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Conserved domains on  [gi|2549828669|ref|WP_302016590|]
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MULTISPECIES: ABC transporter ATP-binding protein [Sutterella]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11467491)

ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ATP transporter complex responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of substrates including carbohydrates and heme

CATH:  3.40.50.300
PubMed:  25750732|24638992
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1-495 0e+00

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


:

Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 707.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:COG3845     2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVALGLSTG----ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPK 156
Cdd:COG3845    82 IGMVHQHFMLVPNLTVAENIVLGLEPTkggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMIGND 236
Cdd:COG3845   162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGRE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 237 -PPTVREGTAKAGEVVFEMRHVSAPGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSP 315
Cdd:COG3845   242 vLLRVEKAPAEPGEVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 316 VGELDTHARRISGLRYVPEQRLGHAAVPELSLTANTYLT---GDSLVRSGFILRDRARSFANLVIERFHVKTPNAEKAAG 392
Cdd:COG3845   322 ITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGryrRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPAR 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 393 SLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALS 472
Cdd:COG3845   402 SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
                         490       500
                  ....*....|....*....|...
gi 2549828669 473 PAVPKPTISIEEVGRWMSGLWPD 495
Cdd:COG3845   482 GEVPAAEATREEIGLLMAGVKEE 504
 
Name Accession Description Interval E-value
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1-495 0e+00

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 707.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:COG3845     2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVALGLSTG----ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPK 156
Cdd:COG3845    82 IGMVHQHFMLVPNLTVAENIVLGLEPTkggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMIGND 236
Cdd:COG3845   162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGRE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 237 -PPTVREGTAKAGEVVFEMRHVSAPGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSP 315
Cdd:COG3845   242 vLLRVEKAPAEPGEVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 316 VGELDTHARRISGLRYVPEQRLGHAAVPELSLTANTYLT---GDSLVRSGFILRDRARSFANLVIERFHVKTPNAEKAAG 392
Cdd:COG3845   322 ITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGryrRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPAR 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 393 SLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALS 472
Cdd:COG3845   402 SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
                         490       500
                  ....*....|....*....|...
gi 2549828669 473 PAVPKPTISIEEVGRWMSGLWPD 495
Cdd:COG3845   482 GEVPAAEATREEIGLLMAGVKEE 504
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1-471 1.94e-114

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 347.30  E-value: 1.94e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKII-----YGAArpdEGEISFDGHPLGVETPAQ 75
Cdd:PRK13549    2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvypHGTY---EGEIIFEGEELQASNIRD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  76 ARELGIAMVHQHFALFDTLSVTENVALG--LSTG--ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRAL 151
Cdd:PRK13549   79 TERAGIAIIHQELALVKELSVLENIFLGneITPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARL 231
Cdd:PRK13549  159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITM 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 232 MIGndpptvREGTA-------KAGEVVFEMRHVSA--PGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEY 302
Cdd:PRK13549  239 MVG------RELTAlyprephTIGEVILEVRNLTAwdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 303 --LCEADrVLLFNSPVgELDTHARRIS-GLRYVPEQRLGHAAVPELSLTANTYLTG-DSLVRSGFILRDRARSFANLVIE 378
Cdd:PRK13549  313 pgRWEGE-IFIDGKPV-KIRNPQQAIAqGIAMVPEDRKRDGIVPVMGVGKNITLAAlDRFTGGSRIDDAAELKTILESIQ 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 379 RFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFE 458
Cdd:PRK13549  391 RLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLG 470
                         490
                  ....*....|...
gi 2549828669 459 ISDRIAVMYRGAL 471
Cdd:PRK13549  471 LSDRVLVMHEGKL 483
GguA NF040905
sugar ABC transporter ATP-binding protein;
5-489 6.38e-97

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 302.09  E-value: 6.38e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYG--AARPDEGEISFDGHPLGVETPAQARELGIA 82
Cdd:NF040905    2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyPHGSYEGEILFDGEVCRFKDIRDSEALGIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTLSVTENVALGLSTG----ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLL 158
Cdd:NF040905   82 IIHQELALIPYLSIAENIFLGNERAkrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAE--SEENLARLMIGND 236
Cdd:NF040905  162 ILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRADevTEDRIIRGMVGRD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 237 -----PPTvregTAKAGEVVFEMRHVSA--PG-STRVCgIDNVSLAVRAGEIVGIAGISGNGQARFMAA---------AS 299
Cdd:NF040905  242 ledryPER----TPKIGEVVFEVKNWTVyhPLhPERKV-VDDVSLNVRRGEIVGIAGLMGAGRTELAMSvfgrsygrnIS 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 300 GEylceadrVLLFNSPVgELDTHARRI-SGLRYVPEQRLGHAAVPELSLTANTYLTG-DSLVRSGFILRDRARSFANLVI 377
Cdd:NF040905  317 GT-------VFKDGKEV-DVSTVSDAIdAGLAYVTEDRKGYGLNLIDDIKRNITLANlGKVSRRGVIDENEEIKVAEEYR 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 378 ERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELF 457
Cdd:NF040905  389 KKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELL 468
                         490       500       510
                  ....*....|....*....|....*....|..
gi 2549828669 458 EISDRIAVMYRGALSPAVPKPTISIEEVGRWM 489
Cdd:NF040905  469 GMCDRIYVMNEGRITGELPREEASQERIMRLI 500
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
5-471 4.06e-92

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 289.80  E-value: 4.06e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAaRPD---EGEISFDGHPLGVETPAQARELGI 81
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASNIRDTERAGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQHFALFDTLSVTENVALG----LSTGISA-AEIEREIRLLGEKYGLEVDPAS-VVMELSMGERQRVEILRALMTKP 155
Cdd:TIGR02633  81 VIIHQELTLVPELSVAENIFLGneitLPGGRMAyNAMYLRAKNLLRELQLDADNVTrPVGDYGGGQQQLVEIAKALNKQA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 156 KLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMIGn 235
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 236 dpptvREGTA-------KAGEVVFEMRHVSA--PGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEY--LC 304
Cdd:TIGR02633 240 -----REITSlyphephEIGDVILEARNLTCwdVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpgKF 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 305 EADrVLLFNSPVgELDTHARRI-SGLRYVPEQRLGHAAVPELSLTANTYLTgdSLVRSGFILRDRARSFANLV---IERF 380
Cdd:TIGR02633 315 EGN-VFINGKPV-DIRNPAQAIrAGIAMVPEDRKRHGIVPILGVGKNITLS--VLKSFCFKMRIDAAAELQIIgsaIQRL 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 381 HVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEIS 460
Cdd:TIGR02633 391 KVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLS 470
                         490
                  ....*....|.
gi 2549828669 461 DRIAVMYRGAL 471
Cdd:TIGR02633 471 DRVLVIGEGKL 481
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
5-217 1.68e-81

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: 250.42  E-value: 1.68e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAMV 84
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQhfalfdtlsvtenvalglstgisaaeiereirllgekyglevdpasvvmeLSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:cd03216    81 YQ--------------------------------------------------LSVGERQMVEIARALARNARLLILDEPT 110
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 165 SVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:cd03216   111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
21-165 3.07e-45

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 155.50  E-value: 3.07e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIAMVHQHFALFDTLSVTENV 100
Cdd:pfam00005   2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 ALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVM----ELSMGERQRVEILRALMTKPKLLILDEPTS 165
Cdd:pfam00005  81 RLGLLlKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
13-209 1.69e-27

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 108.86  E-value: 1.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  13 RYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEIsfdghplgvetpAQARELGIAMVHQHFALFD 92
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGARVAYVPQRSEVPD 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  93 TLSVT--ENVALGL---------STGISAAEIEREIRLLGEKyGLEVDPASvvmELSMGERQRVEILRALMTKPKLLILD 161
Cdd:NF040873   69 SLPLTvrDLVAMGRwarrglwrrLTRDDRAAVDDALERVGLA-DLAGRQLG---ELSGGQRQRALLAQGLAQEADLLLLD 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2549828669 162 EPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIReLADRCVVL 209
Cdd:NF040873  145 EPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVR-RADPCVLL 191
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
8-222 6.65e-23

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 102.90  E-value: 6.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   8 RNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvetpaqARELGIAM---- 83
Cdd:NF033858  270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD------AGDIATRRrvgy 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 VHQHFALFDTLSVTENVALG--LsTGISAAEIEREIRLLGEKYGLE--VD--PASvvmeLSMGERQRVEILRALMTKPKL 157
Cdd:NF033858  344 MSQAFSLYGELTVRQNLELHarL-FHLPAAEIAARVAEMLERFDLAdvADalPDS----LPLGIRQRLSLAVAVIHKPEL 418
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 158 LILDEPTSVLTPQAvRKLF-KTLHQLSSE-GVSIlFIS-HKLDEIrELADRCVVLRAGKVVASVDPKA 222
Cdd:NF033858  419 LILDEPTSGVDPVA-RDMFwRLLIELSREdGVTI-FIStHFMNEA-ERCDRISLMHAGRVLASDTPAA 483
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
6-469 4.52e-18

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 87.49  E-value: 4.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   6 SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgvetpAQARELgiAMVH 85
Cdd:NF033858    3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM-----ADARHR--RAVC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  86 QHFA---------LFDTLSVTENVAL-GLSTGISAAEIEREIRLLGEKYGLE--VD-PASvvmELSMGERQRVEILRALM 152
Cdd:NF033858   76 PRIAympqglgknLYPTLSVFENLDFfGRLFGQDAAERRRRIDELLRATGLApfADrPAG---KLSGGMKQKLGLCCALI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 153 TKPKLLILDEPTSVLTPQAvRKLFKTL---HQLSSEGVSILFISHKLDEIrELADRCVVLRAGKVVASVDPK-------A 222
Cdd:NF033858  153 HDPDLLILDEPTTGVDPLS-RRQFWELidrIRAERPGMSVLVATAYMEEA-ERFDWLVAMDAGRVLATGTPAellartgA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 223 ES-EENLARLMigndPPTVREGTA----------KAGEVVFEMRHVsapgsTRVCG----IDNVSLAVRAGEIVGIAGIS 287
Cdd:NF033858  231 DTlEAAFIALL----PEEKRRGHQpvvipprpadDDDEPAIEARGL-----TMRFGdftaVDHVSFRIRRGEIFGFLGSN 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 288 GNGQARFM-------AAASGEylceadrVLLFNSPV---------------------GE------LDTHARrisgLRYVP 333
Cdd:NF033858  302 GCGKSTTMkmltgllPASEGE-------AWLFGQPVdagdiatrrrvgymsqafslyGEltvrqnLELHAR----LFHLP 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 334 EQRLGhAAVPELsltantyltgdslvrsgfilrdrarsfanlvIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPR 413
Cdd:NF033858  371 AAEIA-ARVAEM-------------------------------LERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPE 417
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 414 VLLVHQPTWGVDVGAaaviRNS----LIRL-RDDGAAIIVVSEEIDELfEISDRIAVMYRG 469
Cdd:NF033858  418 LLILDEPTSGVDPVA----RDMfwrlLIELsREDGVTIFISTHFMNEA-ERCDRISLMHAG 473
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
5-216 1.08e-12

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 69.38  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAG--KSTLMKIIYGaarPDEGEISFDGHPLGVETPAQARELGIa 82
Cdd:NF000106   14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 mvHQ--HFALFDTLSVTENV-ALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLI 159
Cdd:NF000106   90 --HRpvR*GRRESFSGRENLyMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:NF000106  168 LDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
239-469 1.14e-10

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 63.22  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 239 TVREGTAKAGEVVFEMRHVSapgstRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGE 318
Cdd:NF000106    5 TISNGARNAVEVRGLVKHFG-----EVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCAN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 319 LDTHARRISGLRYVpeqRLGHAAvpELSLTANTYLTGDSLVRSgfilRDRARSFANLVIERFHVkTPNAEKAAGSLSGGN 398
Cdd:NF000106   80 RRALRRTIG*HRPV---R*GRRE--SFSGRENLYMIGR*LDLS----RKDARARADELLERFSL-TEAAGRAAAKYSGGM 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 399 LQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:NF000106  150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRG 220
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
29-205 1.26e-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: 45.06  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   29 PGEVLAILGENGAGKSTLMKIIYGAARPDEGEIsfdghplgvetpaqarelgiamvhqhfalfdtlsvtenVALGLSTGI 108
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------------IYIDGEDIL 42
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  109 SAAEIEREIRLLGEKYGLEVDpasvvmelsmGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLH------QL 182
Cdd:smart00382  43 EEVLDQLLLIIVGGKKASGSG----------ELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllllLK 112
                          170       180
                   ....*....|....*....|...
gi 2549828669  183 SSEGVSILFISHKLDEIRELADR 205
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPALLR 135
 
Name Accession Description Interval E-value
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1-495 0e+00

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 707.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:COG3845     2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVALGLSTG----ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPK 156
Cdd:COG3845    82 IGMVHQHFMLVPNLTVAENIVLGLEPTkggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMIGND 236
Cdd:COG3845   162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGRE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 237 -PPTVREGTAKAGEVVFEMRHVSAPGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSP 315
Cdd:COG3845   242 vLLRVEKAPAEPGEVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 316 VGELDTHARRISGLRYVPEQRLGHAAVPELSLTANTYLT---GDSLVRSGFILRDRARSFANLVIERFHVKTPNAEKAAG 392
Cdd:COG3845   322 ITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGryrRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPAR 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 393 SLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALS 472
Cdd:COG3845   402 SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
                         490       500
                  ....*....|....*....|...
gi 2549828669 473 PAVPKPTISIEEVGRWMSGLWPD 495
Cdd:COG3845   482 GEVPAAEATREEIGLLMAGVKEE 504
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-491 3.36e-173

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 497.23  E-value: 3.36e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:COG1129     1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVALG--LSTG--ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPK 156
Cdd:COG1129    81 IAIIHQELNLVPNLSVAENIFLGrePRRGglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMIGND 236
Cdd:COG1129   161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGRE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 237 PPTVR-EGTAKAGEVVFEMRHVSAPGstrvcGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSP 315
Cdd:COG1129   241 LEDLFpKRAAAPGEVVLEVEGLSVGG-----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKP 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 316 VGELDTHARRISGLRYVPEQRLGHAAVPELSLTANTYLTG-DSLVRSGFILRDRARSFANLVIERFHVKTPNAEKAAGSL 394
Cdd:COG1129   316 VRIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASlDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNL 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 395 SGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALSPA 474
Cdd:COG1129   396 SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGE 475
                         490
                  ....*....|....*..
gi 2549828669 475 VPKPTISIEEVGRWMSG 491
Cdd:COG1129   476 LDREEATEEAIMAAATG 492
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1-471 1.94e-114

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 347.30  E-value: 1.94e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKII-----YGAArpdEGEISFDGHPLGVETPAQ 75
Cdd:PRK13549    2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvypHGTY---EGEIIFEGEELQASNIRD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  76 ARELGIAMVHQHFALFDTLSVTENVALG--LSTG--ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRAL 151
Cdd:PRK13549   79 TERAGIAIIHQELALVKELSVLENIFLGneITPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARL 231
Cdd:PRK13549  159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITM 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 232 MIGndpptvREGTA-------KAGEVVFEMRHVSA--PGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEY 302
Cdd:PRK13549  239 MVG------RELTAlyprephTIGEVILEVRNLTAwdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 303 --LCEADrVLLFNSPVgELDTHARRIS-GLRYVPEQRLGHAAVPELSLTANTYLTG-DSLVRSGFILRDRARSFANLVIE 378
Cdd:PRK13549  313 pgRWEGE-IFIDGKPV-KIRNPQQAIAqGIAMVPEDRKRDGIVPVMGVGKNITLAAlDRFTGGSRIDDAAELKTILESIQ 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 379 RFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFE 458
Cdd:PRK13549  391 RLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLG 470
                         490
                  ....*....|...
gi 2549828669 459 ISDRIAVMYRGAL 471
Cdd:PRK13549  471 LSDRVLVMHEGKL 483
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1-506 6.38e-103

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 317.76  E-value: 6.38e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:PRK15439    8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVALGLSTgiSAAEIEREIRLLGEkYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLIL 160
Cdd:PRK15439   88 IYLVPQEPLLFPNLSVKENILFGLPK--RQASMQKMKQLLAA-LGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMigndPPTV 240
Cdd:PRK15439  165 DEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI----TPAA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 241 REGTAKAGEVVF----EMRHVSAPGST--RVC-----GIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRV 309
Cdd:PRK15439  241 REKSLSASQKLWlelpGNRRQQAAGAPvlTVEdltgeGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 310 LLFNSPVGELDTHARRISGLRYVPEQRLGHAAVPELSLTANTYltgdSLV--RSGFILRdRARSFAnlVIERFH----VK 383
Cdd:PRK15439  321 MLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVC----ALThnRRGFWIK-PARENA--VLERYRralnIK 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 384 TPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRI 463
Cdd:PRK15439  394 FNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRV 473
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 2549828669 464 AVMYRGALSPAVPKPTISIEEVGRWMSGlwpdspfTQKTSEAH 506
Cdd:PRK15439  474 LVMHQGEISGALTGAAINVDTIMRLAFG-------EHQAQEAS 509
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1-478 3.35e-101

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 313.00  E-value: 3.35e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:PRK11288    1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVALG-LSTG---ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPK 156
Cdd:PRK11288   81 VAIIYQELHLVPEMTVAENLYLGqLPHKggiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAE-SEENLARLMIGN 235
Cdd:PRK11288  161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQvDRDQLVQAMVGR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 236 DPPTV-----REgtakAGEVVFEMRHVSAPGSTrvcgiDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVL 310
Cdd:PRK11288  241 EIGDIygyrpRP----LGEVRLRLDGLKGPGLR-----EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVY 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 311 LFNSPVGELDTHARRISGLRYVPEQRLGHAAVPELSLTANTYLTG-DSLVRSGFILRDRA-RSFANLVIERFHVKTPNAE 388
Cdd:PRK11288  312 LDGKPIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISArRHHLRAGCLINNRWeAENADRFIRSLNIKTPSRE 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 389 KAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYR 468
Cdd:PRK11288  392 QLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMRE 471
                         490
                  ....*....|
gi 2549828669 469 GALSPAVPKP 478
Cdd:PRK11288  472 GRIAGELARE 481
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
1-472 1.24e-100

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 311.55  E-value: 1.24e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:PRK10762    1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVALGLST-----GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKP 155
Cdd:PRK10762   81 IGIIHQELNLIPQLTIAENIFLGREFvnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 156 KLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMIG- 234
Cdd:PRK10762  161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGr 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 235 ---------NDPPtvregtakaGEVVFEMRHVSAPgstrvcGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCE 305
Cdd:PRK10762  241 kledqyprlDKAP---------GEVRLKVDNLSGP------GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRT 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 306 ADRVLLFNSPVGELDTHARRISGLRYVPEQRLGHAAVPELSLTANTYLTG-DSLVRSGFILRDRARSFA-NLVIERFHVK 383
Cdd:PRK10762  306 SGYVTLDGHEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTAlRYFSRAGGSLKHADEQQAvSDFIRLFNIK 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 384 TPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRI 463
Cdd:PRK10762  386 TPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRI 465

                  ....*....
gi 2549828669 464 AVMYRGALS 472
Cdd:PRK10762  466 LVMHEGRIS 474
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1-488 1.23e-99

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 309.41  E-value: 1.23e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:PRK09700    2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVALG-LSTG-------ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALM 152
Cdd:PRK09700   82 IGIIYQELSVIDELTVLENLYIGrHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLM 232
Cdd:PRK09700  162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLM 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 233 IGNDP----PTVREGTAK-AGEVVFEMRHVSAPGSTRVcgiDNVSLAVRAGEIVGIAGISGNGQARFMAA-------ASG 300
Cdd:PRK09700  242 VGRELqnrfNAMKENVSNlAHETVFEVRNVTSRDRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNClfgvdkrAGG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 301 EYLCEADRVllfnSPVGELDTHARrisGLRYVPEQRLGHAAVPELSLTANTYLTgDSLVRSGF-----ILRDR-ARSFAN 374
Cdd:PRK09700  319 EIRLNGKDI----SPRSPLDAVKK---GMAYITESRRDNGFFPNFSIAQNMAIS-RSLKDGGYkgamgLFHEVdEQRTAE 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 375 LVIERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEID 454
Cdd:PRK09700  391 NQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELP 470
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 2549828669 455 ELFEISDRIAVMYRGALSPAVP-KPTISIEEVGRW 488
Cdd:PRK09700  471 EIITVCDRIAVFCEGRLTQILTnRDDMSEEEIMAW 505
GguA NF040905
sugar ABC transporter ATP-binding protein;
5-489 6.38e-97

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 302.09  E-value: 6.38e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYG--AARPDEGEISFDGHPLGVETPAQARELGIA 82
Cdd:NF040905    2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyPHGSYEGEILFDGEVCRFKDIRDSEALGIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTLSVTENVALGLSTG----ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLL 158
Cdd:NF040905   82 IIHQELALIPYLSIAENIFLGNERAkrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAE--SEENLARLMIGND 236
Cdd:NF040905  162 ILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRADevTEDRIIRGMVGRD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 237 -----PPTvregTAKAGEVVFEMRHVSA--PG-STRVCgIDNVSLAVRAGEIVGIAGISGNGQARFMAA---------AS 299
Cdd:NF040905  242 ledryPER----TPKIGEVVFEVKNWTVyhPLhPERKV-VDDVSLNVRRGEIVGIAGLMGAGRTELAMSvfgrsygrnIS 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 300 GEylceadrVLLFNSPVgELDTHARRI-SGLRYVPEQRLGHAAVPELSLTANTYLTG-DSLVRSGFILRDRARSFANLVI 377
Cdd:NF040905  317 GT-------VFKDGKEV-DVSTVSDAIdAGLAYVTEDRKGYGLNLIDDIKRNITLANlGKVSRRGVIDENEEIKVAEEYR 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 378 ERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELF 457
Cdd:NF040905  389 KKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELL 468
                         490       500       510
                  ....*....|....*....|....*....|..
gi 2549828669 458 EISDRIAVMYRGALSPAVPKPTISIEEVGRWM 489
Cdd:NF040905  469 GMCDRIYVMNEGRITGELPREEASQERIMRLI 500
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
5-471 4.06e-92

