSAVSIDVEGKIfQAAKDA---GIALLSITHRPS 662
Cdd:TIGR02203 489 PILILDEATSALDNESERLV-QAALERlmqGRTTLVIAHRLS 529
cbiO PRK13640
energy-coupling factor transporter ATPase;
485-659 1.17e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 50.95  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   485 SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLwptyggVLYKPPPQRMFYIPQRPYMS--VGSLRDQV--IY- 559
Cdd:PRK13640  18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL------LLPDDNPNSKITVDGITLTAktVWDIREKVgiVFq 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   560 -PD------SVED-----MQRKGYSEQDLEAILdvvhlHHILQREGgweaMCDWKDV----LSGGEKQRIGMARMFYHRP 623
Cdd:PRK13640  92 nPDnqfvgaTVGDdvafgLENRAVPRPEMIKIV-----RDVLADVG----MLDYIDSepanLSGGQKQRVAIAGILAVEP 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 7262393   624 KYALLDECTSAvsIDVEGK------IFQAAKDAGIALLSITH 659
Cdd:PRK13640 163 KIIILDESTSM--LDPAGKeqilklIRKLKKKNNLTVISITH 202
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
490-666 1.22e-06

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 51.25  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   490 VASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP-TYGGVLY----------------KPPPQRMFYIPQ---RPYMS 549
Cdd:PRK15079  37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKaTDGEVAWlgkdllgmkddewravRSDIQMIFQDPLaslNPRMT 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   550 VGS-----LRdqVIYPDsvedMQRKGYSEQDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPK 624
Cdd:PRK15079 117 IGEiiaepLR--TYHPK----LSRQEVKDRVKAMMLKVGLLPNLINR---------YPHEFSGGQCQRIGIARALILEPK 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 7262393   625 YALLDECTSAVSIDVEGKIF----QAAKDAGIALLSITHRPSLWKY 666
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVnllqQLQREMGLSLIFIAHDLAVVKH 227
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
486-634 1.72e-06

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 49.99  E-value: 1.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVaslnirveegmhllITGPNGCGKSSLFRILGGLWP------TYGGVLYKPPPQRMFYIPQR-----------PYM 548
Cdd:COG1126  27 GEVVV--------------IIGPSGSGKSTLLRCINLLEEpdsgtiTVDGEDLTDSKKDINKLRRKvgmvfqqfnlfPHL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  549 SVgslRDQVIYPDsvedMQRKGYSEQDLEAI----LDVVHLHhilqreggweamcDWKDV----LSGGEKQRIGMAR--- 617
Cdd:COG1126  93 TV---LENVTLAP----IKVKKMSKAEAEERamelLERVGLA-------------DKADAypaqLSGGQQQRVAIARala 152
                       170
                ....*....|....*..
gi 7262393  618 MfyhRPKYALLDECTSA 634
Cdd:COG1126 153 M---EPKVMLFDEPTSA 166
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
488-660 1.76e-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: 49.67  E-value: 1.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVL------YKPP---PQRMFYIPQR----PYMSVgsl 553
Cdd:cd03266  19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDAGFATvdgfdvVKEPaeaRRRLGFVSDStglyDRLTA--- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  554 RDQVIYPDSVEDMQRKGYsEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:cd03266  96 RENLEYFAGLYGLKGDEL-TARLEELADRLGMEELLDRRVG---------GFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
                       170       180       190
                ....*....|....*....|....*....|
gi 7262393  634 AVSIDVEGKIF---QAAKDAGIALLSITHR 660
Cdd:cd03266 166 GLDVMATRALRefiRQLRALGKCILFSTHI 195
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
482-643 2.82e-06

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 50.23  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   482 VTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKPPP----------QRMFYIPQRPYMSV 550
Cdd:PRK09536  11 VEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRaINGTLTPTAGTVLVAGDDvealsaraasRRVASVPQDTSLSF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   551 GSLRDQVIYPDSVEDMQRKGYSEQDLEAILDvvhlhHILQReGGWEAMCDWK-DVLSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:PRK09536  91 EFDVRQVVEMGRTPHRSRFDTWTETDRAAVE-----RAMER-TGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLD 164
                        170
                 ....*....|....
gi 7262393   630 ECTSavSIDVEGKI 643
Cdd:PRK09536 165 EPTA--SLDINHQV 176
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
484-674 2.84e-06

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 51.10  E-value: 2.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393     484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSS----LFRIL---------GGLwpTYGGVLYKPPPQRMFYIPQRPYMSV 550
Cdd:TIGR00957 1296 EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINesaegeiiiDGL--NIAKIGLHDLRFKITIIPQDPVLFS 1373
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393     551 GSLRDQvIYPDSvedmqrkGYSEQDLEAILDVVHLHHILQRE-GGWEAMC-DWKDVLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:TIGR00957 1374 GSLRMN-LDPFS-------QYSDEEVWWALELAHLKTFVSALpDKLDHECaEGGENLSVGQRQLVCLARALLRKTKILVL 1445
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 7262393     629 DECTSAVSIDVEGKIFQAAKDA--GIALLSITHRPSLWKYHTHLLQFD 674
Cdd:TIGR00957 1446 DEATAAVDLETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVLD 1493
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
500-659 3.05e-06