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 289.80  E-value: 4.06e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAaRPD---EGEISFDGHPLGVETPAQARELGI 81
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASNIRDTERAGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQHFALFDTLSVTENVALG----LSTGISA-AEIEREIRLLGEKYGLEVDPAS-VVMELSMGERQRVEILRALMTKP 155
Cdd:TIGR02633  81 VIIHQELTLVPELSVAENIFLGneitLPGGRMAyNAMYLRAKNLLRELQLDADNVTrPVGDYGGGQQQLVEIAKALNKQA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 156 KLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMIGn 235
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 236 dpptvREGTA-------KAGEVVFEMRHVSA--PGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEY--LC 304
Cdd:TIGR02633 240 -----REITSlyphephEIGDVILEARNLTCwdVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpgKF 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 305 EADrVLLFNSPVgELDTHARRI-SGLRYVPEQRLGHAAVPELSLTANTYLTgdSLVRSGFILRDRARSFANLV---IERF 380
Cdd:TIGR02633 315 EGN-VFINGKPV-DIRNPAQAIrAGIAMVPEDRKRHGIVPILGVGKNITLS--VLKSFCFKMRIDAAAELQIIgsaIQRL 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 381 HVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEIS 460
Cdd:TIGR02633 391 KVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLS 470
                         490
                  ....*....|.
gi 2549828669 461 DRIAVMYRGAL 471
Cdd:TIGR02633 471 DRVLVIGEGKL 481
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
7-485 7.64e-90

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 283.54  E-value: 7.64e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   7 LRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAMVHQ 86
Cdd:PRK10982    1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  87 HFALFDTLSVTENVALGL----STGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDE 162
Cdd:PRK10982   81 ELNLVLQRSVMDNMWLGRyptkGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 163 PTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMIGNDpPTVR- 241
Cdd:PRK10982  161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRS-LTQRf 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 242 -EGTAKAGEVVFEMRHVSApgsTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELD 320
Cdd:PRK10982  240 pDKENKPGEVILEVRNLTS---LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHN 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 321 THARRISGLRYVPEQRLGHAAVPELSLTANTYLTGDSLVRSGFILRD--RARSFANLVIERFHVKTPNAEKAAGSLSGGN 398
Cdd:PRK10982  317 ANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDnsRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGN 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 399 LQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALSPAVPKP 478
Cdd:PRK10982  397 QQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTK 476

                  ....*..
gi 2549828669 479 TISIEEV 485
Cdd:PRK10982  477 TTTQNEI 483
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
5-217 1.68e-81

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: 250.42  E-value: 1.68e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAMV 84
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQhfalfdtlsvtenvalglstgisaaeiereirllgekyglevdpasvvmeLSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:cd03216    81 YQ--------------------------------------------------LSVGERQMVEIARALARNARLLILDEPT 110
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 165 SVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:cd03216   111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1-469 2.26e-70

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: 233.26  E-value: 2.26e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPG--ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPD---EGEISFDGHPLgVETPAQ 75
Cdd:COG1123     1 MTPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL-LELSEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  76 ARELGIAMVHQHF-ALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMT 153
Cdd:COG1123    80 LRGRRIGMVFQDPmTQLNPVTVGDQIAEALEnLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA--ESEENLAR 230
Cdd:COG1123   160 DPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEilAAPQALAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 231 LMIGNDPPTVREGTAKAGEVVFEMRHVS----APGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQ-------ARFMAAAS 299
Cdd:COG1123   240 VPRLGAARGRAAPAAAAAEPLLEVRNLSkrypVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKstlarllLGLLRPTS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 300 GEylceadrVLLFNSPVGELDTHARRisGLR----YVPeQRlghaavPELSLtaNTYLT-----GDSLVRSGFILRDRAR 370
Cdd:COG1123   320 GS-------ILFDGKDLTKLSRRSLR--ELRrrvqMVF-QD------PYSSL--NPRMTvgdiiAEPLRLHGLLSRAERR 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 371 SFANLVIERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVV 449
Cdd:COG1123   382 ERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFI 461
                         490       500
                  ....*....|....*....|
gi 2549828669 450 SEEIDELFEISDRIAVMYRG 469
Cdd:COG1123   462 SHDLAVVRYIADRVAVMYDG 481
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
5-228 5.31e-66

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 213.00  E-value: 5.31e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARELgIAMV 84
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV-ARDPAEVRRR-IGYV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVAL-GLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:COG1131    79 PQEPALYPDLTVRENLRFfARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 164 TSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENL 228
Cdd:COG1131   159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
248-471 1.37e-59

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


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 194.19  E-value: 1.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 248 GEVVFEMRHVSAPGSTRvcgidNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRIS 327
Cdd:cd03215     1 GEPVLEVRGLSVKGAVR-----DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 328 GLRYVPEQRLGHAAVPELSLtantyltgdslvrsgfilrdrarsFANLVIERFhvktpnaekaagsLSGGNLQKFIMGRE 407
Cdd:cd03215    76 GIAYVPEDRKREGLVLDLSV------------------------AENIALSSL-------------LSGGNQQKVVLARW 118
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 408 ILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03215   119 LARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
1-217 1.20e-58

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: 194.49  E-value: 1.20e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:COG0411     1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVALG-------------LSTGISAAEiEREIR-----LLgEKYGLEVDPASVVMELSMGER 142
Cdd:COG0411    81 IARTFQNPRLFPELTVLENVLVAaharlgrgllaalLRLPRARRE-EREAReraeeLL-ERVGLADRADEPAGNLSYGQQ 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 143 QRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:COG0411   159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
5-214 1.24e-58

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: 191.46  E-value: 1.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvETPAQARELgIAMV 84
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK-KEPEEVKRR-IGYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENValglstgisaaeiereirllgekyglevdpasvvmELSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:cd03230    79 PEEPSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2549828669 165 SVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:cd03230   124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
5-220 2.32e-57

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: 190.34  E-value: 2.32e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAMV 84
Cdd:cd03219     1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVALGL----STGISAAEIEREIRLLGEK----------YGLEVDPASvvmELSMGERQRVEILRA 150
Cdd:cd03219    81 FQIPRLFPELTVLENVMVAAqartGSGLLLARARREEREARERaeellervglADLADRPAG---ELSYGQQRRLEIARA 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDP 220
Cdd:cd03219   158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
5-222 2.57e-56

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: 187.54  E-value: 2.57e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIAM 83
Cdd:COG1122     1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 VHQH-----FALfdtlSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKL 157
Cdd:COG1122    80 VFQNpddqlFAP----TVEEDVAFGPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:COG1122   156 LVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
5-223 7.60e-56

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 189.97  E-value: 7.60e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARelGIAMV 84
Cdd:COG1118     3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRER--RVGFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVALGLST-GISAAEIEREIRLLGEKYGLE----VDPAsvvmELSMGERQRVEILRALMTKPKLLI 159
Cdd:COG1118    81 FQHYALFPHMTVAENIAFGLRVrPPSKAEIRARVEELLELVQLEgladRYPS----QLSGGQRQRVALARALAVEPEVLL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 160 LDEPTSVLTPQaVRK-----LFKTLHQLsseGVSILFISHKLDEIRELADRCVVLRAGKVVAsVDPKAE 223
Cdd:COG1118   157 LDEPFGALDAK-VRKelrrwLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIEQ-VGTPDE 220
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
5-226 2.29e-55

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: 185.45  E-value: 2.29e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARELgIAMV 84
Cdd:COG4555     2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV-RKEPREARRQ-IGVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVA-LGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:COG4555    80 PDERGLYDRLTVRENIRyFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 164 TSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEE 226
Cdd:COG4555   160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
5-216 3.06e-54

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: 181.56  E-value: 3.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARelGIAMV 84
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERR--NIGMV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVALGL-STGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03259    78 FQDYALFPHLTVAENIAFGLkLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 164 TSVLTPQ---AVRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:cd03259   158 LSALDAKlreELREELKELQR--ELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
6-213 4.32e-53

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: 178.43  E-value: 4.32e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   6 SLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIAM 83
Cdd:cd03225     1 ELKNLSFSYPDGARPalDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 VHQHFAL-FDTLSVTENVALGL-STGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILD 161
Cdd:cd03225    80 VFQNPDDqFFGPTVEEEVAFGLeNLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 162 EPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGK 213
Cdd:cd03225   160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
2-222 4.73e-53

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: 187.03  E-value: 4.73e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   2 TPRLSLRNITKRYP-----GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQA 76
Cdd:COG1123   258 EPLLEVRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSL 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  77 RELG--IAMVHQH-FA-LFDTLSVTENVALGLS--TGISAAEIEREIRLLGEKYGLEVD-----PAsvvmELSMGERQRV 145
Cdd:COG1123   338 RELRrrVQMVFQDpYSsLNPRMTVGDIIAEPLRlhGLLSRAERRERVAELLERVGLPPDladryPH----ELSGGQRQRV 413
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 146 EILRALMTKPKLLILDEPTSVLTP--QA-VRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:COG1123   414 AIARALALEPKLLILDEPTSALDVsvQAqILNLLRDLQR--ELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
5-219 5.26e-53

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: 178.43  E-value: 5.26e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAqarelg 80
Cdd:cd03293     1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLE--VD--PAsvvmELSMGERQRVEILRALMTKP 155
Cdd:cd03293    75 RGYVFQQDALLPWLTVLDNVALGLElQGVPKAEARERAEELLELVGLSgfENayPH----QLSGGMRQRVALARALAVDP 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 156 KLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVL--RAGKVVASVD 219
Cdd:cd03293   151 DVLLLDEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVE 217
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
5-222 5.74e-53

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: 178.40  E-value: 5.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAMV 84
Cdd:cd03224     1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVALGLSTGISA---AEIEREIRL---LGEKYGlevDPASvvmELSMGERQRVEILRALMTKPKLL 158
Cdd:cd03224    81 PEGRRIFPELTVEENLLLGAYARRRAkrkARLERVYELfprLKERRK---QLAG---TLSGGEQQMLAIARALMSRPKLL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:cd03224   155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAE 218
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1-281 6.71e-53

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 182.61  E-value: 6.71e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARelG 80
Cdd:COG3842     2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGLPPEKR--N 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVALGLST-GISAAEIEREIR--L-------LGEKYglevdPAsvvmELSMGERQRVEILRA 150
Cdd:COG3842    79 VGMVFQDYALFPHLTVAENVAFGLRMrGVPKAEIRARVAelLelvglegLADRY-----PH----QLSGGQQQRVALARA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQ---AVRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA--ESE 225
Cdd:COG3842   150 LAPEPRVLLLDEPLSALDAKlreEMREELRRLQR--ELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEiyERP 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 226 ENL--ARLmIGND---PPTVREGTakAGEVVFEMRHVSAPGSTRVCGIDNVSLAVRAGEIV 281
Cdd:COG3842   228 ATRfvADF-IGEAnllPGTVLGDE--GGGVRTGGRTLEVPADAGLAAGGPVTVAIRPEDIR 285
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-216 7.15e-53

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 178.31  E-value: 7.15e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYP----GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ- 75
Cdd:COG1136     1 MSPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  76 ----ARELGIamVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLE--VD--PAsvvmELSMGERQRVE 146
Cdd:COG1136    81 arlrRRHIGF--VFQFFNLLPELTALENVALPLLlAGVSRKERRERARELLERVGLGdrLDhrPS----QLSGGQQQRVA 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 147 ILRALMTKPKLLILDEPTSVL---TPQAVRKLFKTLHQlsSEGVSILFISHklD-EIRELADRCVVLRAGKVVA 216
Cdd:COG1136   155 IARALVNRPKLILADEPTGNLdskTGEEVLELLRELNR--ELGTTIVMVTH--DpELAARADRVIRLRDGRIVS 224
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
5-231 2.62e-52

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 177.56  E-value: 2.62e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL--GI 81
Cdd:COG3638     3 LELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrRI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQHFALFDTLSVTENVALG----------LSTGISAAEIEREIRLLgEKYGLE---VDPASvvmELSMGERQRVEIL 148
Cdd:COG3638    83 GMIFQQFNLVPRLSVLTNVLAGrlgrtstwrsLLGLFPPEDRERALEAL-ERVGLAdkaYQRAD---QLSGGQQQRVAIA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 149 RALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEEN 227
Cdd:COG3638   159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDAV 238

                  ....
gi 2549828669 228 LARL 231
Cdd:COG3638   239 LREI 242
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
4-280 1.62e-51

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 178.73  E-value: 1.62e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvETPAQARelGIAM 83
Cdd:COG3839     3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-DLPPKDR--NIAM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 VHQHFALFDTLSVTENVALGLST-GISAAEIEREIR----LLG-EKYgLEVDPAsvvmELSMGERQRVEILRALMTKPKL 157
Cdd:COG3839    80 VFQSYALYPHMTVYENIAFPLKLrKVPKAEIDRRVReaaeLLGlEDL-LDRKPK----QLSGGQRQRVALGRALVREPKV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 158 LILDEPTSVLTPQ---AVRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKV--VASVD-----PKaeseeN 227
Cdd:COG3839   155 FLLDEPLSNLDAKlrvEMRAEIKRLHR--RLGTTTIYVTHDQVEAMTLADRIAVMNDGRIqqVGTPEelydrPA-----N 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 228 L--ARLmIGNDPPTVREGTAKAGEVVFEMRHVSAPGSTRVCGIDNVSLAVRAGEI 280
Cdd:COG3839   228 LfvAGF-IGSPPMNLLPGTVEGGGVRLGGVRLPLPAALAAAAGGEVTLGIRPEHL 281
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
1-217 1.97e-51

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 175.17  E-value: 1.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL- 79
Cdd:COG1127     2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  80 -GIAMVHQHFALFDTLSVTENVALGL--STGISAAEIEREIRLLGEKYGLEVD----PAsvvmELSMGERQRVEILRALM 152
Cdd:COG1127    82 rRIGMLFQGGALFDSLTVFENVAFPLreHTDLSEAEIRELVLEKLELVGLPGAadkmPS----ELSGGMRKRVALARALA 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:COG1127   158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1-219 3.64e-51

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 174.89  E-value: 3.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYP----GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlgVETPAQA 76
Cdd:COG1116     4 AAPALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP--VTGPGPD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  77 RelgiAMVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLE--VD--PAsvvmELSMGERQRVEILRAL 151
Cdd:COG1116    82 R----GVVFQEPALLPWLTVLDNVALGLElRGVPKAERRERARELLELVGLAgfEDayPH----QLSGGMRQRVAIARAL 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 152 MTKPKLLILDEPTS---VLTPQAVRKLFKTLHQlsSEGVSILFISHKLDE-IReLADRCVVLRA--GKVVASVD 219
Cdd:COG1116   154 ANDPEVLLMDEPFGaldALTRERLQDELLRLWQ--ETGKTVLFVTHDVDEaVF-LADRVVVLSArpGRIVEEID 224
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
5-214 3.70e-51

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: 173.44  E-value: 3.70e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ----- 75
Cdd:cd03255     1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  76 ARELGIamVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTK 154
Cdd:cd03255    81 RRHIGF--VFQSFNLLPDLTALENVELPLLlAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKlDEIRELADRCVVLRAGKV 214
Cdd:cd03255   159 PKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
5-215 3.90e-51

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 173.70  E-value: 3.90e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGV----ETPAQAREL 79
Cdd:COG2884     2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLRRRI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  80 GIamVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLL 158
Cdd:COG2884    82 GV--VFQDFRLLPDRTVYENVALPLRvTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:COG2884   160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
2-222 7.14e-51

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: 173.24  E-value: 7.14e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   2 TPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGI 81
Cdd:COG0410     1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQHFALFDTLSVTENVALGLSTGISAAEIEREIRL-------LGEKYGlevDPASvvmELSMGERQRVEILRALMTK 154
Cdd:COG0410    81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERvyelfprLKERRR---QRAG---TLSGGEQQMLAIGRALMSR 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:COG0410   155 PKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAE 222
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
5-215 9.18e-50

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 170.45  E-value: 9.18e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL- 79
Cdd:cd03258     2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  80 -GIAMVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKL 157
Cdd:cd03258    82 rRIGMIFQHFNLLSSRTVFENVALPLEiAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:cd03258   162 LLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
5-216 1.02e-49

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: 170.38  E-value: 1.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG--IA 82
Cdd:cd03261     1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRrrMG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTLSVTENVALGLS--TGISAAEIEREIRLLGEKYGLEVD----PAsvvmELSMGERQRVEILRALMTKPK 156
Cdd:cd03261    81 MLFQSGALFDSLTVFENVAFPLRehTRLSEEEIREIVLEKLEAVGLRGAedlyPA----ELSGGMKKRVALARALALDPE 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 157 LLILDEPTSVLTPQAVRK---LFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:cd03261   157 LLLYDEPTAGLDPIASGViddLIRSLKK--ELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-231 1.03e-48

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 167.96  E-value: 1.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlgvetPAQARELg 80
Cdd:COG1121     3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRR- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFAlFDT---LSVTENVALGLSTGI------SAAEIEREIRLLgEKYGLEvDPASV-VMELSMGERQRVEILRA 150
Cdd:COG1121    77 IGYVPQRAE-VDWdfpITVRDVVLMGRYGRRglfrrpSRADREAVDEAL-ERVGLE-DLADRpIGELSGGQQQRVLLARA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLrAGKVVASVDPK-AESEENLA 229
Cdd:COG1121   154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEeVLTPENLS 232

                  ..
gi 2549828669 230 RL 231
Cdd:COG1121   233 RA 234
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
5-215 2.24e-48

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: 166.53  E-value: 2.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:cd03257     2 LEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 --IAMVHQH--FALFDTLSVTENVA--LGLSTGISAAEIEREIRLLGEKyglEVDPASVVM-----ELSMGERQRVEILR 149
Cdd:cd03257    82 keIQMVFQDpmSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLV---GVGLPEEVLnryphELSGGQRQRVAIAR 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 150 ALMTKPKLLILDEPTS---VLTPQAVRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:cd03257   159 ALALNPKLLIADEPTSaldVSVQAQILDLLKKLQE--ELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
5-213 3.29e-48

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: 164.28  E-value: 3.29e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL---GVETPAQARELGi 81
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdlEDELPPLRRRIG- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 aMVHQHFALFDTLSVTENVALGLSTgisaaeiereirllgekyglevdpasvvmelsmGERQRVEILRALMTKPKLLILD 161
Cdd:cd03229    80 -MVFQDFALFPHLTVLENIALGLSG---------------------------------GQQQRVALARALAMDPDVLLLD 125
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 162 EPTSVLTPQA---VRKLFKTLHQLSseGVSILFISHKLDEIRELADRCVVLRAGK 213
Cdd:cd03229   126 EPTSALDPITrreVRALLKSLQAQL--GITVVLVTHDLDEAARLADRVVVLRDGK 178
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
5-231 6.20e-48

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: 165.82  E-value: 6.20e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL--GI 81
Cdd:cd03256     1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQHFALFDTLSVTENVALG----------LSTGISAAEIEREIRLLgEKYGLEVDPASVVMELSMGERQRVEILRAL 151
Cdd:cd03256    81 GMIFQQFNLIERLSVLENVLSGrlgrrstwrsLFGLFPKEEKQRALAAL-ERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLAR 230
Cdd:cd03256   160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDE 239

                  .
gi 2549828669 231 L 231
Cdd:cd03256   240 I 240
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
5-217 4.65e-47

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 166.41  E-value: 4.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL- 79
Cdd:COG1135     2 IELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  80 -GIAMVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEvD-----PAsvvmELSMGERQRVEILRALM 152
Cdd:COG1135    82 rKIGMIFQHFNLLSSRTVAENVALPLEiAGVPKAEIRKRVAELLELVGLS-DkadayPS----QLSGGQKQRVGIARALA 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 153 TKPKLLILDEPTSVLTPQ---AVRKLFKTLHQ-LsseGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:COG1135   157 NNPKVLLCDEATSALDPEttrSILDLLKDINReL---GLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
5-217 6.86e-47

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: 162.00  E-value: 6.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAReLGiAMV 84
Cdd:cd03268     1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-IG-ALI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHfALFDTLSVTENV-ALGLSTGISAAEIEREIRLLGekygLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03268    79 EAP-GFYPNLTARENLrLLARLLGIRKKRIDEVLDVVG----LKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 164 TSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:cd03268   154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
5-214 7.01e-47

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: 161.93  E-value: 7.01e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvETPAQAREL--GIA 82
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELrqKVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTLSVTENVALGLST--GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLIL 160
Cdd:cd03262    80 MVFQQFNLFPHLTVLENITLAPIKvkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:cd03262   160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
6-213 7.80e-47

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 160.10  E-value: 7.80e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   6 SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIAMVH 85
Cdd:cd00267     1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-RIGYVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  86 QhfalfdtlsvtenvalglstgisaaeiereirllgekyglevdpasvvmeLSMGERQRVEILRALMTKPKLLILDEPTS 165
Cdd:cd00267    80 Q--------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2549828669 166 VLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGK 213
Cdd:cd00267   110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
8-214 1.10e-46

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: 162.51  E-value: 1.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   8 RNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvETPAQARELGiaMVHQH 87
Cdd:cd03296     6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT-DVPVQERNVG--FVFQH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  88 FALFDTLSVTENVALGL-----STGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDE 162
Cdd:cd03296    83 YALFRHMTVFDNVAFGLrvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 163 PTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:cd03296   163 PFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
5-217 3.69e-46

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 162.97  E-value: 3.69e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ------ARe 78
Cdd:COG4152     2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeER- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  79 lgiamvhqhfALFDTLSVTEN-VALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKL 157
Cdd:COG4152    81 ----------GLYPKMKVGEQlVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:COG4152   151 LILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
5-216 3.95e-46

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: 160.14  E-value: 3.95e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETpaqarELGIAMV 84
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRIGYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTEN-VALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03269    76 PEERGLYPKMKVIDQlVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 164 TSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:cd03269   156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
5-221 1.46e-45

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 159.39  E-value: 1.46e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvETPAQAREL--GIA 82
Cdd:COG1126     2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLrrKVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTLSVTENVALGLST--GISAAEIEREIRLLGEKYGL----EVDPAsvvmELSMGERQRVEILRALMTKPK 156
Cdd:COG1126    81 MVFQQFNLFPHLTVLENVTLAPIKvkKMSKAEAEERAMELLERVGLadkaDAYPA----QLSGGQQQRVAIARALAMEPK 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:COG1126   157 VMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPE 221
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
21-165 3.07e-45

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 155.50  E-value: 3.07e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIAMVHQHFALFDTLSVTENV 100
Cdd:pfam00005   2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 ALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVM----ELSMGERQRVEILRALMTKPKLLILDEPTS 165
Cdd:pfam00005  81 RLGLLlKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
4-231 3.93e-45

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: 158.67  E-value: 3.93e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ-ARElgIA 82
Cdd:COG1120     1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElARR--IA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTLSVTENVALGLSTGISA---------AEIEREIRLLG-----EKYglevdpasvVMELSMGERQRVEIL 148
Cdd:COG1120    79 YVPQEPPAPFGLTVRELVALGRYPHLGLfgrpsaedrEAVEEALERTGlehlaDRP---------VDELSGGERQRVLIA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 149 RALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPkAE--SE 225
Cdd:COG1120   150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP-EEvlTP 228

                  ....*.
gi 2549828669 226 ENLARL 231
Cdd:COG1120   229 ELLEEV 234
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
5-215 5.44e-45

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: 157.78  E-value: 5.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARelGIAMV 84
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKR--PVNTV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVALGLST-GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03300    78 FQNYALFPHLTVFENIAFGLRLkKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 164 TSVLTPQAVRKL---FKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:cd03300   158 LGALDLKLRKDMqleLKRLQK--ELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
1-217 7.34e-45

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: 167.70  E-value: 7.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARE 78
Cdd:COG2274   470 LKGDIELENVSFRYPGDSPPvlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR 549
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  79 LgIAMVHQHFALFDTlSVTENVALGlSTGISAAEIEREIRLLG-----EK--YGLEvdpaSVVME----LSMGERQRVEI 147
Cdd:COG2274   550 Q-IGVVLQDVFLFSG-TIRENITLG-DPDATDEEIIEAARLAGlhdfiEAlpMGYD----TVVGEggsnLSGGQRQRLAI 622
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 148 LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIReLADRCVVLRAGKVVAS 217
Cdd:COG2274   623 ARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIR-LADRIIVLDKGRIVED 690
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
5-217 1.72e-44

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: 156.13  E-value: 1.72e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGI--TANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIA 82
Cdd:cd03263     1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MvhQHFALFDTLSVTENVAL-GLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILD 161
Cdd:cd03263    81 P--QFDALFDELTVREHLRFyARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 162 EPTSVLTPQAVRKLFKTLHQLSSeGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:cd03263   159 EPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRCI 213
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
5-213 1.25e-43

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: 151.77  E-value: 1.25e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIA 82
Cdd:cd03228     1 IEFKNVSFSYPGRPKPvlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTlSVTENValglstgisaaeiereirllgekyglevdpasvvmeLSMGERQRVEILRALMTKPKLLILDE 162
Cdd:cd03228    80 YVPQDPFLFSG-TIRENI------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 163 PTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIReLADRCVVLRAGK 213
Cdd:cd03228   123 ATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
5-214 1.82e-43

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 152.66  E-value: 1.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIAMV 84
Cdd:COG4619     1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ-VAYV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTlSVTENVALGLSTGISAAEIEREIRLLgEKYGLevdPASV----VMELSMGERQRVEILRALMTKPKLLIL 160
Cdd:COG4619    80 PQEPALWGG-TVRDNLPFPFQLRERKFDRERALELL-ERLGL---PPDIldkpVERLSGGERQRLALIRALLLQPDVLLL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLS-SEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:COG4619   155 DEPTSALDPENTRRVEELLREYLaEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
5-220 8.23e-43

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: 151.93  E-value: 8.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAMV 84
Cdd:cd03218     1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVALGL-STGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03218    81 PQEASIFRKLTVEENILAVLeIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 164 TSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDP 220
Cdd:cd03218   161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
7-215 8.71e-43

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 154.96  E-value: 8.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   7 LRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL--G 80
Cdd:PRK11153    4 LKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArrQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLE----VDPAsvvmELSMGERQRVEILRALMTKP 155
Cdd:PRK11153   84 IGMIFQHFNLLSSRTVFDNVALPLElAGTPKAEIKARVTELLELVGLSdkadRYPA----QLSGGQKQRVAIARALASNP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 156 KLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK11153  160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
7-213 1.33e-42

cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]


Pssm-ID: 131721 [Multi-domain]  Cd Length: 214  Bit Score: 150.86  E-value: 1.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   7 LRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL----GVETPAQARELGI 81
Cdd:TIGR02673   4 FHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVnrlrGRQLPLLRRRIGV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 amVHQHFALFDTLSVTENVALGLST-GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLIL 160
Cdd:TIGR02673  84 --VFQDFRLLPDRTVYENVALPLEVrGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGK 213
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
5-222 1.51e-42

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: 151.49  E-value: 1.51e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYP----GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElG 80
Cdd:COG1124     2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR-R 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQH-FALFD-TLSVTENVALGL-STGIsaAEIEREIRLLGEKYGLEVD-----PAsvvmELSMGERQRVEILRALM 152
Cdd:COG1124    81 VQMVFQDpYASLHpRHTVDRILAEPLrIHGL--PDREERIAELLEQVGLPPSfldryPH----QLSGGQRQRVAIARALI 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 153 TKPKLLILDEPTSVLTP--QA-VRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:COG1124   155 LEPELLLLDEPTSALDVsvQAeILNLLKDLRE--ERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
5-219 2.71e-42

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: 153.29  E-value: 2.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARP---DEGEISFDGHPLGVETPAQAR 77
Cdd:COG0444     2 LEVRNLKVYFPTrrgvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  78 EL---GIAMVHQhfalfDTLS-----------VTEnvALGLSTGISAAEIEREIRLLGEKYGLEvDPASVVM----ELSM 139
Cdd:COG0444    82 KIrgrEIQMIFQ-----DPMTslnpvmtvgdqIAE--PLRIHGGLSKAEARERAIELLERVGLP-DPERRLDryphELSG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 140 GERQRVEILRALMTKPKLLILDEPTSVL--TPQA-VRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVV- 215
Cdd:COG0444   154 GMRQRVMIARALALEPKLLIADEPTTALdvTIQAqILNLLKDLQR--ELGLAILFITHDLGVVAEIADRVAVMYAGRIVe 231

                  ....*
gi 2549828669 216 -ASVD 219
Cdd:COG0444   232 eGPVE 236
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
5-215 4.71e-42

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: 149.33  E-value: 4.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHplgVETPAQARELGIAMV 84
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR---DVTDLPPKDRDIAMV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVALGL-STGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03301    78 FQNYALYPHMTVYDNIAFGLkLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 164 TSVLTPQ---AVRKLFKTLHQLssEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:cd03301   158 LSNLDAKlrvQMRAELKRLQQR--LGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
5-215 1.13e-41

phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]


Pssm-ID: 131368 [Multi-domain]  Cd Length: 243  Bit Score: 149.37  E-value: 1.13e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL--GI 81
Cdd:TIGR02315   2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLrrRI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQHFALFDTLSVTENV---ALGLSTGI-------SAAEIEREIRLLgEKYGLEVDPASVVMELSMGERQRVEILRAL 151
Cdd:TIGR02315  82 GMIFQHYNLIERLTVLENVlhgRLGYKPTWrsllgrfSEEDKERALSAL-ERVGLADKAYQRADQLSGGQQQRVAIARAL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
19-215 1.47e-41

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: 149.72  E-value: 1.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  19 ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL---GIAMVHQHFALFDTLS 95
Cdd:cd03294    39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkKISMVFQSFALLPHRT 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  96 VTENVALGLS-TGISAAE-IEREIRLLgEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVR 173
Cdd:cd03294   119 VLENVAFGLEvQGVPRAErEERAAEAL-ELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2549828669 174 KLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:cd03294   198 EMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
5-217 3.08e-41

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: 147.13  E-value: 3.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRY----PGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQAReLG 80
Cdd:cd03266     2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEAR-RR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVA-LGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLI 159
Cdd:cd03266    80 LGFVSDSTGLYDRLTARENLEyFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:cd03266   160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
6-217 9.78e-41

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: 145.75  E-value: 9.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   6 SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlgvetPAQARELgIAMVH 85
Cdd:cd03235     1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP-----LEKERKR-IGYVP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  86 QHFaLFDT---LSVTENVALGL------STGISAAEIEREIRLLgEKYGLEVDPASVVMELSMGERQRVEILRALMTKPK 156
Cdd:cd03235    75 QRR-SIDRdfpISVRDVVLMGLyghkglFRRLSKADKAKVDEAL-ERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLrAGKVVAS 217
Cdd:cd03235   153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVAS 212
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
3-227 2.35e-40

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: 152.99  E-value: 2.35e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgI 81
Cdd:COG4988   335 PSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ-I 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQHFALFDTlSVTENVALGlSTGISAAEIEREIR---LLGEKYGLEVDPASVVME----LSMGERQRVEILRALMTK 154
Cdd:COG4988   414 AWVPQNPYLFAG-TIRENLRLG-RPDASDEELEAALEaagLDEFVAALPDGLDTPLGEggrgLSGGQAQRLALARALLRD 491
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIRElADRCVVLRAGKVVASVDPKAESEEN 227
Cdd:COG4988   492 APLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAKN 562
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
5-241 3.57e-40

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 144.90  E-value: 3.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITAndHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQaRelGIAMV 84
Cdd:COG3840     2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-R--PVSML 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVALGLSTG--ISAAEIEREIRLLgEKYGLE--VD--PAsvvmELSMGERQRVEILRALMTKPKLL 158
Cdd:COG3840    77 FQENNLFPHLTVAQNIGLGLRPGlkLTAEQRAQVEQAL-ERVGLAglLDrlPG----QLSGGQRQRVALARCLVRKRPIL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 159 ILDEPTSVLTPqAVRK----LFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPkaeseenlARLMIG 234
Cdd:COG3840   152 LLDEPFSALDP-ALRQemldLVDELCR--ERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPT--------AALLDG 220

                  ....*..
gi 2549828669 235 NDPPTVR 241
Cdd:COG3840   221 EPPPALA 227
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
23-221 5.55e-40

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: 144.40  E-value: 5.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgveTPAQARELGIAMVHQHFALFDTLSVTENVAL 102
Cdd:cd03299    18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI---TNLPPEKRDISYVPQNYALFPHMTVYKNIAY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 103 GLST-GISAAEIEREIRLLGEKYG----LEVDPASvvmeLSMGERQRVEILRALMTKPKLLILDEPTSVLTPQ---AVRK 174
Cdd:cd03299    95 GLKKrKVDKKEIERKVLEIAEMLGidhlLNRKPET----LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRtkeKLRE 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2549828669 175 LFKTLHQLSseGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:cd03299   171 ELKKIRKEF--GVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
3-213 7.43e-40

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: 143.00  E-value: 7.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIA 82
Cdd:COG4133     1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MvhQHFALFDTLSVTENVAL---GLSTGISAAEIEREIRLLGeKYGLEVDPASvvmELSMGERQRVEILRALMTKPKLLI 159
Cdd:COG4133    81 G--HADGLKPELTVRENLRFwaaLYGLRADREAIDEALEAVG-LAGLADLPVR---QLSAGQKRRVALARLLLSPAPLWL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHklDEIRELADRCVVLRAGK 213
Cdd:COG4133   155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH--QPLELAAARVLDLGDFK 206
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
4-217 7.66e-40

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 151.86  E-value: 7.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYPG-ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIA 82
Cdd:COG1132   339 EIEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ-IG 417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTlSVTENVALGlSTGISAAEIER---------EIRLLGEKYGLEVDPASVvmELSMGERQRVEILRALMT 153
Cdd:COG1132   418 VVPQDTFLFSG-TIRENIRYG-RPDATDEEVEEaakaaqaheFIEALPDGYDTVVGERGV--NLSGGQRQRIAIARALLK 493
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIRElADRCVVLRAGKVVAS 217
Cdd:COG1132   494 DPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
9-263 2.15e-39

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: 146.40  E-value: 2.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   9 NITKRYPGITANdhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL-----GVETPAQARELGiaM 83
Cdd:COG4148     6 DFRLRRGGFTLD--VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsarGIFLPPHRRRIG--Y 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 VHQHFALFDTLSVTENVALGLS---TGISAAEIEREIRLLGEKYGLEVDPASvvmeLSMGERQRVEILRALMTKPKLLIL 160
Cdd:COG4148    82 VFQEARLFPHLSVRGNLLYGRKrapRAERRISFDEVVELLGIGHLLDRRPAT----LSGGERQRVAIGRALLSSPRLLLM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASvDPKAE--SEENLARLMIGNDP 237
Cdd:COG4148   158 DEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVAS-GPLAEvlSRPDLLPLAGGEEA 236
                         250       260
                  ....*....|....*....|....*.
gi 2549828669 238 PTVREGTAKAGEVVFEMRHVSAPGST 263
Cdd:COG4148   237 GSVLEATVAAHDPDYGLTRLALGGGR 262
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
4-217 3.10e-39

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: 141.66  E-value: 3.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRnITKRYPGITANdhVSLDIaPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL-----GVETPAQARe 78
Cdd:cd03297     1 MLCVD-IEKRLPDFTLK--IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkKINLPPQQR- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  79 lGIAMVHQHFALFDTLSVTENVALGLStGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLL 158
Cdd:cd03297    76 -KIGLVFQQYALFPHLNVRENLAFGLK-RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELL 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:cd03297   154 LLDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
5-221 1.31e-38

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: 140.39  E-value: 1.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYG-----AARPDEGEISFDGHPL-GVETPAQARE 78
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIyDLDVDVLELR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  79 LGIAMVHQHFALFDtLSVTENVALGLS-TGI-SAAEIEREIRLLGEKYGL--EVDPASVVMELSMGERQRVEILRALMTK 154
Cdd:cd03260    81 RRVGMVFQKPNPFP-GSIYDNVAYGLRlHGIkLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALANE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSEgVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:cd03260   160 PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
6-217 1.54e-38

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: 138.72  E-value: 1.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   6 SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ-ARELGIamV 84
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElARKIAY--V 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQhfalfdtlsvtenvALGLsTGISAaeiereirlLGEKYglevdpasvVMELSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:cd03214    79 PQ--------------ALEL-LGLAH---------LADRP---------FNELSGGERQRVLLARALAQEPPILLLDEPT 125
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 165 SVLTPQAVRKLFKTLHQLS-SEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:cd03214   126 SHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
5-215 5.93e-38

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 138.97  E-value: 5.93e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGIT-ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIAM 83
Cdd:cd03295     1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR-KIGY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 VHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLevDPASVV----MELSMGERQRVEILRALMTKPKLL 158
Cdd:cd03295    80 VIQQIGLFPHMTVEENIALVPKlLKWPKEKIRERADELLALVGL--DPAEFAdrypHELSGGQQQRVGVARALAADPPLL 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 159 ILDEPTSVLTP---QAVRKLFKTLHQLSseGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:cd03295   158 LMDEPFGALDPitrDQLQEEFKRLQQEL--GKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
4-221 6.44e-38

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 275199 [Multi-domain]  Cd Length: 239  Bit Score: 138.95  E-value: 6.44e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQAR-ELGIA 82
Cdd:TIGR04406   1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI-THLPMHERaRLGIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTLSVTENV--ALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLIL 160
Cdd:TIGR04406  80 YLPQEASIFRKLTVEENImaVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPA 220
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
3-221 9.19e-38

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: 145.68  E-value: 9.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYPG--ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELg 80
Cdd:COG4987   332 PSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR- 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTlSVTENVALG--------LSTGISAAEIEREIRLLGEKYGLEVDPASvvMELSMGERQRVEILRALM 152
Cdd:COG4987   411 IAVVPQRPHLFDT-TLRENLRLArpdatdeeLWAALERVGLGDWLAALPDGLDTWLGEGG--RRLSGGERRRLALARALL 487
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIrELADRCVVLRAGKVVASVDPK 221
Cdd:COG4987   488 RDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHE 554
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
3-214 1.10e-37

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


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 136.41  E-value: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITkrypGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIA 82
Cdd:cd03215     3 PVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MV---HQHFALFDTLSVTENVALGLStgisaaeiereirllgekyglevdpasvvmeLSMGERQRVEILRALMTKPKLLI 159
Cdd:cd03215    79 YVpedRKREGLVLDLSVAENIALSSL-------------------------------LSGGNQQKVVLARWLARDPRVLI 127
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:cd03215   128 LDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
2-231 1.16e-37

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: 138.68  E-value: 1.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   2 TPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEG-EISFDGHPLGVETPAQARELg 80
Cdd:COG1119     1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKR- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQhfALFDTLSVTENV----------ALGLSTGISAAEIEREIRLLGEkYGLEVDPASVVMELSMGERQRVEILRA 150
Cdd:COG1119    80 IGLVSP--ALQLRFPRDETVldvvlsgffdSIGLYREPTDEQRERARELLEL-LGLAHLADRPFGTLSQGEQRRVLIARA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEG-VSILFISHKLDEIRELADRCVVLRAGKVVASVdPKAE--SEEN 227
Cdd:COG1119   157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG-PKEEvlTSEN 235

                  ....
gi 2549828669 228 LARL 231
Cdd:COG1119   236 LSEA 239
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
3-220 1.34e-37

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 138.84  E-value: 1.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYPGITAN----DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlgVETPAQARe 78
Cdd:COG4525     2 SMLTVRHVSVRYPGGGQPqpalQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP--VTGPGADR- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  79 lgiAMVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKL 157
Cdd:COG4525    79 ---GVVFQKDALLPWLNVLDNVAFGLRlRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 158 LILDEPTSVL---TPQAVRKLFKTLHQLSseGVSILFISHKLDEIRELADRCVVL--RAGKVVASVDP 220
Cdd:COG4525   156 LLMDEPFGALdalTREQMQELLLDVWQRT--GKGVFLITHSVEEALFLATRLVVMspGPGRIVERLEL 221
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
9-216 1.53e-37

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: 141.40  E-value: 1.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   9 NITKRYPGITANdhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL-----GVETPAQARELGIam 83
Cdd:TIGR02142   4 RFSKRLGDFSLD--ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkGIFLPPEKRRIGY-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 VHQHFALFDTLSVTENVALGLS------TGISAAEIereIRLLGEKYGLEVDPASvvmeLSMGERQRVEILRALMTKPKL 157
Cdd:TIGR02142  80 VFQEARLFPHLSVRGNLRYGMKrarpseRRISFERV---IELLGIGHLLGRLPGR----LSGGEKQRVAIGRALLSSPRL 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:TIGR02142 153 LLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1-290 5.25e-37

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 143.29  E-value: 5.25e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKS-TLMKII----YGAARPDeGEISFDGHPLGVE 71
Cdd:COG4172     3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHPS-GSILFDGQDLLGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  72 TPAQAREL---GIAMVHQH--FALFDTLSVTENVA--LGLSTGISAAEIEREIRLLGEKYGLEvDPASVV----MELSMG 140
Cdd:COG4172    82 SERELRRIrgnRIAMIFQEpmTSLNPLHTIGKQIAevLRLHRGLSGAAARARALELLERVGIP-DPERRLdaypHQLSGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 141 ERQRVEILRALMTKPKLLILDEPTSVL--TPQA-VRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:COG4172   161 QRQRVMIAMALANEPDLLIADEPTTALdvTVQAqILDLLKDLQR--ELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 218 vdpkAESEENLA-------RLMIGNDPPTVREGTAKAGEVVFEMRHVS----------APGSTRVCGIDNVSLAVRAGEI 280
Cdd:COG4172   239 ----GPTAELFAapqhpytRKLLAAEPRGDPRPVPPDAPPLLEARDLKvwfpikrglfRRTVGHVKAVDGVSLTLRRGET 314
                         330
                  ....*....|
gi 2549828669 281 VGIAGISGNG 290
Cdd:COG4172   315 LGLVGESGSG 324
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
7-241 5.70e-37

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 136.38  E-value: 5.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   7 LRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGhpLGVETPAQA-----RELGi 81
Cdd:PRK09493    4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDerlirQEAG- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 aMVHQHFALFDTLSVTENVALG--LSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLI 159
Cdd:PRK09493   81 -MVFQQFYLFPHLTALENVMFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAeseenlarlMIGNdPPT 239
Cdd:PRK09493  160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQV---------LIKN-PPS 229

                  ..
gi 2549828669 240 VR 241
Cdd:PRK09493  230 QR 231
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
7-214 1.37e-36

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: 134.46  E-value: 1.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   7 LRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL----GVETPAQARELGi 81
Cdd:cd03292     3 FINVTKTYPnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKIG- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 aMVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLIL 160
Cdd:cd03292    82 -VVFQDFRLLPDRNVYENVAFALEvTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:cd03292   161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
5-230 2.41e-36

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 135.24  E-value: 2.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ-ARELgiAM 83
Cdd:COG4559     2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElARRR--AV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 VHQHFAL-FDtLSVTENVALGLSTGISAAEIEREI-----------RLLGEKYglevdpasvvMELSMGERQRVEILRAL 151
Cdd:COG4559    80 LPQHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIvrealalvglaHLAGRSY----------QTLSGGEQQRVQLARVL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 152 -------MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPkAE- 223
Cdd:COG4559   149 aqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTP-EEv 227

                  ....*...
gi 2549828669 224 -SEENLAR 230
Cdd:COG4559   228 lTDELLER 235
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
3-221 2.70e-36

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 134.39  E-value: 2.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgveTP----AQARe 78
Cdd:COG1137     2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI---THlpmhKRAR- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  79 LGIAMVHQHFALFDTLSVTENVALGLST-GISAAEIEREIRLLGEKYGLE--VD-PAsvvMELSMGERQRVEILRALMTK 154
Cdd:COG1137    78 LGIGYLPQEASIFRKLTVEDNILAVLELrKLSKKEREERLEELLEEFGIThlRKsKA---YSLSGGERRRVEIARALATN 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:COG1137   155 PKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPE 221
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
5-237 4.14e-36

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 136.88  E-value: 4.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFdghpLGVETPAQAR--ELGIA 82
Cdd:PRK13536   42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV----LGVPVPARARlaRARIG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQhfalFDTL----SVTEN-VALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKL 157
Cdd:PRK13536  118 VVPQ----FDNLdlefTVRENlLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMI---G 234
Cdd:PRK13536  194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQVIeiyG 273

                  ...
gi 2549828669 235 NDP 237
Cdd:PRK13536  274 GDP 276
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
1-238 6.80e-36

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 134.76  E-value: 6.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGIT--ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARE 78
Cdd:PRK13635    2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  79 LgIAMVHQH-FALFDTLSVTENVALGL-STGISAAE-IER---EIRLLGEKYGLEVDPASvvmeLSMGERQRVEILRALM 152
Cdd:PRK13635   82 Q-VGMVFQNpDNQFVGATVQDDVAFGLeNIGVPREEmVERvdqALRQVGMEDFLNREPHR----LSGGQKQRVAIAGVLA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRElADRCVVLRAGKVVASVDPKAESEENLARL 231
Cdd:PRK13635  157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQ 235

                  ....*..
gi 2549828669 232 MIGNDPP 238
Cdd:PRK13635  236 EIGLDVP 242
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
2-215 7.03e-36

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 139.82  E-value: 7.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   2 TPRLSLRNITKRYPG-----------ITANDHVSLDIAPGEVLAILGENGAGKSTL----MKIIygaarPDEGEISFDGH 66
Cdd:COG4172   273 PPLLEARDLKVWFPIkrglfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQ 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  67 PLGVETPAQAREL--GIAMVHQH-FALFDT-LSVTENVALGLST---GISAAEIEREIRLLGEKYGLevDPASvvM---- 135
Cdd:COG4172   348 DLDGLSRRALRPLrrRMQVVFQDpFGSLSPrMTVGQIIAEGLRVhgpGLSAAERRARVAEALEEVGL--DPAA--Rhryp 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 136 -ELSMGERQRVEILRALMTKPKLLILDEPTSVL--TPQA-VRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRA 211
Cdd:COG4172   424 hEFSGGQRQRIAIARALILEPKLLVLDEPTSALdvSVQAqILDLLRDLQR--EHGLAYLFISHDLAVVRALAHRVMVMKD 501