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 50.62  E-value: 3.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   500 GMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPpQRMFYIPQRPYMSVgsLRD-QVIYPD---SVEDMQRKGYSeqd 575
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG-QRIDTLSPGKLQAL--RRDiQFIFQDpyaSLDPRQTVGDS--- 423
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   576 leaILDVVHLHHILQREGG-----W---------EAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEG 641
Cdd:PRK10261 424 ---IMEPLRVHGLLPGKAAaarvaWllervgllpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
                        170       180
                 ....*....|....*....|..
gi 7262393   642 KI----FQAAKDAGIALLSITH 659
Cdd:PRK10261 501 QIinllLDLQRDFGIAYLFISH 522
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
483-659 3.51e-06

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 49.72  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   483 TPSGEVV-VASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGV------------------LYKPPPQRMFYIP 543
Cdd:PRK09473  24 TPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIggsatfngreilnlpekeLNKLRAEQISMIF 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   544 Q------RPYMSVGSLRDQVIypdsvedMQRKGYSEQD--LEAI--LDVVHLHHILQReggweaMCDWKDVLSGGEKQRI 613
Cdd:PRK09473 104 QdpmtslNPYMRVGEQLMEVL-------MLHKGMSKAEafEESVrmLDAVKMPEARKR------MKMYPHEFSGGMRQRV 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 7262393   614 GMARMFYHRPKYALLDECTSAVSIDVEGKIF----QAAKDAGIALLSITH 659
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMtllnELKREFNTAIIMITH 220
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
507-630 3.78e-06

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: 49.71  E-value: 3.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  507 GPNGCGKSSLFRILGGLWPTYGG-------VLYK-------PPPQRMF-YIPQ--R--PYMSV-GSLRdqviYPdsvedM 566
Cdd:COG4148  32 GPSGSGKTTLLRAIAGLERPDSGrirlggeVLQDsargiflPPHRRRIgYVFQeaRlfPHLSVrGNLL----YG-----R 102
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7262393  567 QR--KGYSEQDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:COG4148 103 KRapRAERRISFDEVVELLGIGHLLDR---------RPATLSGGERQRVAIGRALLSSPRLLLMDE 159
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
493-630 4.36e-06

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


Pssm-ID: 440179 [Multi-domain]  Cd Length: 236  Bit Score: 48.44  E-value: 4.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLYK-------PPPQR----MFYIPQRpymsvgslRDqvIYP 560
Cdd:COG0410  22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsIRFDgeditglPPHRIarlgIGYVPEG--------RR--IFP 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  561 D-SVED------MQRKGYSE--QDLEAILDVV-HLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:COG0410  92 SlTVEEnlllgaYARRDRAEvrADLERVYELFpRLKERRRQRAG---------TLSGGEQQMLAIGRALMSRPKLLLLDE 162
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
507-643 4.99e-06

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 48.62  E-value: 4.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   507 GPNGCGKSSLFRIL---GGLWP---TYGGVLYKpppQRMFYIPQRPYMSvgsLRDQV-------------IYPDSVEDMQ 567
Cdd:PRK14239  38 GPSGSGKSTLLRSInrmNDLNPevtITGSIVYN---GHNIYSPRTDTVD---LRKEIgmvfqqpnpfpmsIYENVVYGLR 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   568 RKGYSEQdleAILDVVhLHHILQREGGWEAMcdwKDVL-------SGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVE 640
Cdd:PRK14239 112 LKGIKDK---QVLDEA-VEKSLKGASIWDEV---KDRLhdsalglSGGQQQRVCIARVLATSPKIILLDEPTSALDPISA 184

                 ...
gi 7262393   641 GKI 643
Cdd:PRK14239 185 GKI 187
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
493-662 5.30e-06

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: 47.87  E-value: 5.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  493 LNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLYK------PPPQRmfyipqRPYMSVgsLRDQVIYPD-SVE 564
Cdd:cd03298  17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINgvdvtaAPPAD------RPVSML--FQENNLFAHlTVE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  565 DMQRKGYS------EQDLEAIldvvhlHHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID 638
Cdd:cd03298  89 QNVGLGLSpglkltAEDRQAI------EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
                       170       180
                ....*....|....*....|....*...
gi 7262393  639 VEGKIFQAAKDA----GIALLSITHRPS 662
Cdd:cd03298 163 LRAEMLDLVLDLhaetKMTVLMVTHQPE 190
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
486-634 5.36e-06