                  ....
gi 2549828669 212 GKVV 215
Cdd:COG4172   502 GKVV 505
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
5-471 9.32e-36

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: 139.55  E-value: 9.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYG--AARPDEGEI----------------SFDGH 66
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpSKVGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  67 PLGV------------------ETPAQARELGIaMVHQHFALFDTLSVTENVALGL-STGISAAE-IEREIRLLgEKYGL 126
Cdd:TIGR03269  81 PCPVcggtlepeevdfwnlsdkLRRRIRKRIAI-MLQRTFALYGDDTVLDNVLEALeEIGYEGKEaVGRAVDLI-EMVQL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 127 EVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQL-SSEGVSILFISHKLDEIRELADR 205
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSDK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 206 CVVLRAGKVVASVDPkaesEENLARLMIGNDPPTvREGTAKAGEVVFEMRHVsapgSTRVCGI--------DNVSLAVRA 277
Cdd:TIGR03269 239 AIWLENGEIKEEGTP----DEVVAVFMEGVSEVE-KECEVEVGEPIIKVRNV----SKRYISVdrgvvkavDNVSLEVKE 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 278 GEIVGIAGISGNGQ---ARFMAA----ASGEYLCE-ADRVLLFNSPVGELDTHARRISGLRYVPEQRLGHAAVPElSLTA 349
Cdd:TIGR03269 310 GEIFGIVGTSGAGKttlSKIIAGvlepTSGEVNVRvGDEWVDMTKPGPDGRGRAKRYIGILHQEYDLYPHRTVLD-NLTE 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 350 NTYLT-GDSLVRSGFILRDRARSFANLVIERFHVKTPNaekaagSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGA 428
Cdd:TIGR03269 389 AIGLElPDELARMKAVITLKMVGFDEEKAEEILDKYPD------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPIT 462
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 2549828669 429 AAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:TIGR03269 463 KVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
2-214 1.35e-35

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 136.23  E-value: 1.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   2 TPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARElgI 81
Cdd:PRK09452   12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENRH--V 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQHFALFDTLSVTENVALGLS-TGISAAEIE-------REIRLlgEKYGlEVDPAsvvmELSMGERQRVEILRALMT 153
Cdd:PRK09452   89 NTVFQSYALFPHMTVFENVAFGLRmQKTPAAEITprvmealRMVQL--EEFA-QRKPH----QLSGGQQQRVAIARAVVN 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK09452  162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
4-216 2.87e-35

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: 131.17  E-value: 2.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYPG--ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGI 81
Cdd:cd03245     2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-NI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQHFALFDTlSVTENVALGlSTGISAAEIEREIRLLG-------EKYGLEVDPASVVMELSMGERQRVEILRALMTK 154
Cdd:cd03245    81 GYVPQDVTLFYG-TLRDNITLG-APLADDERILRAAELAGvtdfvnkHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSeGVSILFISHKLdEIRELADRCVVLRAGKVVA 216
Cdd:cd03245   159 PPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRP-SLLDLVDRIIVMDSGRIVA 218
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
1-270 2.99e-35

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 133.78  E-value: 2.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgvetPAQARE-- 78
Cdd:PRK13537    4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARHar 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  79 LGIAMVHQHFALFDTLSVTENV-ALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKL 157
Cdd:PRK13537   80 QRVGVVPQFDNLDPDFTVRENLlVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA--ESEENLARLMI-G 234
Cdd:PRK13537  160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAliESEIGCDVIEIyG 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2549828669 235 NDPPTVREGTAKAGEvvfemrHVSAPGSTRVCGIDN 270
Cdd:PRK13537  240 PDPVALRDELAPLAE------RTEISGETLFCYVRD 269
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
3-230 3.47e-35

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 132.20  E-value: 3.47e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ-ARELgi 81
Cdd:PRK13548    1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElARRR-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQHFAL-FDtLSVTENVALGLST-GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALM------T 153
Cdd:PRK13548   79 AVLPQHSSLsFP-FTVEEVVAMGRAPhGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASvDPKAE--SEENLAR 230
Cdd:PRK13548  158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVAD-GTPAEvlTPETLRR 236
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
6-215 7.35e-35

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 129.68  E-value: 7.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   6 SLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgvetPAQARELGIAMV 84
Cdd:cd03226     1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI----KAKERRKSIGYV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQH--FALFdTLSVTENVALGL-STGISAAEIEREIRLLGEKYGLEVDPASvvmeLSMGERQRVEILRALMTKPKLLILD 161
Cdd:cd03226    77 MQDvdYQLF-TDSVREELLLGLkELDAGNEQAETVLKDLDLYALKERHPLS----LSGGQKQRLAIAAALLSGKDLLIFD 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 162 EPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:cd03226   152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
7-209 7.46e-35

putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 129.66  E-value: 7.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   7 LRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL---GIAM 83
Cdd:TIGR03608   1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFrreKLGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 VHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDE 162
Cdd:TIGR03608  81 LFQNFALIENETVEENLDLGLKyKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2549828669 163 PTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLdEIRELADRCVVL 209
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRVIEL 206
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
9-216 2.68e-34

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


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 128.64  E-value: 2.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   9 NITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARElGIAMVHQHF 88
Cdd:cd03265     5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVRR-RIGIVFQDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  89 ALFDTLSVTENVAL-GLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVL 167
Cdd:cd03265    83 SVDDELTGWENLYIhARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2549828669 168 TPQAVRKLFKTLHQL-SSEGVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:cd03265   163 DPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIA 212
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
4-215 3.29e-34

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: 135.61  E-value: 3.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYPG--ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGI 81
Cdd:TIGR02203 330 DVEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRR-QV 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQHFALFDTlSVTENVALGLSTGISAAEIEREIRLLGEK-------YGLEVDPASVVMELSMGERQRVEILRALMTK 154
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYGRTEQADRAEIERALAAAYAQdfvdklpLGLDTPIGENGVLLSGGQRQRLAIARALLKD 487
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIrELADRCVVLRAGKVV 215
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTI-EKADRIVVMDDGRIV 546
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
1-215 3.83e-34

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 131.01  E-value: 3.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPG-----------ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLG 69
Cdd:COG4608     4 AEPLLEVRDLKKHFPVrgglfgrtvgvVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDIT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  70 VETPAQAREL--GIAMVHQH-FALFDT-LSVTENVALGL--STGISAAEIEREIRLLGEKYGLEVD-----PAsvvmELS 138
Cdd:COG4608    84 GLSGRELRPLrrRMQMVFQDpYASLNPrMTVGDIIAEPLriHGLASKAERRERVAELLELVGLRPEhadryPH----EFS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 139 MGERQRVEILRALMTKPKLLILDEPTSVL--TPQA-VRKLFKTLHQlssE-GVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:COG4608   160 GGQRQRIGIARALALNPKLIVCDEPVSALdvSIQAqVLNLLEDLQD---ElGLTYLFISHDLSVVRHISDRVAVMYLGKI 236

                  .
gi 2549828669 215 V 215
Cdd:COG4608   237 V 237
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
5-217 5.37e-34

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: 127.31  E-value: 5.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGeVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlGVETPAQARELgIAMV 84
Cdd:cd03264     1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD-VLKQPQKLRRR-IGYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVA-LGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03264    78 PQEFGVYPNFTVREFLDyIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 164 TSVLTPqAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:cd03264   158 TAGLDP-EERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-215 6.49e-34

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 128.07  E-value: 6.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:PRK11614    2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVALGlstGISAAE------IEREIRLLGEKYGLEVDPASVvmeLSMGERQRVEILRALMTK 154
Cdd:PRK11614   82 VAIVPEGRRVFSRMTVEENLAMG---GFFAERdqfqerIKWVYELFPRLHERRIQRAGT---MSGGEQQMLAIGRALMSQ 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK11614  156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
2-221 1.35e-33

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 128.18  E-value: 1.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   2 TPRLSLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARE- 78
Cdd:PRK13632    5 SVMIKVENVSFSYPNSENNalKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKk 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  79 LGIamVHQH-FALFDTLSVTENVALGLSTG-ISAAEIEREIRLLGEKYG----LEVDPASvvmeLSMGERQRVEILRALM 152
Cdd:PRK13632   85 IGI--IFQNpDNQFIGATVEDDIAFGLENKkVPPKKMKDIIDDLAKKVGmedyLDKEPQN----LSGGQKQRVAIASVLA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGV-SILFISHKLDEIReLADRCVVLRAGKVVASVDPK 221
Cdd:PRK13632  159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPK 227
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
1-221 2.95e-33

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 129.96  E-value: 2.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARelg 80
Cdd:PRK11607   16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP--- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVALGLSTG-ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLI 159
Cdd:PRK11607   93 INMMFQSYALFPHMTVEQNIAFGLKQDkLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 160 LDEPTSVLTPQAVRKL-FKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:PRK11607  173 LDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
9-214 5.24e-33

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 128.66  E-value: 5.24e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   9 NITKRYpGITA--NDhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgveTPAQARELGIAMVHQ 86
Cdd:PRK10851    7 NIKKSF-GRTQvlND-ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDRKVGFVFQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  87 HFALFDTLSVTENVALGLST-----GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILD 161
Cdd:PRK10851   82 HYALFRHMTVFDNIAFGLTVlprreRPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 162 EPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK10851  162 EPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
3-209 6.72e-33

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: 131.25  E-value: 6.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYPGIT-ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGI 81
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-QI 398
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQHFALFDTlSVTENVALGLStGISAAEIEREIRL---------LGEKYGLEVDPASVvmELSMGERQRVEILRALM 152
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLARP-DASDAEIREALERagldefvaaLPQGLDTPIGEGGA--GLSGGQAQRLALARAFL 474
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLdEIRELADRCVVL 209
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRL-ALAALADRIVVL 529
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
5-216 8.18e-33

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: 124.14  E-value: 8.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPgiTANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAqarELGIAMV 84
Cdd:cd03298     1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA---DRPVSML 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVALGLSTGISAAEIERE-IRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03298    76 FQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEP 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 164 TSVLTP---QAVRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:cd03298   156 FAALDPalrAEMLDLVLDLHA--ETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
5-215 8.73e-33

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: 124.91  E-value: 8.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAR-ELGI 81
Cdd:cd03252     1 ITFEHVRFRYKPDGPVilDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRrQVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMvhQHFALFDTlSVTENVALGlSTGISAAEIEREIRLLG---------EKYGLEVDPASVvmELSMGERQRVEILRALM 152
Cdd:cd03252    81 VL--QENVLFNR-SIRDNIALA-DPGMSMERVIEAAKLAGahdfiselpEGYDTIVGEQGA--GLSGGQRQRIAIARALI 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSeGVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:cd03252   155 HNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIV 215
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
1-241 9.99e-33

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 125.49  E-value: 9.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:PRK11300    2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTEN--VA--LGLSTGISA----------AE---IEREIRLLgEKYGLEVDPASVVMELSMGERQ 143
Cdd:PRK11300   82 VVRTFQHVRLFREMTVIENllVAqhQQLKTGLFSgllktpafrrAEseaLDRAATWL-ERVGLLEHANRQAGNLAYGQQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 144 RVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:PRK11300  161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
                         250
                  ....*....|....*....
gi 2549828669 223 eseenlarlmIGNDPPTVR 241
Cdd:PRK11300  241 ----------IRNNPDVIK 249
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
2-223 2.62e-32

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 123.31  E-value: 2.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   2 TPRLSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGV---ETPA 74
Cdd:COG4181     6 APIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldeDARA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  75 QARELGIAMVHQHFALFDTLSVTENVALGLS-TGISAAEiEREIRLLgEKYGLE--VD--PAsvvmELSMGERQRVEILR 149
Cdd:COG4181    86 RLRARHVGFVFQSFQLLPTLTALENVMLPLElAGRRDAR-ARARALL-ERVGLGhrLDhyPA----QLSGGEQQRVALAR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 150 ALMTKPKLLILDEPTSVL---TPQAVRKLFKTLHQLSseGVSILFISHklDEirELADRC---VVLRAGKVVASVDPKAE 223
Cdd:COG4181   160 AFATEPAILFADEPTGNLdaaTGEQIIDLLFELNRER--GTTLVLVTH--DP--ALAARCdrvLRLRAGRLVEDTAATAA 233
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
7-215 3.56e-32

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: 123.42  E-value: 3.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   7 LRNITKRYP---GITANDHVSLDIAPGEVLAILGENGAGKSTLMKII---YGaarPDEGEISFDGHPLGVETPAQARELg 80
Cdd:cd03249     3 FKNVSFRYPsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfYD---PTSGEILLDGVDIRDLNLRWLRSQ- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTlSVTENVALGLSTGIS--------AAEIEREIRLLGEKYGLEVDPASVvmELSMGERQRVEILRALM 152
Cdd:cd03249    79 IGLVSQEPVLFDG-TIAENIRYGKPDATDeeveeaakKANIHDFIMSLPDGYDTLVGERGS--QLSGGQKQRIAIARALL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:cd03249   156 RNPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
23-217 4.46e-32

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 126.14  E-value: 4.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL-----GVETPAQARELGiaMVHQHFALFDTLSVT 97
Cdd:PRK11144   17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaekGICLPPEKRRIG--YVFQDARLFPHYKVR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  98 ENVALGLStGISAAEIEREIRLLGEKYGLEVDPASvvmeLSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFK 177
Cdd:PRK11144   95 GNLRYGMA-KSMVAQFDKIVALLGIEPLLDRYPGS----LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2549828669 178 TLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:PRK11144  170 YLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAF 210
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
1-217 6.94e-32

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 123.11  E-value: 6.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISF---DGHPLGVETPAQAR 77
Cdd:PRK11701    3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEAE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  78 -------ELGIamVHQHfalfdtlsvtenVALGLSTGISA-AEIEREIRLLGEK-YG------------LEVDPASV--- 133
Cdd:PRK11701   83 rrrllrtEWGF--VHQH------------PRDGLRMQVSAgGNIGERLMAVGARhYGdiratagdwlerVEIDAARIddl 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 134 VMELSMGERQRVEILRALMTKPKLLILDEPTSVL--TPQAvrKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLR 210
Cdd:PRK11701  149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLdvSVQA--RLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMK 226

                  ....*..
gi 2549828669 211 AGKVVAS 217
Cdd:PRK11701  227 QGRVVES 233
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
6-215 1.46e-31

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 124.04  E-value: 1.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   6 SLRNITKR-YPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHplgveTPAQ-----AREL 79
Cdd:COG4586    23 ALKGLFRReYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY-----VPFKrrkefARRI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  80 GIAM-----VHQHFALFDTLSVtenvaLGLSTGISAAEIEREIRLLGEKygLEVDP--ASVVMELSMGERQRVEILRALM 152
Cdd:COG4586    98 GVVFgqrsqLWWDLPAIDSFRL-----LKAIYRIPDAEYKKRLDELVEL--LDLGEllDTPVRQLSLGQRMRCELAAALL 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 153 TKPKLLILDEPT---SVLTPQAVRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:COG4586   171 HRPKILFLDEPTiglDVVSKEAIREFLKEYNR--ERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
5-215 2.24e-31

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: 120.80  E-value: 2.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIA 82
Cdd:cd03251     1 VEFKNVTFRYPGDGPPvlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-IG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTlSVTENVALGLStGISAAEIEREIRL---------LGEKYGLEVDPASVvmELSMGERQRVEILRALMT 153
Cdd:cd03251    80 LVSQDVFLFND-TVAENIAYGRP-GATREEVEEAARAanahefimeLPEGYDTVIGERGV--KLSGGQRQRIAIARALLK 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:cd03251   156 DPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIV 215
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
5-221 3.63e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 121.72  E-value: 3.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPA--QARE-LG 80
Cdd:PRK13639    2 LETRDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKtVG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTlSVTENVALG-LSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLI 159
Cdd:PRK13639   82 IVFQNPDDQLFAP-TVEEDVAFGpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:PRK13639  161 LDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
5-216 6.30e-31

lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 119.38  E-value: 6.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYP----GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDG---HPLGVETPAQAR 77
Cdd:TIGR02211   2 LKCENLGKRYQegklDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGqslSKLSSNERAKLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  78 ELGIAMVHQHFALFDTLSVTENVALGLSTG-ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPK 156
Cdd:TIGR02211  82 NKKLGFIYQFHHLLPDFTALENVAMPLLIGkKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELaDRCVVLRAGKVVA 216
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRElNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
5-214 6.40e-31

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: 117.70  E-value: 6.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIA 82
Cdd:cd03246     1 LEVENVSFRYPGAEPPvlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-VG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTlSVTENValglstgisaaeiereirllgekyglevdpasvvmeLSMGERQRVEILRALMTKPKLLILDE 162
Cdd:cd03246    80 YLPQDDELFSG-SIAENI------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 163 PTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLdEIRELADRCVVLRAGKV 214
Cdd:cd03246   123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
5-222 1.52e-30

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 121.75  E-value: 1.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARElgIAMV 84
Cdd:PRK11432    7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRD--ICMV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVALGLST-GISAAEIEREIrllgeKYGLE-VDPASV----VMELSMGERQRVEILRALMTKPKLL 158
Cdd:PRK11432   84 FQSYALFPHMSLGENVGYGLKMlGVPKEERKQRV-----KEALElVDLAGFedryVDQISGGQQQRVALARALILKPKVL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:PRK11432  159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
35-226 2.30e-30

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 120.68  E-value: 2.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  35 ILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARelGIAMVHQHFALFDTLSVTENVALGLST-GISAAEI 113
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-TNVPPHLR--HINMVFQSYALFPHMTVEENVAFGLKMrKVPRAEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 114 EREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLT----PQAVRKLFKTLHQLsseGVSI 189
Cdd:TIGR01187  78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQL---GITF 154
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2549828669 190 LFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEE 226
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
5-215 2.58e-30

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 118.19  E-value: 2.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVET---PAQAREL-- 79
Cdd:COG4161     3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQkpsEKAIRLLrq 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  80 GIAMVHQHFALFDTLSVTENV------ALGLStgiSAAEIEREIRLLGEkygLEVDPASVV--MELSMGERQRVEILRAL 151
Cdd:COG4161    83 KVGMVFQQYNLWPHLTVMENLieapckVLGLS---KEQAREKAMKLLAR---LRLTDKADRfpLHLSGGQQQRVAIARAL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:COG4161   157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
5-214 3.29e-30

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 120.72  E-value: 3.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPG-ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAqarELGIAM 83
Cdd:PRK11650    4 LKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA---DRDIAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 VHQHFALFDTLSVTENVALGLST-GISAAEIEREI----RLLG-EKYgLEVDPAsvvmELSMGERQRVEILRALMTKPKL 157
Cdd:PRK11650   81 VFQNYALYPHMSVRENMAYGLKIrGMPKAEIEERVaeaaRILElEPL-LDRKPR----ELSGGQRQRVAMGRAIVREPAV 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 158 LILDEPTSVLTPQ---AVRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK11650  156 FLFDEPLSNLDAKlrvQMRLEIQRLHR--RLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
5-228 4.32e-30

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 118.26  E-value: 4.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKR-YPGiTAN-----DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARE 78
Cdd:COG1101     2 LELKNLSKTfNPG-TVNekralDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEYKRA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  79 LGIAMVHQhfalfD-------TLSVTENVAL--------GLSTGISAAEIER---EIRLLGekYGLEVDPASVVMELSMG 140
Cdd:COG1101    80 KYIGRVFQ-----DpmmgtapSMTIEENLALayrrgkrrGLRRGLTKKRRELfreLLATLG--LGLENRLDTKVGLLSGG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 141 ERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVasVD 219
Cdd:COG1101   153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEEnNLTTLMVTHNMEQALDYGNRLIMMHEGRII--LD 230

                  ....*....
gi 2549828669 220 PKAESEENL 228
Cdd:COG1101   231 VSGEEKKKL 239
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
7-222 4.54e-30

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 117.93  E-value: 4.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   7 LRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEG-----EISFDG-HPLGvETPAQAREL- 79
Cdd:PRK11264    6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTaRSLS-QQKGLIRQLr 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  80 -GIAMVHQHFALFDTLSVTENVALG--LSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPK 156
Cdd:PRK11264   85 qHVGFVFQNFNLFPHRTVLENIIEGpvIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPE 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:PRK11264  165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
6-216 9.70e-30

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


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 116.66  E-value: 9.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   6 SLRNITKR-YPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAMv 84
Cdd:cd03267    22 SLKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVF- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVALGLST-GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03267   101 GQKTQLWWDLPVIDSFYLLAAIyDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 164 TSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:cd03267   181 TIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
5-211 1.33e-29

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 115.27  E-value: 1.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPD---EGEISFDGHPLGvETPAQARELGI 81
Cdd:COG4136     2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLT-ALPAEQRRIGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMvhQHFALFDTLSVTENVALGLSTGISAAEIEREIRLLGEKYGL----EVDPAsvvmELSMGERQRVEILRALMTKPKL 157
Cdd:COG4136    81 LF--QDDLLFPHLSVGENLAFALPPTIGRAQRRARVEQALEEAGLagfaDRDPA----TLSGGQRARVALLRALLAEPRA 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 158 LILDEPTSVLTP---QAVRKL-FKTLHQLsseGVSILFISHKLDEIrELADRCVVLRA 211
Cdd:COG4136   155 LLLDEPFSKLDAalrAQFREFvFEQIRQR---GIPALLVTHDEEDA-PAAGRVLDLGN 208
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
1-221 1.40e-29

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 116.33  E-value: 1.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYP----------------------GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDE 58
Cdd:COG1134     1 MSSMIEVENVSKSYRlyhepsrslkelllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  59 GEISFDGH---PLgvetpaqarELGIAMVHQhfalfdtLSVTENVAL-GLSTGISAAEIER---EIRL---LGEKygleV 128
Cdd:COG1134    81 GRVEVNGRvsaLL---------ELGAGFHPE-------LTGRENIYLnGRLLGLSRKEIDEkfdEIVEfaeLGDF----I 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 129 D-PasvVMELSMGERQRveiLR---ALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELAD 204
Cdd:COG1134   141 DqP---VKTYSSGMRAR---LAfavATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCD 214
                         250
                  ....*....|....*..
gi 2549828669 205 RCVVLRAGKVVASVDPK 221
Cdd:COG1134   215 RAIWLEKGRLVMDGDPE 231
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
5-212 1.63e-29