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 48.61  E-value: 5.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLY--KP----PPQRMFYI----PQRPYMSvgslr 554
Cdd:PRK13548  14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEVRLngRPladwSPAELARRravlPQHSSLS----- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   555 dqviYPDSVED---MQRKGYSEQDLE---------AILDVVHLHHILQREggweamcdwkdvLSGGEKQRIGMARMF--- 619
Cdd:PRK13548  89 ----FPFTVEEvvaMGRAPHGLSRAEddalvaaalAQVDLAHLAGRDYPQ------------LSGGEQQRVQLARVLaql 152
                        170
                 ....*....|....*...
gi 7262393   620 ---YHRPKYALLDECTSA 634
Cdd:PRK13548 153 wepDGPPRWLLLDEPTSA 170
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
505-635 5.65e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 48.85  E-value: 5.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   505 ITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP------------QRMFYIPQRPymsvgslRDQVIYPDSVED----MQ 567
Cdd:PRK13638  32 LVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKPldyskrgllalrQQVATVFQDP-------EQQIFYTDIDSDiafsLR 104
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7262393   568 RKGYSEQDL----EAILDVVHLHHILQReggwEAMCdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAV 635
Cdd:PRK13638 105 NLGVPEAEItrrvDEALTLVDAQHFRHQ----PIQC-----LSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
488-660 7.05e-06

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 48.57  E-value: 7.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  488 VVVASLNIRVEEG--MHLLitGPNGCGKSSLFR-ILGGLWPTYGGVLYK-----PPPQRMF-YIPQ----RPYMSVGslr 554
Cdd:COG4152  15 TAVDDVSFTVPKGeiFGLL--GPNGAGKTTTIRiILGILAPDSGEVLWDgepldPEDRRRIgYLPEerglYPKMKVG--- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  555 DQVIYpdsvedM-QRKGYSEQDLEAILDvvhlhHILQREGgweaMCDWKDV----LSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:COG4152  90 EQLVY------LaRLKGLSKAEAKRRAD-----EWLERLG----LGDRANKkveeLSKGNQQKVQLIAALLHDPELLILD 154
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 7262393  630 ECTS---AVSIDV-EGKIF-QAAKDAGIaLLSiTHR 660
Cdd:COG4152 155 EPFSgldPVNVELlKDVIReLAAKGTTV-IFS-SHQ 188
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
486-661 9.45e-06

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 49.03  E-value: 9.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL---WPTYGGVLYK----------PPPQRM------------- 539
Cdd:TIGR03269  12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyEPTSGRIIYHvalcekcgyvERPSKVgepcpvcggtlep 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    540 ----FYIPQRPYMSVGSLR-------------DQVIYPDSVEDMQRKGYSEQD-----LEaILDVVHLHHI---LQREgg 594
Cdd:TIGR03269  92 eevdFWNLSDKLRRRIRKRiaimlqrtfalygDDTVLDNVLEALEEIGYEGKEavgraVD-LIEMVQLSHRithIARD-- 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7262393    595 weamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSavSID------VEGKIFQAAKDAGIALLSITHRP 661
Cdd:TIGR03269 169 ----------LSGGEKQRVVLARQLAKEPFLFLADEPTG--TLDpqtaklVHNALEEAVKASGISMVLTSHWP 229
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
489-659 1.91e-05

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 47.78  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   489 VVASLNIRVEEGMHLLITGPNGCGKS----SLFRIL--------GGLWPTYGGVLYKPPPQ--------RMFYIPQRPYM 548
Cdd:PRK15134  24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypSGDIRFHGESLLHASEQtlrgvrgnKIAMIFQEPMV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   549 SVG---SLRDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQReggweaMCDWKDVLSGGEKQRIGMARMFYHRPKY 625
Cdd:PRK15134 104 SLNplhTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKR------LTDYPHQLSGGERQRVMIAMALLTRPEL 177
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 7262393   626 ALLDECTSAVSIDVEGKIFQAAKD----AGIALLSITH 659
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRElqqeLNMGLLFITH 215
cbiO PRK13643
energy-coupling factor transporter ATPase;
483-659 2.18e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 47.04  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   483 TPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY--------------KPPPQRMFYIPQRPY 547
Cdd:PRK13643  15 SPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVgdivvsstskqkeiKPVRKKVGVVFQFPE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   548 msvGSLRDQVIYPDSVEDMQRKGYSEQDLEAI----LDVVHLHHILQREGGWEamcdwkdvLSGGEKQRIGMARMFYHRP 623
Cdd:PRK13643  95 ---SQLFEETVLKDVAFGPQNFGIPKEKAEKIaaekLEMVGLADEFWEKSPFE--------LSGGQMRRVAIAGILAMEP 163
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 7262393   624 KYALLDECTSAVSIDVE---GKIFQAAKDAGIALLSITH 659
Cdd:PRK13643 164 EVLVLDEPTAGLDPKARiemMQLFESIHQSGQTVVLVTH 202
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
488-659 2.33e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 47.00  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK----PPPQRMFYIPQRPYMSVGSLRDQVIYPDS 562
Cdd:PRK13633  24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPSEGKVYVDgldtSDEENLWDIRNKAGMVFQNPDNQIVATIV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   563 VEDM----QRKGYSEQDLEAILDvvhlhHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVS-- 636
Cdd:PRK13633 104 EEDVafgpENLGIPPEEIRERVD-----ESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDps 178
                        170       180
                 ....*....|....*....|....*
gi 7262393   637 --IDVEGKIFQAAKDAGIALLSITH 659
Cdd:PRK13633 179 grREVVNTIKELNKKYGITIILITH 203
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
505-665 2.35e-05