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 116.34  E-value: 1.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlgVETPAQARelgiAMV 84
Cdd:PRK11248    2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP--VEGPGAER----GVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:PRK11248   76 FQNEGLLPWRNVQDNVAFGLQlAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 164 TSVL---TPQAVRKLFKTLHQLSseGVSILFISHKLDEIRELADRCVVLRAG 212
Cdd:PRK11248  156 FGALdafTREQMQTLLLKLWQET--GKQVLLITHDIEEAVFMATELVLLSPG 205
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
5-215 2.39e-29

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 115.50  E-value: 2.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVET---PAQAREL-- 79
Cdd:PRK11124    3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKtpsDKAIRELrr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  80 GIAMVHQHFALFDTLSVTENV------ALGLStgiSAAEIEREIRLLgEKYGLEVDPASVVMELSMGERQRVEILRALMT 153
Cdd:PRK11124   83 NVGMVFQQYNLWPHLTVQQNLieapcrVLGLS---KDQALARAEKLL-ERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK11124  159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
4-222 4.32e-29

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 115.45  E-value: 4.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGH----------PLGVETP 73
Cdd:PRK10619    5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgQLKVADK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  74 AQARELG--IAMVHQHFALFDTLSVTENV------ALGLStgiSAAEIEREIRLLgEKYGL-EVDPASVVMELSMGERQR 144
Cdd:PRK10619   85 NQLRLLRtrLTMVFQHFNLWSHMTVLENVmeapiqVLGLS---KQEARERAVKYL-AKVGIdERAQGKYPVHLSGGQQQR 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 145 VEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:PRK10619  161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
4-215 5.69e-29

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 113.03  E-value: 5.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYPGITANDH------VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARP--DEGEISFDGHPLGVETPAQ 75
Cdd:cd03213     3 TLSFRNLTVTVKSSPSKSGkqllknVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  76 ArelgIAMVHQHFALFDTLSVTENVALglstgisAAEIEReirllgekyglevdpasvvmeLSMGERQRVEILRALMTKP 155
Cdd:cd03213    83 I----IGYVPQDDILHPTLTVRETLMF-------AAKLRG---------------------LSGGERKRVSIALELVSNP 130
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 156 KLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKL-DEIRELADRCVVLRAGKVV 215
Cdd:cd03213   131 SLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
3-221 5.76e-29

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: 119.91  E-value: 5.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYPG-----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISF-------DGHPLGV 70
Cdd:TIGR03269 278 PIIKVRNVSKRYISvdrgvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvDMTKPGP 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  71 ETPAQARELgIAMVHQHFALFDTLSVTENV--ALGLSTGISAAEIEREIRL----LGEKYGLEVDPaSVVMELSMGERQR 144
Cdd:TIGR03269 358 DGRGRAKRY-IGILHQEYDLYPHRTVLDNLteAIGLELPDELARMKAVITLkmvgFDEEKAEEILD-KYPDELSEGERHR 435
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 145 VEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
5-219 7.90e-29

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: 114.90  E-value: 7.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPG---------ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ 75
Cdd:TIGR02769   3 LEVRDVTHTYRTgglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  76 AREL--GIAMVHQ--HFALFDTLSVTENVALGLS--TGISAAEIEREIRLLGEKYGLEVDPAS-VVMELSMGERQRVEIL 148
Cdd:TIGR02769  83 RRAFrrDVQLVFQdsPSAVNPRMTVRQIIGEPLRhlTSLDESEQKARIAELLDMVGLRSEDADkLPRQLSGGQLQRINIA 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 149 RALMTKPKLLILDEPTS----VLTPQAVRkLFKTLHQLSseGVSILFISHKLDEIRELADRCVVLRAGKVVASVD 219
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSnldmVLQAVILE-LLRKLQQAF--GTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECD 234
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
5-217 9.78e-29

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: 112.02  E-value: 9.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPG--ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlgVETPAQARELGIA 82
Cdd:cd03247     1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP--VSDLEKALSSLIS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTlSVTENvalglstgisaaeiereirlLGEKyglevdpasvvmeLSMGERQRVEILRALMTKPKLLILDE 162
Cdd:cd03247    79 VLNQRPYLFDT-TLRNN--------------------LGRR-------------FSGGERQRLALARILLQDAPIVLLDE 124
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 163 PTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIrELADRCVVLRAGKVVAS 217
Cdd:cd03247   125 PTVGLDPITERQLLSLIFEV-LKDKTLIWITHHLTGI-EHMDKILFLENGKIIMQ 177
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
7-290 1.19e-28

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 119.01  E-value: 1.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   7 LRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFdghplgvetPAQARelgIAMVHQ 86
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLR---IGYLPQ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  87 HFALFDTLSVTENVALGLStgiSAAEIEREIRLLGEKY----------------------------------GL---EVD 129
Cdd:COG0488    69 EPPLDDDLTVLDTVLDGDA---ELRALEAELEELEAKLaepdedlerlaelqeefealggweaearaeeilsGLgfpEED 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 130 PASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSegvSILFISHKLDEIRELADRCVVL 209
Cdd:COG0488   146 LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG---TVLVVSHDRYFLDRVATRILEL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 210 RAGKVV-------ASVDPKAESEEN-----------LARL--------------------------MIGNDPPtVREGTA 245
Cdd:COG0488   223 DRGKLTlypgnysAYLEQRAERLEQeaaayakqqkkIAKEeefirrfrakarkakqaqsrikalekLEREEPP-RRDKTV 301
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 246 K--------AGEVVFEMRHVS-APGSTRVcgIDNVSLAVRAGEIVGIAGISGNG 290
Cdd:COG0488   302 EirfppperLGKKVLELEGLSkSYGDKTL--LDDLSLRIDRGDRIGLIGPNGAG 353
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
21-212 1.37e-28

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: 113.33  E-value: 1.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlgVETPAQARelgiAMVHQHFALFDTLSVTENV 100
Cdd:TIGR01184   2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQ--ITEPGPDR----MVVFQNYSLLPWLTVRENI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 ALG-------LSTGISAAEIEREIRLLGEKYGLEVDPAsvvmELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVR 173
Cdd:TIGR01184  76 ALAvdrvlpdLSKSERRAIVEEHIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2549828669 174 KLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAG 212
Cdd:TIGR01184 152 NLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
5-215 1.75e-28

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: 113.09  E-value: 1.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRY-PGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIAM 83
Cdd:cd03253     1 IEFENVTFAYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRR-AIGV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 VHQHFALFDTlSVTENVALG--------LSTGISAAEIEREIRLLGEKYglevdpASVVME----LSMGERQRVEILRAL 151
Cdd:cd03253    80 VPQDTVLFND-TIGYNIRYGrpdatdeeVIEAAKAAQIHDKIMRFPDGY------DTIVGErglkLSGGEKQRVAIARAI 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:cd03253   153 LKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
1-212 1.99e-28

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: 112.53  E-value: 1.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITK----------RYPGItanDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDgHPLGV 70
Cdd:COG4778     1 MTTLLEVENLSKtftlhlqggkRLPVL---DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGW 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  71 ETPAQA--------RELGIAMVHQHfalfdtLSV-----TENV---ALgLSTGISAAEIEREIRLLGEKYGL-----EVD 129
Cdd:COG4778    77 VDLAQAspreilalRRRTIGYVSQF------LRViprvsALDVvaePL-LERGVDREEARARARELLARLNLperlwDLP 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 130 PASvvmeLSMGERQRVEILRALMTKPKLLILDEPTSVLTP---QAVRKLfktLHQLSSEGVSILFISHKLDEIRELADRC 206
Cdd:COG4778   150 PAT----FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAanrAVVVEL---IEEAKARGTAIIGIFHDEEVREAVADRV 222

                  ....*.
gi 2549828669 207 VVLRAG 212
Cdd:COG4778   223 VDVTPF 228
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
5-215 2.04e-28

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 112.75  E-value: 2.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITAndHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQaRElgIAMV 84
Cdd:PRK10771    2 LKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR-RP--VSML 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVALGLSTGIS-AAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:PRK10771   77 FQENNLFSHLTVAQNIGLGLNPGLKlNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEP 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 164 TSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK10771  157 FSALDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
23-215 4.58e-28

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 117.50  E-value: 4.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKST----LMKIIygaarPDEGEISFDGHPLGVETPAQAREL--GIAMVHQ--HFALFDTL 94
Cdd:PRK15134  305 ISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVrhRIQVVFQdpNSSLNPRL 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  95 SVTENVALGLST---GISAAEIEREIRLLGEKYGLevDPAS---VVMELSMGERQRVEILRALMTKPKLLILDEPTSVL- 167
Cdd:PRK15134  380 NVLQIIEEGLRVhqpTLSAAQREQQVIAVMEEVGL--DPETrhrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLd 457
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2549828669 168 -TPQA-VRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK15134  458 kTVQAqILALLKSLQQ--KHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
4-235 4.93e-28

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 117.03  E-value: 4.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKryPGItanDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAM 83
Cdd:PRK10762  257 RLKVDNLSG--PGV---NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVY 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 V---HQHFALFDTLSVTENVALGLSTGIS--------AAE---IEREIRLLGEKyglevDPA--SVVMELSMGERQRVEI 147
Cdd:PRK10762  332 IsedRKRDGLVLGMSVKENMSLTALRYFSraggslkhADEqqaVSDFIRLFNIK-----TPSmeQAIGLLSGGNQQKVAI 406
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 148 LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEEN 227
Cdd:PRK10762  407 ARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQEK 486

                  ....*...
gi 2549828669 228 LARLMIGN 235
Cdd:PRK10762  487 LMAAAVGK 494
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
4-215 1.17e-27

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: 110.39  E-value: 1.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRY-PGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIA 82
Cdd:cd03254     2 EIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM-IG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTlSVTENVALGLSTgISAAEIEREIRLLGEKYGLEVDP---ASVVME----LSMGERQRVEILRALMTKP 155
Cdd:cd03254    81 VVLQDTFLFSG-TIMENIRLGRPN-ATDEEVIEAAKEAGAHDFIMKLPngyDTVLGEnggnLSQGERQLLAIARAMLRDP 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 156 KLLILDEPTSVLTP-------QAVRKLFKtlhqlsseGVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:cd03254   159 KILILDEATSNIDTetekliqEALEKLMK--------GRTSIIIAHRLSTIKN-ADKILVLDDGKII 216
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-222 1.31e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 111.75  E-value: 1.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITAN---DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAR 77
Cdd:PRK13650    1 MSNIIEVKNLTFKYKEDQEKytlNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  78 ELgIAMVHQH-FALFDTLSVTENVALGL-STGISAAE----IEREIRLLGEKYGLEVDPAsvvmELSMGERQRVEILRAL 151
Cdd:PRK13650   81 HK-IGMVFQNpDNQFVGATVEDDVAFGLeNKGIPHEEmkerVNEALELVGMQDFKEREPA----RLSGGQKQRVAIAGAV 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIrELADRCVVLRAGKVVASVDPKA 222
Cdd:PRK13650  156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRE 226
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
23-220 1.48e-27

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 110.54  E-value: 1.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYG--AARPDEGEISFDGHPLGVETPAQ-AReLGIAMVHQHFALFDTLSVTE- 98
Cdd:COG0396    19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILELSPDErAR-AGIFLAFQYPVEIPGVSVSNf 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  99 -NVALGLSTG--ISAAEIEREIRLLGEKYGLEVDPA--SVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVR 173
Cdd:COG0396    98 lRTALNARRGeeLSAREFLKLLKEKMKELGLDEDFLdrYVNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALR 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2549828669 174 KLFKTLHQLSSEGVSILFISHK---LDEIRelADRCVVLRAGKVVASVDP 220
Cdd:COG0396   178 IVAEGVNKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDGRIVKSGGK 225
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
5-221 1.50e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 111.86  E-value: 1.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPA--QARElGI 81
Cdd:PRK13636    6 LKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRE-SV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQH--FALFdTLSVTENVALG-LSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLL 158
Cdd:PRK13636   85 GMVFQDpdNQLF-SASVYQDVSFGaVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:PRK13636  164 VLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
13-209 1.69e-27

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 108.86  E-value: 1.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  13 RYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEIsfdghplgvetpAQARELGIAMVHQHFALFD 92
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGARVAYVPQRSEVPD 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  93 TLSVT--ENVALGL---------STGISAAEIEREIRLLGEKyGLEVDPASvvmELSMGERQRVEILRALMTKPKLLILD 161
Cdd:NF040873   69 SLPLTvrDLVAMGRwarrglwrrLTRDDRAAVDDALERVGLA-DLAGRQLG---ELSGGQRQRALLAQGLAQEADLLLLD 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2549828669 162 EPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIReLADRCVVL 209
Cdd:NF040873  145 EPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVR-RADPCVLL 191
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
5-215 2.51e-27

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 110.55  E-value: 2.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRY---------PGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ 75
Cdd:PRK10419    4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  76 AREL--GIAMVHQhfalfDTLS-------VTENVALGLS--TGISAAEIEREIRLLGEKYGLEVDPAS-VVMELSMGERQ 143
Cdd:PRK10419   84 RKAFrrDIQMVFQ-----DSISavnprktVREIIREPLRhlLSLDKAERLARASEMLRAVDLDDSVLDkRPPQLSGGQLQ 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 144 RVEILRALMTKPKLLILDEPTS----VLTPQAVRKLFKTLHQLsseGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK10419  159 RVCLARALAVEPKLLILDEAVSnldlVLQAGVIRLLKKLQQQF---GTACLFITHDLRLVERFCQRVMVMDNGQIV 231
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
6-214 3.56e-27

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 112.43  E-value: 3.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   6 SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAqarELGIAMVH 85
Cdd:PRK11000    5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA---ERGVGMVF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  86 QHFALFDTLSVTENVALGLS-TGISAAEIEREI----RLLGEKYGLEVDPAsvvmELSMGERQRVEILRALMTKPKLLIL 160
Cdd:PRK11000   82 QSYALYPHLSVAENMSFGLKlAGAKKEEINQRVnqvaEVLQLAHLLDRKPK----ALSGGQRQRVAIGRTLVAEPSVFLL 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 161 DEPTSVLTpQAVR--------KLFKTLhqlsseGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK11000  158 DEPLSNLD-AALRvqmrieisRLHKRL------GRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
24-214 3.74e-27

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 108.80  E-value: 3.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  24 SLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARelgIAMVHQHFALFDTLSVTENVALG 103
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP---VSMLFQENNLFAHLTVRQNIGLG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 104 LSTGISAAEIERE-IRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQL 182
Cdd:TIGR01277  95 LHPGLKLNAEQQEkVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQL 174
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2549828669 183 SSE-GVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:TIGR01277 175 CSErQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
4-232 9.08e-27

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: 113.69  E-value: 9.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYPG----ITANdhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPaqaREL 79
Cdd:COG4618   330 RLSVENLTVVPPGskrpILRG--VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR---EEL 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  80 G--IAMVHQHFALFDTlSVTENVA-LGlstGISAAEIEREIRLLG---------EKYGLEVDPASVVmeLSMGERQRVEI 147
Cdd:COG4618   405 GrhIGYLPQDVELFDG-TIAENIArFG---DADPEKVVAAAKLAGvhemilrlpDGYDTRIGEGGAR--LSGGQRQRIGL 478
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 148 LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRElADRCVVLRAGKVVAsVDPKaesEEN 227
Cdd:COG4618   479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAA-VDKLLVLRDGRVQA-FGPR---DEV 553

                  ....*
gi 2549828669 228 LARLM 232
Cdd:COG4618   554 LARLA 558
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
2-205 1.01e-26

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 107.98  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   2 TPRLSLRNITKRY-PGITAND---HVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLG-VETPAQA 76
Cdd:PRK11629    3 KILLQCDNLCKRYqEGSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSkLSSAAKA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  77 ----RELGiaMVHQHFALFDTLSVTENVALGLSTG-ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRAL 151
Cdd:PRK11629   83 elrnQKLG--FIYQFHHLLPDFTALENVAMPLLIGkKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLS-SEGVSILFISHKLdeirELADR 205
Cdd:PRK11629  161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDL----QLAKR 211
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
4-236 1.45e-26

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 107.67  E-value: 1.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVeTPAQAREL-GIA 82
Cdd:PRK10895    3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISL-LPLHARARrGIG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTLSVTENVALGLSTGISAAEIEREIRL--LGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLIL 160
Cdd:PRK10895   82 YLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRAneLMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA-ESEENLARLMIGND 236
Cdd:PRK10895  162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEiLQDEHVKRVYLGED 238
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
5-215 2.37e-26

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 112.08  E-value: 2.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFdGHplGVEtpaqarelgIAMV 84
Cdd:COG0488   316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE--TVK---------IGYF 383
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFD-TLSVTENVALGLSTGisaaeIEREIRLLGEKYGLEVD----PASVvmeLSMGERQRVEILRALMTKPKLLI 159
Cdd:COG0488   384 DQHQEELDpDKTVLDELRDGAPGG-----TEQEVRGYLGRFLFSGDdafkPVGV---LSGGEKARLALAKLLLSPPNVLL 455
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 160 LDEPTSVLTPQavrklfkTLHQLSS-----EGvSILFISHklDE--IRELADRCVVLRAGKVV 215
Cdd:COG0488   456 LDEPTNHLDIE-------TLEALEEalddfPG-TVLLVSH--DRyfLDRVATRILEFEDGGVR 508
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
21-215 2.52e-26

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: 112.61  E-value: 2.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIAMVHQHFALF-DTLSvtEN 99
Cdd:COG5265   375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA-AIGIVPQDTVLFnDTIA--YN 451
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 100 VALGlSTGISAAEIEREIRL---------LGEKYglevdpASVVME----LSMGERQRVEILRALMTKPKLLILDEPTSV 166
Cdd:COG5265   452 IAYG-RPDASEEEVEAAARAaqihdfiesLPDGY------DTRVGErglkLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 167 L---TPQAVRklfKTLHQLsSEGVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:COG5265   525 LdsrTERAIQ---AALREV-ARGRTTLVIAHRLSTIVD-ADEILVLEAGRIV 571
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
4-214 4.37e-26

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: 106.02  E-value: 4.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYPgiTANDH-----VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARE 78
Cdd:cd03248    11 IVKFQNVTFAYP--TRPDTlvlqdVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  79 LgIAMVHQHFALFdTLSVTENVALGLST--------GISAAEIEREIRLLGEKYGLEVDPASVvmELSMGERQRVEILRA 150
Cdd:cd03248    89 K-VSLVGQEPVLF-ARSLQDNIAYGLQScsfecvkeAAQKAHAHSFISELASGYDTEVGEKGS--QLSGGQKQRVAIARA 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAvRKLFKTLHQLSSEGVSILFISHKLDEIrELADRCVVLRAGKV 214
Cdd:cd03248   165 LIRNPQVLILDEATSALDAES-EQQVQQALYDWPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
23-221 7.25e-26

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: 104.53  E-value: 7.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYG--AARPDEGEISFDGHPLGVETPAQARELGIAMVHQHFALFdtlsvtenv 100
Cdd:cd03217    19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEI--------- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 alglsTGISAAEIereIRLLGEKyglevdpasvvmeLSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLH 180
Cdd:cd03217    90 -----PGVKNADF---LRYVNEG-------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVIN 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2549828669 181 QLSSEGVSILFISHK---LDEIRelADRCVVLRAGKVVASVDPK 221
Cdd:cd03217   149 KLREEGKSVLIITHYqrlLDYIK--PDRVHVLYDGRIVKSGDKE 190
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
1-215 8.49e-26

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 107.74  E-value: 8.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYP---GI-------TANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGV 70
Cdd:PRK11308    2 QQPLLQAIDLKKHYPvkrGLfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  71 ETPAQAREL--GIAMVHQHfaLFDTLSVTENVA------LGLSTGISAAEIEREIRLLGEKYGLEVDPASVV--MeLSMG 140
Cdd:PRK11308   82 ADPEAQKLLrqKIQIVFQN--PYGSLNPRKKVGqileepLLINTSLSAAERREKALAMMAKVGLRPEHYDRYphM-FSGG 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 141 ERQRVEILRALMTKPKLLILDEPTSVL--TPQA-VRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK11308  159 QRQRIAIARALMLDPDVVVADEPVSALdvSVQAqVLNLMMDLQQ--ELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
23-219 1.45e-25

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 104.57  E-value: 1.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLG----VETPAQARELGiaMVHQHFALFDTLSVTE 98
Cdd:PRK10908   21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknREVPFLRRQIG--MIFQDHHLLMDRTVYD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  99 NVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFK 177
Cdd:PRK10908   99 NVAIPLIiAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2549828669 178 TLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVD 219
Cdd:PRK10908  179 LFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVG 220
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
5-217 2.82e-25

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 108.76  E-value: 2.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRY---PGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPD-EGEISFDGHPLGVETPAQARELG 80
Cdd:TIGR02633 258 LEARNLTCWDvinPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAG 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMV---HQHFALFDTLSVTENVAL-------GLSTGISAAE---IEREIRLLGEKyglEVDPASVVMELSMGERQRVEI 147
Cdd:TIGR02633 338 IAMVpedRKRHGIVPILGVGKNITLsvlksfcFKMRIDAAAElqiIGSAIQRLKVK---TASPFLPIGRLSGGNQQKAVL 414
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 148 LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:TIGR02633 415 AKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
5-469 4.64e-25

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 108.79  E-value: 4.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRY----PGITANDHVSLDIAPGEVLAILGENGAGKS----TLMKIIYGAArpdeGEISFDGH---------- 66
Cdd:PRK10261   13 LAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAG----GLVQCDKMllrrrsrqvi 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  67 PLGVETPAQAREL---GIAMVHQH--FALFDTLSVTENVA--LGLSTGISAAEIEREIRLLGEKYGLevdPASVVM---- 135
Cdd:PRK10261   89 ELSEQSAAQMRHVrgaDMAMIFQEpmTSLNPVFTVGEQIAesIRLHQGASREEAMVEAKRMLDQVRI---PEAQTIlsry 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 136 --ELSMGERQRVEILRALMTKPKLLILDEPTSVL--TPQA-VRKLFKTLHQLSSEGVsiLFISHKLDEIRELADRCVVLR 210
Cdd:PRK10261  166 phQLSGGMRQRVMIAMALSCRPAVLIADEPTTALdvTIQAqILQLIKVLQKEMSMGV--IFITHDMGVVAEIADRVLVMY 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 211 AGKVV--ASVD------------------PK--AESEENLAR---LMIGNDP----PTVREGTAKAGEVVFEMRHVSAPG 261
Cdd:PRK10261  244 QGEAVetGSVEqifhapqhpytrallaavPQlgAMKGLDYPRrfpLISLEHPakqePPIEQDTVVDGEPILQVRNLVTRF 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 262 STR----------VCGIDNVSLAVRAGEIVGIAGISGNGQA-------RFMAAASGEYLCEADRV--------------- 309
Cdd:PRK10261  324 PLRsgllnrvtreVHAVEKVSFDLWPGETLSLVGESGSGKSttgrallRLVESQGGEIIFNGQRIdtlspgklqalrrdi 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 310 -LLFNSPVGELDtharrisglryvPEQRLGHAAVPELSLtantyltgdslvrSGFILRDRARSFANLVIERFHVKTPNAE 388
Cdd:PRK10261  404 qFIFQDPYASLD------------PRQTVGDSIMEPLRV-------------HGLLPGKAAAARVAWLLERVGLLPEHAW 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 389 KAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMY 467
Cdd:PRK10261  459 RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMY 538