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 46.02  E-value: 2.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   505 ITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMFyipQRPYMS-VG---SLRDQVIYPDSVEDMQRKGYSEQDLEAI 579
Cdd:PRK13541  31 IKGANGCGKSSLLRMIAGIMqPSSGNIYYKNCNINNI---AKPYCTyIGhnlGLKLEMTVFENLKFWSEIYNSAETLYAA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   580 LDVVHLHHILQREggweamCdwkDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID----VEGKIFQAAKDAGIALL 655
Cdd:PRK13541 108 IHYFKLHDLLDEK------C---YSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEnrdlLNNLIVMKANSGGIVLL 178
                        170
                 ....*....|
gi 7262393   656 SiTHRPSLWK 665
Cdd:PRK13541 179 S-SHLESSIK 187
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
486-630 2.66e-05

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 47.37  E-value: 2.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRpymsvgslRDQVIYPDSVED 565
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQH--------QEELDPDKTVLD 398
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  566 -MQRkgYSEQDLEaildvVHLHHILQREG--GWEAmcdWK--DVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:COG0488 399 eLRD--GAPGGTE-----QEVRGYLGRFLfsGDDA---FKpvGVLSGGEKARLALAKLLLSPPNVLLLDE 458
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
483-659 3.09e-05

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: 46.58  E-value: 3.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  483 TPSGEV-VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP----TYGGVLYK-------PPPQ-------RMFYIP 543
Cdd:COG0444  13 TRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgiTSGEILFDgedllklSEKElrkirgrEIQMIF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  544 QRPY------MSVGslrDQVIYPdsvedMQR-KGYSEQDLEA----ILDVVHLHHILQR------EggweamcdwkdvLS 606
Cdd:COG0444  93 QDPMtslnpvMTVG---DQIAEP-----LRIhGGLSKAEAREraieLLERVGLPDPERRldryphE------------LS 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7262393  607 GGEKQRIGMARMFYHRPKYALLDECTSA--VSIdvegkifQA---------AKDAGIALLSITH 659
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTAldVTI-------QAqilnllkdlQRELGLAILFITH 209
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
486-633 3.30e-05

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


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 45.96  E-value: 3.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY-------------KPPPQRMFYIPQRPY---- 547
Cdd:cd03261  12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLrPDSGEVLIdgedisglseaelYRLRRRMGMLFQSGAlfds 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  548 MSVGslrDQVIYPDSvedmQRKGYSEQDLEAI----LDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRP 623
Cdd:cd03261  92 LTVF---ENVAFPLR----EHTRLSEEEIREIvlekLEAVGLRGAEDL---------YPAELSGGMKKRVALARALALDP 155
                       170
                ....*....|
gi 7262393  624 KYALLDECTS 633
Cdd:cd03261 156 ELLLYDEPTA 165
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
484-659 3.63e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 46.38  E-value: 3.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLYKPPP-----QRMFYIPQRPYMSVGSLRDQV 557
Cdd:PRK13636  16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGiLKPSSGRILFDGKPidysrKGLMKLRESVGMVFQDPDNQL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   558 IYPDSVEDMQrkgYSEQDLEAILDVVH--LHHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAv 635
Cdd:PRK13636  96 FSASVYQDVS---FGAVNLKLPEDEVRkrVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG- 171
                        170       180       190
                 ....*....|....*....|....*....|
gi 7262393   636 sIDVEGK------IFQAAKDAGIALLSITH 659
Cdd:PRK13636 172 -LDPMGVseimklLVEMQKELGLTIIIATH 200
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
507-659 4.31e-05

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 45.93  E-value: 4.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   507 GPNGCGKSSLFRILGGLW-PTYGGVLYKPPP----------QRMFYIPQR-PYMSVGSLRDQVI---YP-------DSVE 564
Cdd:PRK10575  44 GHNGSGKSTLLKMLGRHQpPSEGEILLDAQPleswsskafaRKVAYLPQQlPAAEGMTVRELVAigrYPwhgalgrFGAA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   565 DMQRkgyseqdLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSI----DVE 640
Cdd:PRK10575 124 DREK-------VEEAISLVGLKPLAHR---------LVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVL 187
                        170
                 ....*....|....*....
gi 7262393   641 GKIFQAAKDAGIALLSITH 659
Cdd:PRK10575 188 ALVHRLSQERGLTVIAVLH 206
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
605-660 4.33e-05

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 47.33  E-value: 4.33e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    605 LSGGEKQRIGMARMFYHRPKYALLDECTSAVSID----VEGKIFQAAKDAGIALLSITHR 660
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAHR 1418
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
471-659 7.02e-05

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 45.26  E-value: 7.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   471 EQGIICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG---VLYKPPPQRM-----FYI 542
Cdd:PRK15056   4 QAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGkisILGQPTRQALqknlvAYV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   543 PQrpymsvgSLRDQVIYPDSVED---MQRKGY----------SEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGE 609
Cdd:PRK15056  84 PQ-------SEEVDWSFPVLVEDvvmMGRYGHmgwlrrakkrDRQIVTAALARVDMVEFRHRQIG---------ELSGGQ 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 7262393   610 KQRIGMARMFYHRPKYALLDECTSAVSIDVEGKI---FQAAKDAGIALLSITH 659
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIislLRELRDEGKTMLVSTH 200
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
505-681 7.52e-05