                  ..
gi 2549828669 468 RG 469
Cdd:PRK10261  539 LG 540
cbiO PRK13637
energy-coupling factor transporter ATPase;
19-221 6.67e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 104.36  E-value: 6.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  19 ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL---GVETPAQARELGIAMVHQHFALFDTlS 95
Cdd:PRK13637   22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIRKKVGLVFQYPEYQLFEE-T 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  96 VTENVALGLST-GISAAEIEREIRLLGEKYGLEVD------PasvvMELSMGERQRVEILRALMTKPKLLILDEPTSVLT 168
Cdd:PRK13637  101 IEKDIAFGPINlGLSEEEIENRVKRAMNIVGLDYEdykdksP----FELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 169 PQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:PRK13637  177 PKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPR 230
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
4-216 9.54e-25

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 107.58  E-value: 9.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYPGITANDH-----VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARE 78
Cdd:COG4615   327 TLELRGVTYRYPGEDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQ 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  79 LgIAMVHQHFALFDTLsvtenvaLGLSTGISAAEIEREIRLLG--EKYGLEVDPASVVmELSMGERQRVEILRALMTKPK 156
Cdd:COG4615   407 L-FSAVFSDFHLFDRL-------LGLDGEADPARARELLERLEldHKVSVEDGRFSTT-DLSQGQRKRLALLVALLEDRP 477
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 157 LLILDE------PTsvltpqaVRKLFKT--LHQLSSEGVSILFISHklDEiR--ELADRCVVLRAGKVVA 216
Cdd:COG4615   478 ILVFDEwaadqdPE-------FRRVFYTelLPELKARGKTVIAISH--DD-RyfDLADRVLKMDYGKLVE 537
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
2-213 1.04e-24

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 102.10  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   2 TPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGI 81
Cdd:PRK10247    5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ-QV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQHFALF-DTlsVTENVALGLSTGISAAEIEREIRLLgEKYGLevdPASV----VMELSMGERQRVEILRALMTKPK 156
Cdd:PRK10247   84 SYCAQTPTLFgDT--VYDNLIFPWQIRNQQPDPAIFLDDL-ERFAL---PDTIltknIAELSGGEKQRISLIRNLQFMPK 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRElADRCVVL--RAGK 213
Cdd:PRK10247  158 VLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEINH-ADKVITLqpHAGE 216
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
12-216 2.11e-24

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: 101.07  E-value: 2.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  12 KRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGhplgveTPAQARELGIAMVhqhfalf 91
Cdd:cd03220    30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLGLGGGFN------- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  92 DTLSVTENVAL-GLSTGISAAEIEREIRL------LGEKYGLevdPasvVMELSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:cd03220    97 PELTGRENIYLnGRLLGLSRKEIDEKIDEiiefseLGDFIDL---P---VKTYSSGMKARLAFAIATALEPDILLIDEVL 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 165 SVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:cd03220   171 AVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
4-231 4.45e-24

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 104.99  E-value: 4.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKryPGITANdhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAM 83
Cdd:PRK11288  257 RLRLDGLKG--PGLREP--ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIML 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 V---HQHFALFDTLSVTENVALG-----------LSTGISAAEIEREIRLLGEKyglEVDPASVVMELSMGERQRVEILR 149
Cdd:PRK11288  333 CpedRKAEGIIPVHSVADNINISarrhhlragclINNRWEAENADRFIRSLNIK---TPSREQLIMNLSGGNQQKAILGR 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 150 ALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLA 229
Cdd:PRK11288  410 WLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQATERQAL 489

                  ..
gi 2549828669 230 RL 231
Cdd:PRK11288  490 SL 491
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
7-229 5.03e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 101.35  E-value: 5.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   7 LRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIAMVH 85
Cdd:PRK13647    7 VEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK-VGLVF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  86 QH-----FALfdtlSVTENVALG-LSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLI 159
Cdd:PRK13647   86 QDpddqvFSS----TVWDDVAFGpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLA 229
Cdd:PRK13647  162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIV 231
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
18-242 5.83e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 101.32  E-value: 5.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  18 TANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGhplgVETPAQARELGI----AMVHQH--FALF 91
Cdd:PRK13633   24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG----LDTSDEENLWDIrnkaGMVFQNpdNQIV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  92 DTLsVTENVALGLST-GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQ 170
Cdd:PRK13633  100 ATI-VEEDVAFGPENlGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 171 AVRKLFKTLHQLSSE-GVSILFISHKLDEIRElADRCVVLRAGKVVASVDPKAESEENLARLMIGNDPPTVRE 242
Cdd:PRK13633  179 GRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMKKIGLDVPQVTE 250
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
24-220 5.93e-24

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 103.57  E-value: 5.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  24 SLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL---GIAMVHQHFALFDTLSVTENV 100
Cdd:PRK10070   48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkKIAMVFQSFALMPHMTVLDNT 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 ALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTL 179
Cdd:PRK10070  128 AFGMElAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2549828669 180 HQLSSEGV-SILFISHKLDEIRELADRCVVLRAGKVVASVDP 220
Cdd:PRK10070  208 VKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
23-231 6.45e-24

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 100.30  E-value: 6.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAArPDEGEISFDGHPLG-VETPAQARELgiAMVHQHFALFDTLSVTENVA 101
Cdd:COG4138    15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSdWSAAELARHR--AYLSQQQSPPFAMPVFQYLA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 102 LGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMT-------KPKLLILDEPTSVL--TPQAV 172
Cdd:COG4138    92 LHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLdvAQQAA 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 173 rkLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAE-SEENLARL 231
Cdd:COG4138   172 --LDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVmTPENLSEV 229
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
2-238 8.39e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 100.60  E-value: 8.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   2 TPRLSLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREl 79
Cdd:PRK13648    5 NSIIVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  80 GIAMVHQHFA-LFDTLSVTENVALGLST-GISAAEIEREIRLLGEKYGL----EVDPASvvmeLSMGERQRVEILRALMT 153
Cdd:PRK13648   84 HIGIVFQNPDnQFVGSIVKYDVAFGLENhAVPYDEMHRRVSEALKQVDMleraDYEPNA----LSGGQKQRVAIAGVLAL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRElADRCVVLRAGKVVASVDPKAESEENLARLM 232
Cdd:PRK13648  160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTR 238

                  ....*.
gi 2549828669 233 IGNDPP 238
Cdd:PRK13648  239 IGLDLP 244
cbiO PRK13649
energy-coupling factor transporter ATPase;
23-221 1.06e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 100.59  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGhplgVETPAQARELGIAMVHQHFAL---------FDT 93
Cdd:PRK13649   26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDD----TLITSTSKNKDIKQIRKKVGLvfqfpesqlFEE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  94 lSVTENVALGLST-GISAAEIER----EIRLLGEKYGL-EVDPasvvMELSMGERQRVEILRALMTKPKLLILDEPTSVL 167
Cdd:PRK13649  102 -TVLKDVAFGPQNfGVSQEEAEAlareKLALVGISESLfEKNP----FELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 168 TPQAVRKL---FKTLHQlssEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:PRK13649  177 DPKGRKELmtlFKKLHQ---SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPK 230
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
23-214 1.40e-23

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 99.08  E-value: 1.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGV---ETPAQARELGIAMVHQHFALFDTLSVTEN 99
Cdd:PRK10584   29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeEARAKLRAKHVGFVFQSFMLIPTLNALEN 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 100 VAL-GLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKT 178
Cdd:PRK10584  109 VELpALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2549828669 179 LHQLSSE-GVSILFISHKlDEIRELADRCVVLRAGKV 214
Cdd:PRK10584  189 LFSLNREhGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
24-215 2.55e-23

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 103.65  E-value: 2.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  24 SLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARELGIAMVHQHFALFDTlSVTENVALG 103
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL-VQYDHHYLHRQVALVGQEPVLFSG-SVRENIAYG 578
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 104 LS--------TGISAAEIEREIRLLGEKYGLEVDPASVvmELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRkl 175
Cdd:TIGR00958 579 LTdtpdeeimAAAKAANAHDFIMEFPNGYDTEVGEKGS--QLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ-- 654
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2549828669 176 fkTLHQL-SSEGVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:TIGR00958 655 --LLQESrSRASRTVLLIAHRLSTVER-ADQILVLKKGSVV 692
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
5-215 3.26e-23

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 103.17  E-value: 3.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPG--ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIA 82
Cdd:PRK11176  342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN-QVA 420
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALF-DTlsVTENVALGLSTGISAAEIEREIRLL-------GEKYGLEvdpaSVVME----LSMGERQRVEILRA 150
Cdd:PRK11176  421 LVSQNVHLFnDT--IANNIAYARTEQYSREQIEEAARMAyamdfinKMDNGLD----TVIGEngvlLSGGQRQRIAIARA 494
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSiLFISHKLDEIrELADRCVVLRAGKVV 215
Cdd:PRK11176  495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTS-LVIAHRLSTI-EKADEILVVEDGEIV 557
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
19-215 3.61e-23

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 100.17  E-value: 3.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  19 ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL--GIAMVHQH--FALFDTL 94
Cdd:PRK15079   36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsDIQMIFQDplASLNPRM 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  95 SVTENVALGLST---GISAAEIEREIRLLGEKYGLEvdPASV---VMELSMGERQRVEILRALMTKPKLLILDEPTSVLT 168
Cdd:PRK15079  116 TIGEIIAEPLRTyhpKLSRQEVKDRVKAMMLKVGLL--PNLInryPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2549828669 169 PQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK15079  194 VSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
21-292 5.45e-23

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 102.09  E-value: 5.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  21 DHVSLDIAPGEVLAILGENGAGKS-TLMKIIYGAARPD----EGEISFDGHPLGVETPAQAREL---GIAMVHQH--FAL 90
Cdd:PRK15134   26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGVrgnKIAMIFQEpmVSL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  91 FDTLSVTENVA--LGLSTGISAAEIEREIRLLGEKYGLEvDPASVVM----ELSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:PRK15134  106 NPLHTLEKQLYevLSLHRGMRREAARGEILNCLDRVGIR-QAAKRLTdyphQLSGGERQRVMIAMALLTRPELLIADEPT 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 165 SVL--TPQAvrKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVasvdpkaesEENLARLMIG------- 234
Cdd:PRK15134  185 TALdvSVQA--QILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCV---------EQNRAATLFSapthpyt 253
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 235 ---------NDPPTVREGTAKAGEVvfEMRHVSAPGS----TRVCG----IDNVSLAVRAGEIVGIAGISGNGQA 292
Cdd:PRK15134  254 qkllnsepsGDPVPLPEPASPLLDV--EQLQVAFPIRkgilKRTVDhnvvVKNISFTLRPGETLGLVGESGSGKS 326
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
3-196 5.77e-23

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: 102.05  E-value: 5.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYPG-ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgI 81
Cdd:TIGR02868 333 PTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-V 411
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQHFALFDTlSVTENVALG--------LSTGISAAEIEREIRLLGEkyGLEVDPASVVMELSMGERQRVEILRALMT 153
Cdd:TIGR02868 412 SVCAQDAHLFDT-TVRENLRLArpdatdeeLWAALERVGLADWLRALPD--GLDTVLGEGGARLSGGERQRLALARALLA 488
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQlSSEGVSILFISHKL 196
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
5-213 6.28e-23

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: 94.44  E-value: 6.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHplgvetpaqareLGIAMV 84
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------VKIGYF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQhfalfdtlsvtenvalglstgisaaeiereirllgekyglevdpasvvmeLSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:cd03221    69 EQ--------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2549828669 165 SVLTPQAVRKLFKTLHQLSSegvSILFISHKLDEIRELADRCVVLRAGK 213
Cdd:cd03221    99 NHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIELEDGK 144
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
1-242 6.48e-23

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 102.49  E-value: 6.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGH---PLGVETP 73
Cdd:PRK10535    1 MTALLELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvaTLDADAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  74 AQARELGIAMVHQHFALFDTLSVTENVAL-GLSTGISAAE-IEREIRLLGeKYGLEVDPASVVMELSMGERQRVEILRAL 151
Cdd:PRK10535   81 AQLRREHFGFIFQRYHLLSHLTAAQNVEVpAVYAGLERKQrLLRAQELLQ-RLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKlDEIRELADRCVVLRAGKVVASVDPKAESEENLARL 231
Cdd:PRK10535  160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTE 238
                         250
                  ....*....|.
gi 2549828669 232 MIGNDPPTVRE 242
Cdd:PRK10535  239 PVVNTASGWRQ 249
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
8-222 6.65e-23

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 102.90  E-value: 6.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   8 RNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvetpaqARELGIAM---- 83
Cdd:NF033858  270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD------AGDIATRRrvgy 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 VHQHFALFDTLSVTENVALG--LsTGISAAEIEREIRLLGEKYGLE--VD--PASvvmeLSMGERQRVEILRALMTKPKL 157
Cdd:NF033858  344 MSQAFSLYGELTVRQNLELHarL-FHLPAAEIAARVAEMLERFDLAdvADalPDS----LPLGIRQRLSLAVAVIHKPEL 418
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 158 LILDEPTSVLTPQAvRKLF-KTLHQLSSE-GVSIlFIS-HKLDEIrELADRCVVLRAGKVVASVDPKA 222
Cdd:NF033858  419 LILDEPTSGVDPVA-RDMFwRLLIELSREdGVTI-FIStHFMNEA-ERCDRISLMHAGRVLASDTPAA 483
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
268-471 7.82e-23

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 97.06  E-value: 7.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQ-------ARFMAAASGEylceadrVLLFNSPVGELDTHARRISGlrYVPEQrlgHA 340
Cdd:COG1131    16 LDGVSLTVEPGEIFGLLGPNGAGKtttirmlLGLLRPTSGE-------VRVLGEDVARDPAEVRRRIG--YVPQE---PA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 341 AVPELSLTANTYLTGDSLVRSGFILRDRARSfanlVIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQP 420
Cdd:COG1131    84 LYPDLTVRENLRFFARLYGLPRKEARERIDE----LLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 421 TWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:COG1131   159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-215 9.76e-23

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 97.41  E-value: 9.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKII------YGAARPdEGEISFDGHPL---GVE 71
Cdd:COG1117     8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlIPGARV-EGEILLDGEDIydpDVD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  72 TPAQARELGiaMVHQH---FALfdtlSVTENVALGLST-GI-SAAEIErEI--RLLgEKYGL--EV-----DPAsvvMEL 137
Cdd:COG1117    87 VVELRRRVG--MVFQKpnpFPK----SIYDNVAYGLRLhGIkSKSELD-EIveESL-RKAALwdEVkdrlkKSA---LGL 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 138 SMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEgVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:COG1117   156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELV 232
cbiO PRK13640
energy-coupling factor transporter ATPase;
5-220 1.02e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 97.95  E-value: 1.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPG--ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGE---ISFDGHPLGVETPAQARE- 78
Cdd:PRK13640    6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREk 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  79 LGIamVHQH-FALFDTLSVTENVALGLST-GISAAEIEREIRLLGEKYGL----EVDPASvvmeLSMGERQRVEILRALM 152
Cdd:PRK13640   86 VGI--VFQNpDNQFVGATVGDDVAFGLENrAVPRPEMIKIVRDVLADVGMldyiDSEPAN----LSGGQKQRVAIAGILA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIrELADRCVVLRAGKVVASVDP 220
Cdd:PRK13640  160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSP 227
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
6-231 1.02e-22

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 97.08  E-value: 1.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   6 SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvETPAQ--ARELGIAM 83
Cdd:COG4604     3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA-TTPSRelAKRLAILR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 VHQHFALfdTLSVTENVALG--------LsTGISAAEIEREIRLLG-----EKYgleVDpasvvmELSMGERQRVEILRA 150
Cdd:COG4604    82 QENHINS--RLTVRELVAFGrfpyskgrL-TAEDREIIDEAIAYLDledlaDRY---LD------ELSGGQRQRAFIAMV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASvDPKAE--SEEN 227
Cdd:COG4604   150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ-GTPEEiiTPEV 228

                  ....
gi 2549828669 228 LARL 231
Cdd:COG4604   229 LSDI 232
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
5-217 1.17e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 97.57  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPG-ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARE-LGIA 82
Cdd:PRK13652    4 IETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKfVGLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTlSVTENVA-----LGLSTGISAAEIEREIRLLGekygLEVDPASVVMELSMGERQRVEILRALMTKPKL 157
Cdd:PRK13652   84 FQNPDDQIFSP-TVEQDIAfgpinLGLDEETVAHRVSSALHMLG----LEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:PRK13652  159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
7-220 1.20e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 98.23  E-value: 1.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   7 LRNITKRYPG-----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISF---DGHPLGVETPAQA-- 76
Cdd:PRK13651    5 VKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEKvl 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  77 --------------------RELGIAMVHQHFALFDTlSVTENVALG-LSTGISAAEIERE----IRLLG--EKYgLEVD 129
Cdd:PRK13651   85 eklviqktrfkkikkikeirRRVGVVFQFAEYQLFEQ-TIEKDIIFGpVSMGVSKEEAKKRaakyIELVGldESY-LQRS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 130 PasvvMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVL 209
Cdd:PRK13651  163 P----FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
                         250
                  ....*....|.
gi 2549828669 210 RAGKVVASVDP 220
Cdd:PRK13651  239 KDGKIIKDGDT 249
cbiO PRK13641
energy-coupling factor transporter ATPase;
21-222 1.31e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 97.59  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQA-----RELGIAMVHQHFALFDTlS 95
Cdd:PRK13641   24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlkklrKKVSLVFQFPEAQLFEN-T 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  96 VTENVALG-LSTGISAAEIEREIRLLGEKYGLEVDPAS-VVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVR 173
Cdd:PRK13641  103 VLKDVEFGpKNFGFSEDEAKEKALKWLKKVGLSEDLISkSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2549828669 174 KLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:PRK13641  183 EMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKE 231
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
2-214 2.11e-22

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 96.29  E-value: 2.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   2 TPrLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgvetpAQARElGI 81
Cdd:PRK11247   11 TP-LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEARE-DT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQHFALFDTLSVTENVALGLSTGISAAEIEREirllgEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILD 161
Cdd:PRK11247   84 RLMFQDARLLPWKKVIDNVGLGLKGQWRDAALQAL-----AAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 162 EP---TSVLTPQAVRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK11247  159 EPlgaLDALTRIEMQDLIESLWQ--QHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
21-242 2.60e-22

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 96.37  E-value: 2.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgvetPAQAREL------GIAMVHQHFALFDTL 94
Cdd:PRK11831   24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI----PAMSRSRlytvrkRMSMLFQSGALFTDM 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  95 SVTENVALGLS--TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAV 172
Cdd:PRK11831  100 NVFDNVAYPLRehTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 173 RKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEenlarlmigNDPPTVRE 242
Cdd:PRK11831  180 GVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA---------NPDPRVRQ 241
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
23-220 2.64e-22

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 96.61  E-value: 2.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVEtpaqarELGIAMVHQHFA---------LFDT 93
Cdd:PRK13638   20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYS------KRGLLALRQQVAtvfqdpeqqIFYT 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  94 lSVTENVALGL-STGISAAEIEREIR---LLGEKYGLEVDPasvVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTP 169
Cdd:PRK13638   94 -DIDSDIAFSLrNLGVPEAEITRRVDealTLVDAQHFRHQP---IQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 170 QAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDP 220
Cdd:PRK13638  170 AGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
cbiO PRK13644
energy-coupling factor transporter ATPase;
5-262 4.16e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 95.82  E-value: 4.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAM 83
Cdd:PRK13644    2 IRLENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 VHQH-FALFDTLSVTENVALGLST-GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILD 161
Cdd:PRK13644   82 VFQNpETQFVGRTVEEDLAFGPENlCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 162 EPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRElADRCVVLRAGKVVASVDPKAE-SEENLARLmiGNDPPTV 240
Cdd:PRK13644  162 EVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVlSDVSLQTL--GLTPPSL 238
                         250       260
                  ....*....|....*....|....
gi 2549828669 241 RE--GTAKAGEVVFEMRHVSAPGS 262
Cdd:PRK13644  239 IElaENLKMHGVVIPWENTSSPSS 262
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
5-237 5.61e-22

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 95.08  E-value: 5.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ-ARELgiAM 83
Cdd:PRK11231    3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlARRL--AL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 VHQHFALFDTLSVTENVALGLSTGIS-----AAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLL 158
Cdd:PRK11231   81 LPQHHLTPEGITVRELVAYGRSPWLSlwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLAR------LM 232
Cdd:PRK11231  161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRtvfdveAE 240

                  ....*
gi 2549828669 233 IGNDP 237
Cdd:PRK11231  241 IHPEP 245
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
5-217 6.16e-22

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 99.13  E-value: 6.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIA 82
Cdd:PRK11160  339 LTLNNVSFTYPDQPQPvlKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ-AIS 417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALF-DTLSvtENVALGLSTgisaAEIEREIRLLgEKYGLEV---DPASVVM-------ELSMGERQRVEILRAL 151
Cdd:PRK11160  418 VVSQRVHLFsATLR--DNLLLAAPN----ASDEALIEVL-QQVGLEKlleDDKGLNAwlgeggrQLSGGEQRRLGIARAL 490
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIrELADRCVVLRAGKVVAS 217
Cdd:PRK11160  491 LHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGL-EQFDRICVMDNGQIIEQ 554
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
1-214 9.31e-22

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 94.69  E-value: 9.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPD---EGEISFDGHPLGVETPAqAR 77
Cdd:PRK09984    1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGRTVQREGRL-AR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  78 ELGIAMVH-----QHFALFDTLSVTENVALGL--STGI--------SAAEIEREIRLLgEKYGLEVDPASVVMELSMGER 142
Cdd:PRK09984   80 DIRKSRANtgyifQQFNLVNRLSVLENVLIGAlgSTPFwrtcfswfTREQKQRALQAL-TRVGMVHFAHQRVSTLSGGQQ 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 143 QRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLS-SEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK09984  159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
1-215 1.00e-21