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 46.08  E-value: 7.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    505 ITGPNGCGKSSLFRILGGLWPTYGGVLykpppqrmfyipqrpymSVGslrdqviypDSVedmqRKGYSEQDLEAI----- 579
Cdd:TIGR03719 353 VIGPNGAGKSTLFRMITGQEQPDSGTI-----------------EIG---------ETV----KLAYVDQSRDALdpnkt 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    580 --------LDVVHLhhilqreGGWE----AMCDW---------KDV--LSGGEKQRIGMARMFYHRPKYALLDECTSavS 636
Cdd:TIGR03719 403 vweeisggLDIIKL-------GKREipsrAYVGRfnfkgsdqqKKVgqLSGGERNRVHLAKTLKSGGNVLLLDEPTN--D 473
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 7262393    637 IDVEgkIFQAAKDA-----GIALLsITH-RPSLWKYHTHLLQFDGEGGWKF 681
Cdd:TIGR03719 474 LDVE--TLRALEEAllnfaGCAVV-ISHdRWFLDRIATHILAFEGDSHVEW 521
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
502-663 7.58e-05

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 43.52  E-value: 7.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393     502 HLLITGPNGCGKSSLFRILGGlwptyggvLYKPPPQRMFYIpqrpymsvgslrdqviypdsvedmqrkgyseqDLEAILD 581
Cdd:smart00382   4 VILIVGPPGSGKTTLARALAR--------ELGPPGGGVIYI--------------------------------DGEDILE 43
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393     582 VVHLHHILQREGGWEAMcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDAGIALLSITHRP 661
Cdd:smart00382  44 EVLDQLLLIIVGGKKAS------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNL 117

                   ..
gi 7262393     662 SL 663
Cdd:smart00382 118 TV 119
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
489-662 8.19e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 44.83  E-value: 8.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP------------TYGGVLYKPP--PQRM-------FYIPQR-P 546
Cdd:PRK14267  19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneearvegevrLFGRNIYSPDvdPIEVrrevgmvFQYPNPfP 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   547 YMSvgslrdqvIYPDSVEDMQRKGY--SEQDLEAILDVVhlhhiLQREGGWEA----MCDWKDVLSGGEKQRIGMARMFY 620
Cdd:PRK14267  99 HLT--------IYDNVAIGVKLNGLvkSKKELDERVEWA-----LKKAALWDEvkdrLNDYPSNLSGGQRQRLVIARALA 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 7262393   621 HRPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALlsITHRPS 662
Cdd:PRK14267 166 MKPKILLMDEPTANIdpvgTAKIEELLFELKKEYTIVL--VTHSPA 209
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
491-669 9.07e-05

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 45.06  E-value: 9.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   491 ASLNIRVEEGMHLLitGPNGCGKSSLFRILGGL-WPTYGGVLYKPPP--------QRMFyipQR--------------PY 547
Cdd:PRK10419  31 VSLSLKSGETVALL--GRSGCGKSTLARLLVGLeSPSQGNVSWRGEPlaklnraqRKAF---RRdiqmvfqdsisavnPR 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   548 MSVG-SLRDQVIYPDSVEDMQRKGYSEQDLEAI-LDVVHLHHILQReggweamcdwkdvLSGGEKQRIGMARMFYHRPKY 625
Cdd:PRK10419 106 KTVReIIREPLRHLLSLDKAERLARASEMLRAVdLDDSVLDKRPPQ-------------LSGGQLQRVCLARALAVEPKL 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 7262393   626 ALLDECTSAVSIDVEGKIFQAAKD----AGIALLSITHRPSLWKYHTH 669
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKlqqqFGTACLFITHDLRLVERFCQ 220
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
490-674 1.30e-04

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 45.34  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   490 VASLNIRVEEGMHLLITGPNGCGKSSLFRILgglwptyggvlykpppQRmFYIPQRPY----------MSVGSLRDQ--V 557
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLL----------------QR-VFDPQSGRilidgtdirtVTRASLRRNiaV 413
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   558 IYPD------SVEDMQRKGY---SEQDLEAILDVVHLHH-ILQREGGWEAMCDWK-DVLSGGEKQRIGMARMFYHRPKYA 626
Cdd:PRK13657 414 VFQDaglfnrSIEDNIRVGRpdaTDEEMRAAAERAQAHDfIERKPDGYDTVVGERgRQLSGGERQRLAIARALLKDPPIL 493
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 7262393   627 LLDECTSAVSIDVEGKIfQAAKDA---GIALLSITHRPSLWKYHTHLLQFD 674
Cdd:PRK13657 494 ILDEATSALDVETEAKV-KAALDElmkGRTTFIIAHRLSTVRNADRILVFD 543
PTZ00243 PTZ00243
ABC transporter; Provisional
443-645 1.35e-04

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 45.54  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    443 AQAGSGTI---GRSGVRVEGPLKIRG---------QVVDVEQGIICENIPIVTPSGEVVVaslnirveegmhllITGPNG 510
Cdd:PTZ00243  631 PSSASRHIvegGTGGGHEATPTSERSaktpkmktdDFFELEPKVLLRDVSVSVPRGKLTV--------------VLGATG 696
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    511 CGKSSLFRILGGLWPTYGGVLYKpppQRMF-YIPQRPYMSVGSLRDQVIYPDsvedmqrkgysEQDLEAILDVVHLHH-- 587
Cdd:PTZ00243  697 SGKSTLLQSLLSQFEISEGRVWA---ERSIaYVPQQAWIMNATVRGNILFFD-----------EEDAARLADAVRVSQle 762
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7262393    588 --ILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQ 645
Cdd:PTZ00243  763 adLAQLGGGLETEIGEKGVnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVE 823
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
605-705 1.57e-04

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 44.19  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   605 LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEG---KIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGgwKF 681
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG--KI 230
                         90       100
                 ....*....|....*....|....
gi 7262393   682 EKLDSAARLSLTEEKQRLEQQLAG 705
Cdd:PRK10619 231 EEEGAPEQLFGNPQSPRLQQFLKG 254
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
492-637 1.98e-04

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 44.34  E-value: 1.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  492 SLNIRveEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY-------------KPPPQRMFYIPQRPY------MSVG 551
Cdd:COG4608  38 SFDIR--RGETLGLVGESGCGKSTLGRLLLRLEePTSGEILFdgqditglsgrelRPLRRRMQMVFQDPYaslnprMTVG 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  552 slrDQVIYPDSVEDMQRKGYSEQDLEAILDVVHL--HHiLQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRPKYA 626
Cdd:COG4608 116 ---DIIAEPLRIHGLASKAERRERVAELLELVGLrpEH-ADRyphE------------FSGGQRQRIGIARALALNPKLI 179
                       170
                ....*....|...
gi 7262393  627 LLDECTSA--VSI 637
Cdd:COG4608 180 VCDEPVSAldVSI 192
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
486-663 2.20e-04

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 43.32  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYKPPPQRMFYIPQRPYmsvgsLRDQV--IYPDS 562
Cdd:PRK10908  14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIeRPSAGKIWFSGHDITRLKNREVPF-----LRRQIgmIFQDH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   563 VEDMQRKGYSEQDLEAILDVVHLHHI-------LQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECT--- 632
Cdd:PRK10908  89 HLLMDRTVYDNVAIPLIIAGASGDDIrrrvsaaLDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTgnl 168
                        170       180       190
                 ....*....|....*....|....*....|..
gi 7262393   633 -SAVSIDVEgKIFQAAKDAGIALLSITHRPSL 663
Cdd:PRK10908 169 dDALSEGIL-RLFEEFNRVGVTVLMATHDIGL 199
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
485-662 2.48e-04

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 44.32  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   485 SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGlwptyggvlYKPPPQRMFYIPQRPY--MSVGSLR-------- 554
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG---------YYPLTEGEIRLDGRPLssLSHSVLRqgvamvqq 422
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   555 DQVIYPDSVEDMQRKG--YSEQDLEAILDVVHLHHILQR--EGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:PRK10790 423 DPVVLADTFLANVTLGrdISEEQVWQALETVQLAELARSlpDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDE 502
                        170       180       190
                 ....*....|....*....|....*....|....
gi 7262393   631 CTSAVSIDVEGKIFQA--AKDAGIALLSITHRPS 662
Cdd:PRK10790 503 ATANIDSGTEQAIQQAlaAVREHTTLVVIAHRLS 536
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
492-630 2.60e-04

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 43.92  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   492 SLNIRVEEGMHLLitGPNGCGKSSLFRILGGLWPTYGGVL---------YKPPPQRMFYIPQR----PYMSVGslrDQVI 558
Cdd:PRK10851  22 SLDIPSGQMVALL--GPSGSGKTTLLRIIAGLEHQTSGHIrfhgtdvsrLHARDRKVGFVFQHyalfRHMTVF---DNIA 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7262393   559 YPDSV---EDMQRKGYSEQDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:PRK10851  97 FGLTVlprRERPNAAAIKAKVTQLLEMVQLAHLADR---------YPAQLSGGQKQRVALARALAVEPQILLLDE 162
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
496-616 2.94e-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: 44.00  E-value: 2.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393  496 RVEEG-MH----LLITGPNGCGKSSLFRILGG-LWPTYGGVlykPPPQRMFYIPQrpYMSVGslrdqviYPDSVEDMQRK 569
Cdd:COG1245 357 EVEGGeIRegevLGIVGPNGIGKTTFAKILAGvLKPDEGEV---DEDLKISYKPQ--YISPD-------YDGTVEEFLRS 424
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 7262393  570 GYSEqDLEA------ILDVVHLHHILQREggweaMCDwkdvLSGGEKQRIGMA 616
Cdd:COG1245 425 ANTD-DFGSsyykteIIKPLGLEKLLDKN-----VKD----LSGGELQRVAIA 467
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
605-634 3.67e-04