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 94.46  E-value: 1.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKII--YGAARPD---EGEISFDGHPL---GVET 72
Cdd:PRK14239    2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIyspRTDT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  73 PAQARELGiaMVHQHFALFdTLSVTENVALGLS-TGISAAEIEREI---RLLGEKYGLEV-----DPAsvvMELSMGERQ 143
Cdd:PRK14239   82 VDLRKEIG--MVFQQPNPF-PMSIYENVVYGLRlKGIKDKQVLDEAvekSLKGASIWDEVkdrlhDSA---LGLSGGQQQ 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 144 RVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEgVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK14239  156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLI 226
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
25-220 2.19e-21

anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 163483 [Multi-domain]  Cd Length: 223  Bit Score: 92.61  E-value: 2.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  25 LDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvetpAQARELGIAMVHQHFALFDTLSVTENVALGL 104
Cdd:TIGR03771   1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPG----KGWRHIGYVPQRHEFAWDFPISVAHTVMSGR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 105 STGI-----SAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTL 179
Cdd:TIGR03771  77 TGHIgwlrrPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELF 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2549828669 180 HQLSSEGVSILFISHKLDEIRELADRcVVLRAGKVVASVDP 220
Cdd:TIGR03771 157 IELAGAGTAILMTTHDLAQAMATCDR-VVLLNGRVIADGTP 196
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
3-220 3.44e-21

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: 91.79  E-value: 3.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYP--GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELg 80
Cdd:cd03244     1 GDIEFKNVSLRYRpnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTlSVTENVA-LGLStgiSAAEIEREIRLLGEK-------YGLEvdpaSVVME----LSMGERQRVEIL 148
Cdd:cd03244    80 ISIIPQDPVLFSG-TIRSNLDpFGEY---SDEELWQALERVGLKefveslpGGLD----TVVEEggenLSVGQRQLLCLA 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 149 RALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSeGVSILFISHKLDEIRElADRCVVLRAGKVVASVDP 220
Cdd:cd03244   152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
8-217 4.26e-21

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 96.57  E-value: 4.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   8 RNITKRYPGIT-ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIAMVHQ 86
Cdd:PRK13657  338 DDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRR-NIAVVFQ 416
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  87 HFALFDTlSVTENVALGlSTGISAAEIEREIR-------LLGEKYGLEvdpaSVVME----LSMGERQRVEILRALMTKP 155
Cdd:PRK13657  417 DAGLFNR-SIEDNIRVG-RPDATDEEMRAAAEraqahdfIERKPDGYD----TVVGErgrqLSGGERQRLAIARALLKDP 490
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 156 KLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIRElADRCVVLRAGKVVAS 217
Cdd:PRK13657  491 PILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVES 550
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
6-220 5.15e-21

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 92.54  E-value: 5.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   6 SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGV-ETPAQARElgIAMV 84
Cdd:PRK10575   13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARK--VAYL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENVALGL-----STGISAAE----IEREIRLLGEKyglevdPAS--VVMELSMGERQRVEILRALMT 153
Cdd:PRK10575   91 PQQLPAAEGMTVRELVAIGRypwhgALGRFGAAdrekVEEAISLVGLK------PLAhrLVDSLSGGERQRAWIAMLVAQ 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDP 220
Cdd:PRK10575  165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
5-202 8.65e-21

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: 90.11  E-value: 8.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElgIAMV 84
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEN--ILYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDTLSVTENvaLGLSTGISAAEiEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:TIGR01189  79 GHLPGLKPELSALEN--LHFWAAIHGGA-QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2549828669 165 SVLTPQAVRKLFKTLHQLSSEGVSILFISHK---LDEIREL 202
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLARGGIVLLTTHQdlgLVEAREL 196
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
5-215 1.03e-20

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 91.77  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITK---------RYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ 75
Cdd:PRK15112    5 LEVRNLSKtfryrtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  76 aRELGIAMVHQHFALF----DTLSVTENVALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVME-LSMGERQRVEILRA 150
Cdd:PRK15112   85 -RSQRIRMIFQDPSTSlnprQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHmLAPGQKQRLGLARA 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK15112  164 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
23-230 1.38e-20

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 90.76  E-value: 1.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAArPDEGEISFDGHPLG-VETPAQARELGIaMVHQHFALFdTLSVTENVA 101
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEaWSAAELARHRAY-LSQQQTPPF-AMPVFQYLT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 102 LGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRV-------EILRALMTKPKLLILDEPTSVL--TPQAV 172
Cdd:PRK03695   92 LHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEPMNSLdvAQQAA 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 173 rkLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK-AESEENLAR 230
Cdd:PRK03695  172 --LDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDeVLTPENLAQ 228
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
3-217 2.96e-20

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 91.51  E-value: 2.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPD----EGEISFDGHPLGVETPA 74
Cdd:COG4170     2 PLLDIRNLTIEIDTpqgrVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  75 QAREL---GIAMVHQHFAlfDTLSVTENVALGLSTGISAAE------------IEREIRLLgEKYGLEvDPaSVVM---- 135
Cdd:COG4170    82 ERRKIigrEIAMIFQEPS--SCLDPSAKIGDQLIEAIPSWTfkgkwwqrfkwrKKRAIELL-HRVGIK-DH-KDIMnsyp 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 136 -ELSMGERQRVEILRALMTKPKLLILDEPTSVL--TPQA-VRKLFKTLHQLSseGVSILFISHKLDEIRELADRCVVLRA 211
Cdd:COG4170   157 hELTEGECQKVMIAMAIANQPRLLIADEPTNAMesTTQAqIFRLLARLNQLQ--GTSILLISHDLESISQWADTITVLYC 234

                  ....*.
gi 2549828669 212 GKVVAS 217
Cdd:COG4170   235 GQTVES 240
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
23-215 3.90e-20

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


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 89.25  E-value: 3.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDE---GEISFDGHPLgveTPAQARELgIAMVHQHFALFDTLSVTE- 98
Cdd:cd03234    26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR---KPDQFQKC-VAYVRQDDILLPGLTVREt 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  99 -----NVALGLSTGISAAEIEREIRLLGEkYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVR 173
Cdd:cd03234   102 ltytaILRLPRKSSDAIRKKRVEDVLLRD-LALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2549828669 174 KLFKTLHQLSSEGVSILFISHK-LDEIRELADRCVVLRAGKVV 215
Cdd:cd03234   181 NLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
cbiO PRK13642
energy-coupling factor transporter ATPase;
1-238 4.47e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 90.15  E-value: 4.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRY---PGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAR 77
Cdd:PRK13642    1 MNKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  78 ElGIAMVHQH-FALFDTLSVTENVALGL-STGISAAE-IEREIRLLGEKYGLEV---DPAsvvmELSMGERQRVEILRAL 151
Cdd:PRK13642   81 R-KIGMVFQNpDNQFVGATVEDDVAFGMeNQGIPREEmIKRVDEALLAVNMLDFktrEPA----RLSGGQKQRVAVAGII 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRElADRCVVLRAGKVVASVDPKAESEENLAR 230
Cdd:PRK13642  156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDM 234

                  ....*...
gi 2549828669 231 LMIGNDPP 238
Cdd:PRK13642  235 VEIGLDVP 242
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
1-196 5.61e-20

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 89.40  E-value: 5.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEIsfdghplgvETPAQARelg 80
Cdd:PRK09544    1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLR--- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVALGLSTGISAAEIEREIRLLGEKYGLEvdpaSVVMELSMGERQRVEILRALMTKPKLLIL 160
Cdd:PRK09544   69 IGYVPQKLYLDTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLID----APMQKLSGGETQRVLLARALLNRPQLLVL 144
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKL 196
Cdd:PRK09544  145 DEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1-220 9.46e-20

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 93.54  E-value: 9.46e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669    1 MTPRLSLRNITKRYP--GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHplGVETPAQARE 78
Cdd:TIGR01257  925 LVPGVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK--DIETNLDAVR 1002
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   79 LGIAMVHQHFALFDTLSVTENVAL-GLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKL 157
Cdd:TIGR01257 1003 QSLGMCPQHNILFHHLTVAEHILFyAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669  158 LILDEPTSVLTPQAVRKLFKTLHQLSSeGVSILFISHKLDEIRELADRCVVLRAGKVVASVDP 220
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
2-212 1.19e-19

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 93.15  E-value: 1.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669    2 TPRLSLRNITKRYPGIT--ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVEtpaqarel 79
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN-------- 2006
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   80 gIAMVHQHF-------ALFDTLSVTENVAL-GLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRAL 151
Cdd:TIGR01257 2007 -ISDVHQNMgycpqfdAIDDLLTGREHLYLyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2085
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669  152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAG 212
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
17-220 2.13e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 89.14  E-value: 2.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  17 ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEIS----FDGHPLGVETPA---------QARELG--I 81
Cdd:PRK13631   39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHELItnpyskkikNFKELRrrV 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQ--HFALF-DTLS---VTENVALGLSTGISAAEIEREIRLLGEKYG-LEVDPasvvMELSMGERQRVEILRALMTK 154
Cdd:PRK13631  119 SMVFQfpEYQLFkDTIEkdiMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSP----FGLSGGQKRRVAIAGILAIQ 194
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDP 220
Cdd:PRK13631  195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTP 260
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
23-194 2.57e-19

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: 86.01  E-value: 2.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIAMVHQHfALFDTLSVTENV-- 100
Cdd:cd03231    19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL-LYLGHAP-GIKTTLSVLENLrf 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 --ALGLSTGISAAEIEREIRllgekyGLEVDPASvvmELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKT 178
Cdd:cd03231    97 whADHSDEQVEEALARVGLN------GFEDRPVA---QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
                         170
                  ....*....|....*.
gi 2549828669 179 LHQLSSEGVSILFISH 194
Cdd:cd03231   168 MAGHCARGGMVVLTTH 183
cbiO PRK13643
energy-coupling factor transporter ATPase;
23-220 2.64e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 88.25  E-value: 2.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFdGHPLGVETPAQA------RELGIAMVHQHFALFDTlSV 96
Cdd:PRK13643   25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKeikpvrKKVGVVFQFPESQLFEE-TV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  97 TENVALGLST-GISAAEIER----EIRLLG-EKYGLEVDPasvvMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQ 170
Cdd:PRK13643  103 LKDVAFGPQNfGIPKEKAEKiaaeKLEMVGlADEFWEKSP----FELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 171 A---VRKLFKTLHQlssEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDP 220
Cdd:PRK13643  179 ArieMMQLFESIHQ---SGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
21-195 2.92e-19

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 85.77  E-value: 2.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgiAMVHQHFALFDTLSVTENV 100
Cdd:PRK13540   18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQL--CFVGHRSGINPYLTLRENC 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 ALGLSTGISAAEIEREIRLLGEKYGLEVdPASVvmeLSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLH 180
Cdd:PRK13540   96 LYDIHFSPGAVGITELCRLFSLEHLIDY-PCGL---LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
                         170
                  ....*....|....*
gi 2549828669 181 QLSSEGVSILFISHK 195
Cdd:PRK13540  172 EHRAKGGAVLLTSHQ 186
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
1-204 3.28e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 87.40  E-value: 3.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIyGAARPDEGEISFDGHplgVETPAQA---R 77
Cdd:PRK14258    4 LIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGR---VEFFNQNiyeR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  78 ELGI-------AMVHQHFALFdTLSVTENVALGL---------------STGISAAEIEREIRLLGEKYGLEvdpasvvm 135
Cdd:PRK14258   80 RVNLnrlrrqvSMVHPKPNLF-PMSVYDNVAYGVkivgwrpkleiddivESALKDADLWDEIKHKIHKSALD-------- 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 136 eLSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLH--QLSSEgVSILFISHKLDEIRELAD 204
Cdd:PRK14258  151 -LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSE-LTMVIVSHNLHQVSRLSD 219
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
3-226 4.13e-19

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 88.32  E-value: 4.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARpDEGEIS-----FDGHPLGVETP 73
Cdd:PRK15093    2 PLLDIRNLTIEFKTsdgwVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTadrmrFDDIDLLRLSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  74 AQAREL---GIAMVHQHFAlfDTLSVTENVALGLSTGISAAEIE------------REIRLLgEKYGLEvDPASVV---- 134
Cdd:PRK15093   81 RERRKLvghNVSMIFQEPQ--SCLDPSERVGRQLMQNIPGWTYKgrwwqrfgwrkrRAIELL-HRVGIK-DHKDAMrsfp 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 135 MELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLS-SEGVSILFISHKLDEIRELADRCVVLRAGK 213
Cdd:PRK15093  157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
                         250
                  ....*....|...
gi 2549828669 214 VVASvdpkAESEE 226
Cdd:PRK15093  237 TVET----APSKE 245
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
4-215 4.25e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 86.89  E-value: 4.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKI------IYGAARPdEGEISFDGHPLgVETPAQAR 77
Cdd:PRK14247    3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlieLYPEARV-SGEVYLDGQDI-FKMDVIEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  78 ELGIAMVHQHFALFDTLSVTENVALGLSTG---ISAAEIEREIRLLGEKYGL--EVD-----PASvvmELSMGERQRVEI 147
Cdd:PRK14247   81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNrlvKSKKELQERVRWALEKAQLwdEVKdrldaPAG---KLSGGQQQRLCI 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 148 LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEgVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK14247  158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIV 224
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
21-194 1.22e-18

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 84.09  E-value: 1.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL---GiamvHQHfALFDTLSVT 97
Cdd:PRK13538   18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylG----HQP-GIKTELTAL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  98 ENV--ALGLSTGISAAEIEREIRLLGEKyGLEVDPASVvmeLSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKL 175
Cdd:PRK13538   93 ENLrfYQRLHGPGDDEALWEALAQVGLA-GFEDVPVRQ---LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL 168
                         170
                  ....*....|....*....
gi 2549828669 176 FKTLHQLSSEGVSILFISH 194
Cdd:PRK13538  169 EALLAQHAEQGGMVILTTH 187
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
261-469 1.30e-18

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: 83.22  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 261 GSTRVcgIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGlrYVPEqrlgHA 340
Cdd:cd03230    11 GKKTA--LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIG--YLPE----EP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 341 AVPElSLTANTYLTgdslvrsgfilrdrarsfanlvierfhvktpnaekaagsLSGGNLQKFIMGREILNRPRVLLVHQP 420
Cdd:cd03230    83 SLYE-NLTVRENLK---------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2549828669 421 TWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03230   123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
4-213 1.50e-18

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 88.49  E-value: 1.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYPGIT-ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIA 82
Cdd:PRK10522  322 TLELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-FS 400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTLSVTENVAlglstgISAAEIEREIRLLGEKYGLEVDPASVV-MELSMGERQRVEILRALMTKPKLLILD 161
Cdd:PRK10522  401 AVFTDFHLFDQLLGPEGKP------ANPALVEKWLERLKMAHKLELEDGRISnLKLSKGQKKRLALLLALAEERDILLLD 474
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 162 EPTSVLTPQaVRKLF--KTLHQLSSEGVSILFISHKlDEIRELADRCVVLRAGK 213
Cdd:PRK10522  475 EWAADQDPH-FRREFyqVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
23-215 2.28e-18

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 87.98  E-value: 2.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAArPDEGEISFDGHPLGVETPAQARELgIAMVHQHFALFDTlSVTENVAL 102
Cdd:PRK11174  369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKH-LSWVGQNPQLPHG-TLRDNVLL 445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 103 GLSTgISAAEIEReirLLGEKYGLEVDPA------SVVME----LSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAV 172
Cdd:PRK11174  446 GNPD-ASDEQLQQ---ALENAWVSEFLPLlpqgldTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2549828669 173 RKLFKTLHQLsSEGVSILFISHKLDEIRELaDRCVVLRAGKVV 215
Cdd:PRK11174  522 QLVMQALNAA-SRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIV 562
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
22-215 2.53e-18

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 87.85  E-value: 2.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  22 HVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIAMVHQH-FALFDTLSVteNV 100
Cdd:PRK10790  359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ-GVAMVQQDpVVLADTFLA--NV 435
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 ALG-----------LSTgISAAEIEREI-----RLLGEKYGlevdpasvvmELSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:PRK10790  436 TLGrdiseeqvwqaLET-VQLAELARSLpdglyTPLGEQGN----------NLSVGQKQLLALARVLVQTPQILILDEAT 504
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 165 SVL---TPQAVRKLFKTLHQLSsegvSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:PRK10790  505 ANIdsgTEQAIQQALAAVREHT----TLVVIAHRLSTIVE-ADTILVLHRGQAV 553
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
4-214 2.87e-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: 87.79  E-value: 2.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYPG---ITANDhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPaqaRELG 80
Cdd:TIGR01842 316 HLSVENVTIVPPGgkkPTLRG-ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR---ETFG 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 --IAMVHQHFALFDTlSVTENVA-----LGLSTGISAAEI---EREIRLLGEKYGLEVDPASVvmELSMGERQRVEILRA 150
Cdd:TIGR01842 392 khIGYLPQDVELFPG-TVAENIArfgenADPEKIIEAAKLagvHELILRLPDGYDTVIGPGGA--TLSGGQRQRIALARA 468
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIrELADRCVVLRAGKV 214
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLL-GCVDKILVLQDGRI 531
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
3-239 3.48e-18

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 86.43  E-value: 3.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgveTPAQARELG-- 80
Cdd:PRK09536    2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV---EALSARAASrr 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 IAMVHQHFALFDTLSVTENVALG-------LSTGISA--AEIEREIrllgEKYGLEVDPASVVMELSMGERQRVEILRAL 151
Cdd:PRK09536   79 VASVPQDTSLSFEFDVRQVVEMGrtphrsrFDTWTETdrAAVERAM----ERTGVAQFADRPVTSLSGGERQRVLLARAL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 152 MTKPKLLILDEPTSVL-TPQAVRKLfKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAE-SEENL- 228
Cdd:PRK09536  155 AQATPVLLLDEPTASLdINHQVRTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVlTADTLr 233
                         250
                  ....*....|....*
gi 2549828669 229 ----ARLMIGNDPPT 239
Cdd:PRK09536  234 aafdARTAVGTDPAT 248
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
6-469 4.52e-18

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 87.49  E-value: 4.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   6 SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgvetpAQARELgiAMVH 85
Cdd:NF033858    3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM-----ADARHR--RAVC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  86 QHFA---------LFDTLSVTENVAL-GLSTGISAAEIEREIRLLGEKYGLE--VD-PASvvmELSMGERQRVEILRALM 152
Cdd:NF033858   76 PRIAympqglgknLYPTLSVFENLDFfGRLFGQDAAERRRRIDELLRATGLApfADrPAG---KLSGGMKQKLGLCCALI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 153 TKPKLLILDEPTSVLTPQAvRKLFKTL---HQLSSEGVSILFISHKLDEIrELADRCVVLRAGKVVASVDPK-------A 222
Cdd:NF033858  153 HDPDLLILDEPTTGVDPLS-RRQFWELidrIRAERPGMSVLVATAYMEEA-ERFDWLVAMDAGRVLATGTPAellartgA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 223 ES-EENLARLMigndPPTVREGTA----------KAGEVVFEMRHVsapgsTRVCG----IDNVSLAVRAGEIVGIAGIS 287
Cdd:NF033858  231 DTlEAAFIALL----PEEKRRGHQpvvipprpadDDDEPAIEARGL-----TMRFGdftaVDHVSFRIRRGEIFGFLGSN 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 288 GNGQARFM-------AAASGEylceadrVLLFNSPV---------------------GE------LDTHARrisgLRYVP 333
Cdd:NF033858  302 GCGKSTTMkmltgllPASEGE-------AWLFGQPVdagdiatrrrvgymsqafslyGEltvrqnLELHAR----LFHLP 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 334 EQRLGhAAVPELsltantyltgdslvrsgfilrdrarsfanlvIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPR 413
Cdd:NF033858  371 AAEIA-ARVAEM-------------------------------LERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPE 417
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 414 VLLVHQPTWGVDVGAaaviRNS----LIRL-RDDGAAIIVVSEEIDELfEISDRIAVMYRG 469
Cdd:NF033858  418 LLILDEPTSGVDPVA----RDMfwrlLIELsREDGVTIFISTHFMNEA-ERCDRISLMHAG 473
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
13-215 6.26e-18

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 86.69  E-value: 6.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  13 RYPGIT--ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgveTPAQAREL--GIAMVHQHF 88
Cdd:PRK10789  322 TYPQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL---TKLQLDSWrsRLAVVSQTP 398
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  89 ALFDTlSVTENVALGlSTGISAAEIEREIRL---------LGEKYGLEVDPASVVmeLSMGERQRVEILRALMTKPKLLI 159
Cdd:PRK10789  399 FLFSD-TVANNIALG-RPDATQQEIEHVARLasvhddilrLPQGYDTEVGERGVM--LSGGQKQRISIARALLLNAEILI 474
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:PRK10789  475 LDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLSALTE-ASEILVMQHGHIA 528
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
21-215 1.08e-17

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 81.93  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAA--RPDEGEISFDGHPLGVETPaqarelgiaMVHQHFALFDTLSVTE 98
Cdd:COG2401    47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREAS---------LIDAIGRKGDFKDAVE 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  99 NVAL-GLSTGIsaaeiereirLLGEKYGlevdpasvvmELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFK 177
Cdd:COG2401   118 LLNAvGLSDAV----------LWLRRFK----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2549828669 178 TLHQLSSE-GVSILFISHKLDEIRELA-DRCVVLRAGKVV 215
Cdd:COG2401   178 NLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYGGVP 217
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
19-217 1.34e-17

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 83.64  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  19 ANDHVSLDIAPGEVLAILGENGAGKS----TLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL---GIAMVHQH---- 87
Cdd:PRK11022   22 AVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLvgaEVAMIFQDpmts 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  88 --------FALFDTLSVTENvalglstGISAAEIEREIRLLgEKYGLEvDPASVV----MELSMGERQRVEILRALMTKP 155
Cdd:PRK11022  102 lnpcytvgFQIMEAIKVHQG-------GNKKTRRQRAIDLL-NQVGIP-DPASRLdvypHQLSGGMSQRVMIAMAIACRP 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 156 KLLILDEPTSVL--TPQA-VRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:PRK11022  173 KLLIADEPTTALdvTIQAqIIELLLELQQ--KENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
22-221 1.82e-17

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 82.76  E-value: 1.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  22 HVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVET-PAQAREL--GIAMVHQhFA---LFDTlS 95
Cdd:PRK13634   25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKkNKKLKPLrkKVGIVFQ-FPehqLFEE-T 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  96 VTENVALG-LSTGISAAEIEREIRLLGEKYGLevdPASVV----MELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQ 170
Cdd:PRK13634  103 VEKDICFGpMNFGVSEEDAKQKAREMIELVGL---PEELLarspFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 171 AvRK----LFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:PRK13634  180 G-RKemmeMFYKLHK--EKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPR 231
cbiO PRK13646
energy-coupling factor transporter ATPase;
19-222 2.37e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 82.52  E-value: 2.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  19 ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVET------PAQARelgIAMVHQ--HFAL 90
Cdd:PRK13646   22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyirPVRKR---IGMVFQfpESQL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  91 FDTlSVTENVALGLST-GISAAEI-EREIRLLGEkYGLEVDpasvVMELS---M--GERQRVEILRALMTKPKLLILDEP 163
Cdd:PRK13646   99 FED-TVEREIIFGPKNfKMNLDEVkNYAHRLLMD-LGFSRD----VMSQSpfqMsgGQMRKIAIVSILAMNPDIIVLDEP 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 164 TSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:PRK13646  173 TAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
23-215 3.38e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 81.25  E-value: 3.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL-------GVETPAQARELGiaMVHQHFALFDTLS 95
Cdd:PRK14246   29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifQIDAIKLRKEVG--MVFQQPNPFPHLS 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  96 VTENVALGL-STGIS--------AAEIEREIRLLGEKYGLEVDPASvvmELSMGERQRVEILRALMTKPKLLILDEPTSV 166
Cdd:PRK14246  107 IYDNIAYPLkSHGIKekreikkiVEECLRKVGLWKEVYDRLNSPAS---QLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2549828669 167 LTPQAVRKLFKTLHQLSSEgVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK14246  184 IDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
4-215 6.95e-17