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 43.25  E-value: 3.67e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 7262393   605 LSGGEKQRIGMARMFYHRPKYALLDECTSA 634
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSA 170
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
493-635 4.25e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 43.86  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVL-----------YKPPPQRMFYIPQRPYMSVGSLRDQVIYP 560
Cdd:PTZ00265  404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPTEGDIIindshnlkdinLKWWRSKIGVVSQDPLLFSNSIKNNIKYS 483
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    561 -DSVEDMQ-------RKGYSEQ---------------DLEAILDVVHLHHILQREGGWEAMCDWKDV------------- 604
Cdd:PTZ00265  484 lYSLKDLEalsnyynEDGNDSQenknkrnscrakcagDLNDMSNTTDSNELIEMRKNYQTIKDSEVVdvskkvlihdfvs 563
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 7262393    605 ----------------LSGGEKQRIGMARMFYHRPKYALLDECTSAV 635
Cdd:PTZ00265  564 alpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSL 610
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
605-634 4.96e-04

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 43.14  E-value: 4.96e-04
                        10        20        30
                ....*....|....*....|....*....|
gi 7262393  605 LSGGEKQRIGMARMFYHRPKYALLDECTSA 634
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSA 170
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
605-663 5.21e-04

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 42.07  E-value: 5.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7262393   605 LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKI----FQAAKDAGIALLSITHRPSL 663
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIadllFSLNREHGTTLILVTHDLQL 209
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
505-648 5.40e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 43.26  E-value: 5.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   505 ITGPNGCGKSSLFRILGG-LWPTYGGVLYKPppqRMFYIPQrpYMSVGslrdqviYPDSVEDMQRKG---------YSEq 574
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGvLKPDEGEVDPEL---KISYKPQ--YIKPD-------YDGTVEDLLRSItddlgssyyKSE- 436
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7262393   575 dleaILDVVHLHHILQREggweaMCDwkdvLSGGEKQRIGMARMFYHRPKYALLDEcTSAvSIDVEGKIfQAAK 648
Cdd:PRK13409 437 ----IIKPLQLERLLDKN-----VKD----LSGGELQRVAIAACLSRDADLYLLDE-PSA-HLDVEQRL-AVAK 494
PLN03130 PLN03130
ABC transporter C family member; Provisional
493-644 7.45e-04

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 43.19  E-value: 7.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    493 LNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGG-VLYKpppQRMFYIPQRPYMSVGSLRDQVIYPDSvedmqrkg 570
Cdd:PLN03130  636 INLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDAsVVIR---GTVAYVPQVSWIFNATVRDNILFGSP-------- 704
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7262393    571 YSEQDLEAILDVVHLHHILQR-EGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIF 644
Cdd:PLN03130  705 FDPERYERAIDVTALQHDLDLlPGGDLTEIGERGVnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVF 780
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
489-645 7.88e-04

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 42.78  E-value: 7.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP-TYGGVLYK--PPPQ--------RMFYIPQRPYMsvgslrdqv 557
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDvSEGDIRFHdiPLTKlqldswrsRLAVVSQTPFL--------- 400
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   558 iYPDSVED---MQRKGYSEQDLEAILDVVHLHH-ILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:PRK10789 401 -FSDTVANniaLGRPDATQQEIEHVARLASVHDdILRLPQGYDTEVGERGVmLSGGQKQRISIARALLLNAEILILDDAL 479
                        170
                 ....*....|...
gi 7262393   633 SAVSIDVEGKIFQ 645
Cdd:PRK10789 480 SAVDGRTEHQILH 492
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
489-659 9.80e-04

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 41.54  E-value: 9.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLYKPPP----------QRMFYIPQRPYMSVG-SLRDQ 556
Cdd:PRK11231  17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARlLTPQSGTVFLGDKPismlssrqlaRRLALLPQHHLTPEGiTVREL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   557 VIYPDS----------VEDMQRkgySEQDLEAildvVHLHHILQReggweAMCDwkdvLSGGEKQRIGMARMFYHRPKYA 626
Cdd:PRK11231  97 VAYGRSpwlslwgrlsAEDNAR---VNQAMEQ----TRINHLADR-----RLTD----LSGGQRQRAFLAMVLAQDTPVV 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 7262393   627 LLDECTSAVSID--VE-GKIFQAAKDAGIALLSITH 659
Cdd:PRK11231 161 LLDEPTTYLDINhqVElMRLMRELNTQGKTVVTVLH 196
PLN03232 PLN03232
ABC transporter C family member; Provisional
542-660 1.29e-03

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 42.27  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393    542 IPQRPYMSVGSLRDQViypDSVEDmqrkgYSEQDLEAILDVVHLHHILQREG-GWEA-MCDWKDVLSGGEKQRIGMARMF 619
Cdd:PLN03232 1315 IPQSPVLFSGTVRFNI---DPFSE-----HNDADLWEALERAHIKDVIDRNPfGLDAeVSEGGENFSVGQRQLLSLARAL 1386
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 7262393    620 YHRPKYALLDECTSAVSIDVEGKIFQAAKDA--GIALLSITHR 660
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIREEfkSCTMLVIAHR 1429
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
605-662 1.34e-03

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 41.93  E-value: 1.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7262393   605 LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIfQAAKDA---GIALLSITHRPS 662
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAI-QAALDElqkNRTSLVIAHRLS 540
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
507-635 1.67e-03

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 40.92  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   507 GPNGCGKSSLFRI---LGGLWPT---------YGGVLYKP---PPQ---RMFYIPQRPYMSVGSLRDQVIYPDSVEDMQr 568
Cdd:PRK14243  43 GPSGCGKSTILRCfnrLNDLIPGfrvegkvtfHGKNLYAPdvdPVEvrrRIGMVFQKPNPFPKSIYDNIAYGARINGYK- 121
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7262393   569 kgyseQDLEAILDvvhlhHILQREGGWEAMcdwKD-------VLSGGEKQRIGMARMFYHRPKYALLDECTSAV 635
Cdd:PRK14243 122 -----GDMDELVE-----RSLRQAALWDEV---KDklkqsglSLSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
487-675 2.70e-03

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 39.83  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   487 EVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQR-------MFYIPQRPYMsvgslrdqvi 558
Cdd:PRK13543  24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLhVESGQIQIDGKTATrgdrsrfMAYLGHLPGL---------- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   559 ypdsvedmqrkgysEQDLEAI-----LDVVHLHHILQREGGWEA---MCDWKDV----LSGGEKQRIGMARMFYHRPKYA 626
Cdd:PRK13543  94 --------------KADLSTLenlhfLCGLHGRRAKQMPGSALAivgLAGYEDTlvrqLSAGQKKRLALARLWLSPAPLW 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 7262393   627 LLDEctSAVSIDVEG-----KIFQAAKDAGIALLSITH--RPSLwKYHTHLLQFDG 675
Cdd:PRK13543 160 LLDE--PYANLDLEGitlvnRMISAHLRGGGAALVTTHgaYAAP-PVRTRMLTLEA 212
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
489-630 5.13e-03

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 39.83  E-value: 5.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY--------KPPPQR---M------FYipqrPYMSVg 551
Cdd:PRK11650  19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWiggrvvneLEPADRdiaMvfqnyaLY----PHMSV- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   552 slRDQVIYPDSVEDMQrKGYSEQDLEAILDVVHLHHILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:PRK11650  94 --RENMAYGLKIRGMP-KAEIEERVAEAARILELEPLLDRkprE------------LSGGQRQRVAMGRAIVREPAVFLF 158

                 ..
gi 7262393   629 DE 630
Cdd:PRK11650 159 DE 160
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
493-525 5.16e-03

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: 39.05  E-value: 5.16e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 7262393  493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP 525
Cdd:cd03220  41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP 73
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
483-530 5.31e-03

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 39.29  E-value: 5.31e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 7262393  483 TPSGEVVVAS-LNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGV 530
Cdd:COG1134  34 TRREEFWALKdVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEPTSGRV 83
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
483-633 5.33e-03

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: 40.28  E-value: 5.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393     483 TPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYG-----GVLYKPPP----QRMF-YIPQRPYMSVGS 552
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGeiqidGVSWNSVTlqtwRKAFgVIPQKVFIFSGT 1307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393     553 LRDQViypDSVEDmqrkgYSEQDLEAILDVVHLHHILQR----------EGGWeamcdwkdVLSGGEKQRIGMARMFYHR 622
Cdd:TIGR01271 1308 FRKNL---DPYEQ-----WSDEEIWKVAEEVGLKSVIEQfpdkldfvlvDGGY--------VLSNGHKQLMCLARSILSK 1371
                          170
                   ....*....|.
gi 7262393     623 PKYALLDECTS 633
Cdd:TIGR01271 1372 AKILLLDEPSA 1382
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
505-659 6.50e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 39.35  E-value: 6.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   505 ITGPNGCGKSSLFRILGGL-WPTYGGVLYKPPP----------QRMFYIPQRPYMS-VGS---------LRDQVIypdSV 563
Cdd:PRK13648  40 IVGHNGSGKSTIAKLMIGIeKVKSGEIFYNNQAitddnfeklrKHIGIVFQNPDNQfVGSivkydvafgLENHAV---PY 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7262393   564 EDMQRKGYseqdlEAILDVvhlhhilqreggweAMCDWKD----VLSGGEKQRIGMARMFYHRPKYALLDECTSAvsIDV 639
Cdd:PRK13648 117 DEMHRRVS-----EALKQV--------------DMLERADyepnALSGGQKQRVAIAGVLALNPSVIILDEATSM--LDP 175
                        170       180
                 ....*....|....*....|....*.
gi 7262393   640 EGK------IFQAAKDAGIALLSITH 659
Cdd:PRK13648 176 DARqnlldlVRKVKSEHNITIISITH 201
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
504-573 8.24e-03

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 39.49  E-value: 8.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7262393   504 LItGPNGCGKSSLFRILGG-LWPTYGGVLYKpPPQRMfyipqrpymsvGSLR-DQVIYPD-SVEDMQRKGYSE 573
Cdd:PRK15064  32 LI-GANGCGKSTFMKILGGdLEPSAGNVSLD-PNERL-----------GKLRqDQFAFEEfTVLDTVIMGHTE 91
 
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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