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: 79.38  E-value: 6.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRY----PGITANdhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvETPAQAREL 79
Cdd:cd03369     6 EIEVENLSVRYapdlPPVLKN--VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS-TIPLEDLRS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  80 GIAMVHQHFALFDTlSVTENvaLGLSTGISAAEIEREIRLLGEkyGLEvdpasvvmeLSMGERQRVEILRALMTKPKLLI 159
Cdd:cd03369    83 SLTIIPQDPTLFSG-TIRSN--LDPFDEYSDEEIYGALRVSEG--GLN---------LSQGQRQLLCLARALLKRPRVLV 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSeGVSILFISHKLDEIRELaDRCVVLRAGKVV 215
Cdd:cd03369   149 LDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
17-213 7.86e-17

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 81.69  E-value: 7.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  17 ITANDHVSLDIAPGEVLAILGENGAGKS----TLMKIIYGAARPdEGEISFDGHPLgVETPAQA----RELGIAMVHQH- 87
Cdd:PRK09473   29 VTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRI-GGSATFNGREI-LNLPEKElnklRAEQISMIFQDp 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  88 -FALFDTLSVTENVA--LGLSTGISAAE-IEREIRLLGekyGLEVDPASVVM-----ELSMGERQRVEILRALMTKPKLL 158
Cdd:PRK09473  107 mTSLNPYMRVGEQLMevLMLHKGMSKAEaFEESVRMLD---AVKMPEARKRMkmyphEFSGGMRQRVMIAMALLCRPKLL 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 159 ILDEPTSVL--TPQAvrKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGK 213
Cdd:PRK09473  184 IADEPTTALdvTVQA--QIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
cbiO PRK13645
energy-coupling factor transporter ATPase;
7-238 1.00e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 80.44  E-value: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   7 LRNITKRYPGIT-----ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGH--PLGV----ETPAQ 75
Cdd:PRK13645    9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaiPANLkkikEVKRL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  76 ARELGIAMVHQHFALFDTlSVTENVALG-LSTGISAAEIEREIRLLGEKYGLEVDPAS-VVMELSMGERQRVEILRALMT 153
Cdd:PRK13645   89 RKEIGLVFQFPEYQLFQE-TIEKDIAFGpVNLGENKQEAYKKVPELLKLVQLPEDYVKrSPFELSGGQKRRVALAGIIAM 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA--ESEENLAR 230
Cdd:PRK13645  168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEifSNQELLTK 247

                  ....*...
gi 2549828669 231 LMIgnDPP 238
Cdd:PRK13645  248 IEI--DPP 253
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
3-227 1.03e-16

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 82.98  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYP-----------GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVE 71
Cdd:PRK10261  312 PILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  72 TPAQAREL--GIAMVHQH-FALFDT-----LSVTENVAL-GLSTGISAAeieREIRLLGEKYGLEVDPA-SVVMELSMGE 141
Cdd:PRK10261  392 SPGKLQALrrDIQFIFQDpYASLDPrqtvgDSIMEPLRVhGLLPGKAAA---ARVAWLLERVGLLPEHAwRYPHEFSGGQ 468
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 142 RQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVaSVDP 220
Cdd:PRK10261  469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV-EIGP 547

                  ....*..
gi 2549828669 221 KAESEEN 227
Cdd:PRK10261  548 RRAVFEN 554
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
27-215 1.76e-16

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 77.67  E-value: 1.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  27 IAPGEVLAILGENGAGKSTLMKIIygAARPD----EGEISFDGHPLGVETPAQarelgIAMVHQHFALFDTLSVTEnval 102
Cdd:cd03232    30 VKPGTLTALMGESGAGKTTLLDVL--AGRKTagviTGEILINGRPLDKNFQRS-----TGYVEQQDVHSPNLTVRE---- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 103 glSTGISAAeiereIRllgekyglevdpasvvmELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQL 182
Cdd:cd03232    99 --ALRFSAL-----LR-----------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2549828669 183 SSEGVSIL-FISHKLDEIRELADRCVVL-RAGKVV 215
Cdd:cd03232   155 ADSGQAILcTIHQPSASIFEKFDRLLLLkRGGKTV 189
ycf16 CHL00131
sulfate ABC transporter protein; Validated
23-215 2.58e-16

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 78.53  E-value: 2.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIygAARPD----EGEISFDGHPLGVETPAQARELGIAMVHQHfalfdTLSVte 98
Cdd:CHL00131   26 LNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHPAykilEGDILFKGESILDLEPEERAHLGIFLAFQY-----PIEI-- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  99 nvalglsTGISAAEIEREIRLLGEK-YGL-EVDPAS-----------VVME-----------LSMGERQRVEILRALMTK 154
Cdd:CHL00131   97 -------PGVSNADFLRLAYNSKRKfQGLpELDPLEfleiineklklVGMDpsflsrnvnegFSGGEKKRNEILQMALLD 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHK---LDEIRelADRCVVLRAGKVV 215
Cdd:CHL00131  170 SELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYqrlLDYIK--PDYVHVMQNGKII 231
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
3-179 3.09e-16

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 77.22  E-value: 3.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPA-QARELGi 81
Cdd:PRK13539    1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeACHYLG- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 amvHQHfALFDTLSVTENVAL------GLSTGISAAeIER-EIRLLGE-KYGlevdpasvvmELSMGERQRVEILRALMT 153
Cdd:PRK13539   80 ---HRN-AMKPALTVAENLEFwaaflgGEELDIAAA-LEAvGLAPLAHlPFG----------YLSAGQKRRVALARLLVS 144
                         170       180
                  ....*....|....*....|....*.
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRkLFKTL 179
Cdd:PRK13539  145 NRPIWILDEPTAALDAAAVA-LFAEL 169
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
23-227 3.43e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 78.35  E-value: 3.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKI------IYGAARPdEGEISFDGHPLGVE--TPAQARElGIAMVHQHFALFDTL 94
Cdd:PRK14267   23 VDLKIPQNGVFALMGPSGCGKSTLLRTfnrlleLNEEARV-EGEVRLFGRNIYSPdvDPIEVRR-EVGMVFQYPNPFPHL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  95 SVTENVALGLSTG---ISAAEIEREIRLLGEKYGL--EV-----DPASvvmELSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:PRK14267  101 TIYDNVAIGVKLNglvKSKKELDERVEWALKKAALwdEVkdrlnDYPS---NLSGGQRQRLVIARALAMKPKILLMDEPT 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 165 SVLTPQAVRKLFKTLHQLSSEgVSILFISHKLDEIRELADRCVVLRAGKVVaSVDPKAESEEN 227
Cdd:PRK14267  178 ANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLI-EVGPTRKVFEN 238
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
21-215 5.40e-16

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 80.76  E-value: 5.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFdghplgvetpaqARELGIAMVHQHFALFDTLSVTENV 100
Cdd:PRK11147   20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY------------EQDLIVARLQQDPPRNVEGTVYDFV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 ALGLSTGISAAEIEREI-RLLGEKYG--------------------------------LEVDPASVVMELSMGERQRVEI 147
Cdd:PRK11147   88 AEGIEEQAEYLKRYHDIsHLVETDPSeknlnelaklqeqldhhnlwqlenrinevlaqLGLDPDAALSSLSGGWLRKAAL 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 148 LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLhqLSSEGvSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK11147  168 GRALVSNPDVLLLDEPTNHLDIETIEWLEGFL--KTFQG-SIIFISHDRSFIRNMATRIVDLDRGKLV 232
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
268-469 7.22e-16

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: 76.70  E-value: 7.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGLRYVPEqrlGHAAVPELSL 347
Cdd:cd03224    16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPE---GRRIFPELTV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 TANtyltgdslVRSGFILRDRARSFANL--VIERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVD 425
Cdd:cd03224    93 EEN--------LLLGAYARRRAKRKARLerVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2549828669 426 VGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03224   165 PKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERG 208
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
3-212 1.70e-15

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 79.08  E-value: 1.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKII-----YGaarpdEGEISFdghplgvetPAQA 76
Cdd:COG4178   361 GALALEDLTLRTPdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpYG-----SGRIAR---------PAGA 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  77 RelgiamvhqhfALF---------DTLsvTENVAL-GLSTGISAAEIE---REIRL--LGEKYGLEVDPASVvmeLSMGE 141
Cdd:COG4178   427 R-----------VLFlpqrpylplGTL--REALLYpATAEAFSDAELRealEAVGLghLAERLDEEADWDQV---LSLGE 490
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 142 RQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQlSSEGVSILFISHKlDEIRELADRCVVLRAG 212
Cdd:COG4178   491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHR-STLAAFHDRVLELTGD 559
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
268-471 5.83e-15

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: 74.40  E-value: 5.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRisglryvpeqRLG------HAA 341
Cdd:cd03219    16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA----------RLGigrtfqIPR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 342 V-PELSLTANTYLTGDSLVRSGFILRDRARSFANL------VIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPRV 414
Cdd:cd03219    86 LfPELTVLENVMVAAQARTGSGLLLARARREEREAreraeeLLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKL 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 415 LLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03219   165 LLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
23-215 8.11e-15

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 77.01  E-value: 8.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPD---EGEISFDGHPLGVEtpaQARELGiAMVHQHFALFDTLSVTE- 98
Cdd:TIGR00955  44 VSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAK---EMRAIS-AYVQQDDLFIPTLTVREh 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  99 -NVALGLSTGISAAEIEREIRL--LGEKYGLE------VDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTP 169
Cdd:TIGR00955 120 lMFQAHLRMPRRVTKKEKRERVdeVLQALGLRkcantrIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2549828669 170 QAVRKLFKTLHQLSSEGVSILFISHK-LDEIRELADRCVVLRAGKVV 215
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVA 246
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
2-237 1.17e-14

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 73.87  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   2 TPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDG-HPLGVETPAQARELG 80
Cdd:PRK10253    5 VARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGeHIQHYASKEVARRIG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  81 iaMVHQHFALFDTLSVTENVALG------LSTGISaAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTK 154
Cdd:PRK10253   85 --LLAQNATTPGDITVQELVARGryphqpLFTRWR-KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK----AESEENL- 228
Cdd:PRK10253  162 TAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKeivtAELIERIy 241
                         250
                  ....*....|
gi 2549828669 229 -ARLMIGNDP 237
Cdd:PRK10253  242 gLRCMIIDDP 251
hmuV PRK13547
heme ABC transporter ATP-binding protein;
21-221 1.32e-14

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 74.09  E-value: 1.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYG----AARPD----EGEISFDGHPLGVETPAQARELGIAMVHQHFALFd 92
Cdd:PRK13547   18 RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  93 TLSVTENVALG-LSTGISAAEIEREIRLLG----EKYGLEVDPASVVMELSMGERQRVEILRAL---------MTKPKLL 158
Cdd:PRK13547   97 AFSAREIVLLGrYPHARRAGALTHRDGEIAwqalALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYL 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:PRK13547  177 LLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
24-291 1.92e-14

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 75.44  E-value: 1.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  24 SLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEI--SFDgHP--LGVETPAQarelgiaMVHQHFALFDT--LSVT 97
Cdd:PRK10938   23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsQFS-HItrLSFEQLQK-------LVSDEWQRNNTdmLSPG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  98 ENvalglSTGISAAE-IEREIR------LLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQ 170
Cdd:PRK10938   95 ED-----DTGRTTAEiIQDEVKdparceQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 171 AVRKLFKTLHQLSSEGVSILFISHKLDEIRELADR------CVVLRAGK--------VVASVdpkAESEENLARLMIGND 236
Cdd:PRK10938  170 SRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFagvladCTLAETGEreeilqqaLVAQL---AHSEQLEGVQLPEPD 246
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 237 PPTVREgTAKAGEVVFEMRHVSAPGSTRVCgIDNVSLAVRAGEIVGIAGISGNGQ 291
Cdd:PRK10938  247 EPSARH-ALPANEPRIVLNNGVVSYNDRPI-LHNLSWQVNPGEHWQIVGPNGAGK 299
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
6-290 2.28e-14

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: 75.36  E-value: 2.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   6 SLRNITKRYPG---ITANdhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEIsfdghplgveTPAQARELGia 82
Cdd:TIGR03719   6 TMNRVSKVVPPkkeILKD--ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA----------RPQPGIKVG-- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTLSVTENVALGLS---------TGISA--AEIEREIRLLGEKYG-----------------LEV------ 128
Cdd:TIGR03719  72 YLPQEPQLDPTKTVRENVEEGVAeikdaldrfNEISAkyAEPDADFDKLAAEQAelqeiidaadawdldsqLEIamdalr 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 129 --DPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSegvSILFISH------------ 194
Cdd:TIGR03719 152 cpPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTHdryfldnvagwi 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 195 -KLD------------------------EIRELADRCVVLRAGKVVASVDPKAESEENLARL-----MIGNDPPTvREGT 244
Cdd:TIGR03719 229 lELDrgrgipwegnysswleqkqkrleqEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLaryeeLLSQEFQK-RNET 307
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 245 A--------KAGEVVFEMRHVSAPGSTRVCgIDNVSLAVRAGEIVGIAGISGNG 290
Cdd:TIGR03719 308 AeiyippgpRLGDKVIEAENLTKAFGDKLL-IDDLSFKLPPGGIVGVIGPNGAG 360
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
268-471 3.58e-14

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: 71.77  E-value: 3.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQ-------ARFMAAASGEylceadrVLLFNSPVGELDTHARRISGLR--YVPEQrlg 338
Cdd:cd03257    21 LDDVSFSIKKGETLGLVGESGSGKstlaraiLGLLKPTSGS-------IIFDGKDLLKLSRRLRKIRRKEiqMVFQD--- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 339 haavPELSLtaNTYLT-GDSLVRSGFILR-DRARSFANLVIERFHVKTPNAEKAAGS----LSGGNLQKFIMGREILNRP 412
Cdd:cd03257    91 ----PMSSL--NPRMTiGEQIAEPLRIHGkLSKKEARKEAVLLLLVGVGLPEEVLNRypheLSGGQRQRVAIARALALNP 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 413 RVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03257   165 KLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
251-499 3.64e-14

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 74.86  E-value: 3.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 251 VFEMRHVSAPGSTrVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLC-EADRVLLFN-SPV---GELDTHARR 325
Cdd:TIGR02633   1 LLEMKGIVKTFGG-VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgTWDGEIYWSgSPLkasNIRDTERAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 326 ISglryVPEQRLghAAVPELSLTANTYLtGDSLVRSGFILRDRARSF-ANLVIERFHVKTPNAEKAAGSLSGGNLQKFIM 404
Cdd:TIGR02633  80 IV----IIHQEL--TLVPELSVAENIFL-GNEITLPGGRMAYNAMYLrAKNLLRELQLDADNVTRPVGDYGGGQQQLVEI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 405 GREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALSPAVPKPTISIEE 484
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDD 232
                         250       260
                  ....*....|....*....|
gi 2549828669 485 -----VGRWMSGLWPDSPFT 499
Cdd:TIGR02633 233 iitmmVGREITSLYPHEPHE 252
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
5-215 4.30e-14

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 71.14  E-value: 4.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNIT----KRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPD---EGEISFDGHPLGVETPAQAR 77
Cdd:cd03233     4 LSWRNISfttgKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  78 ElgIAMVHQHFALFDTLSVTENvalglstgisaaeIEREIRLLGEKYglevdpasvVMELSMGERQRVEILRALMTKPKL 157
Cdd:cd03233    84 E--IIYVSEEDVHFPTLTVRET-------------LDFALRCKGNEF---------VRGISGGERKRVSIAEALVSRASV 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLS--SEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:cd03233   140 LCWDNSTRGLDSSTALEILKCIRTMAdvLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
264-469 8.16e-14

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: 70.39  E-value: 8.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 264 RVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHArrisgLRYVPEQRlghAAVP 343
Cdd:cd03269    12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-----IGYLPEER---GLYP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 344 ELSLTAN-TYLTgdSLvrSGFILRDrARSFANLVIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTW 422
Cdd:cd03269    84 KMKVIDQlVYLA--QL--KGLKKEE-ARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2549828669 423 GVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03269   158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
PLN03232 PLN03232
ABC transporter C family member; Provisional
13-230 2.79e-13

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 72.70  E-value: 2.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   13 RY-PGITANDH-VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIAMVHQHFAL 90
Cdd:PLN03232  1243 RYrPGLPPVLHgLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV-LSIIPQSPVL 1321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   91 F--------DTLSvtENVALGLSTGISAAEIEREIRllGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDE 162
Cdd:PLN03232  1322 FsgtvrfniDPFS--EHNDADLWEALERAHIKDVID--RNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDE 1397
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669  163 PTS-------VLTPQAVRKLFKTlhqlssegVSILFISHKLDEIRElADRCVVLRAGKVVASVDPkaesEENLAR 230
Cdd:PLN03232  1398 ATAsvdvrtdSLIQRTIREEFKS--------CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSP----QELLSR 1459
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
21-194 2.81e-13

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: 67.56  E-value: 2.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIygaarpdeGEI--SFDGHplgVETPAQArelGIAMVHQHfALFDTLSVTE 98
Cdd:cd03223    18 KDLSFEIKPGDRLLITGPSGTGKSSLFRAL--------AGLwpWGSGR---IGMPEGE---DLLFLPQR-PYLPLGTLRE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  99 NVALGLStgisaaeiereirllgekyglevdpasvvMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKT 178
Cdd:cd03223    83 QLIYPWD-----------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
                         170
                  ....*....|....*.
gi 2549828669 179 LHQlssEGVSILFISH 194
Cdd:cd03223   134 LKE---LGITVISVGH 146
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
5-231 2.93e-13

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 71.68  E-value: 2.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNIT-KRYPGItanDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGiam 83
Cdd:PRK10982  251 LEVRNLTsLRQPSI---RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHG--- 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 vhqhFALfdtlsVTENVAlglSTGISAA-EIE-----REIRLLGEKYGL------------EVDPASV--------VMEL 137
Cdd:PRK10982  325 ----FAL-----VTEERR---STGIYAYlDIGfnsliSNIRNYKNKVGLldnsrmksdtqwVIDSMRVktpghrtqIGSL 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 138 SMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:PRK10982  393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
                         250
                  ....*....|....
gi 2549828669 218 VDPKAESEENLARL 231
Cdd:PRK10982  473 VDTKTTTQNEILRL 486
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
3-199 3.15e-13

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: 71.89  E-value: 3.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRL-----SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDghplgvETpaqar 77
Cdd:TIGR03719 316 PRLgdkviEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG------ET----- 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  78 eLGIAMVHQ-HFALFDTLSVTENVALGLstgisaaeierEIRLLGekyGLEV--------------DPASVVMELSMGER 142
Cdd:TIGR03719 385 -VKLAYVDQsRDALDPNKTVWEEISGGL-----------DIIKLG---KREIpsrayvgrfnfkgsDQQKKVGQLSGGER 449
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 143 QRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLhqLSSEGVSILfISHK---LDEI 199
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL--LNFAGCAVV-ISHDrwfLDRI 506
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
262-471 3.71e-13

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: 68.55  E-value: 3.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 262 STRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGeyLCEADRvllFNSPVGELDTH-----ARRisGLRYVPEQR 336
Cdd:cd03266    15 KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAG--LLEPDA---GFATVDGFDVVkepaeARR--RLGFVSDST 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 337 lghAAVPELSLTANTYLTGDSLVRSGFILRDRArsfaNLVIERFHVKtPNAEKAAGSLSGGNLQKFIMGREILNRPRVLL 416
Cdd:cd03266    88 ---GLYDRLTARENLEYFAGLYGLKGDELTARL----EELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 417 VHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03266   160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
249-497 3.91e-13

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 71.50  E-value: 3.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 249 EVVFEMRHV--SAPGstrVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLC---EADrvLLFNspvGEL---- 319
Cdd:PRK13549    3 EYLLEMKNItkTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtyEGE--IIFE---GEElqas 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 320 ---DTHARRISglryVPEQRLghAAVPELSLTANTYLtGDSLVRSGFILRDRARSFANLVIERFHVKTPNAEKAaGSLSG 396
Cdd:PRK13549   75 nirDTERAGIA----IIHQEL--ALVKELSVLENIFL-GNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPV-GNLGL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 397 GNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALSPAVP 476
Cdd:PRK13549  147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRP 226
                         250       260
                  ....*....|....*....|....*.
gi 2549828669 477 KPTISIEE-----VGRWMSGLWPDSP 497
Cdd:PRK13549  227 AAGMTEDDiitmmVGRELTALYPREP 252
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
21-215 4.06e-13

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 72.06  E-value: 4.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIygAARPDEGEISFD-----GHPLgvETPAQARelgIAMVHQHFALFDTLS 95
Cdd:TIGR00956  780 NNVDGWVKPGTLTALMGASGAGKTTLLNVL--AERVTTGVITGGdrlvnGRPL--DSSFQRS---IGYVQQQDLHLPTST 852
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   96 VTENV----ALGLSTGISAAE----IEREIRLLG-EKYGLEVdpASVVME-LSMGERQRVEILRALMTKPKLLI-LDEPT 164
Cdd:TIGR00956  853 VRESLrfsaYLRQPKSVSKSEkmeyVEEVIKLLEmESYADAV--VGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPT 930
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2549828669  165 SVLTPQAVRKLFKTLHQLSSEGVSILFISHKLD-EIRELADRCVVL-RAGKVV 215
Cdd:TIGR00956  931 SGLDSQTAWSICKLMRKLADHGQAILCTIHQPSaILFEEFDRLLLLqKGGQTV 983
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
268-469 4.33e-13

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: 66.88  E-value: 4.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRiSGLRYVPEqrlghaavpelsl 347
Cdd:cd00267    15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR-RRIGYVPQ------------- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 tantyltgdslvrsgfilrdrarsfanlvierfhvktpnaekaagsLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVG 427
Cdd:cd00267    81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2549828669 428 AAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd00267   115 SRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
PLN03211 PLN03211
ABC transporter G-25; Provisional
27-213 4.47e-13

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 71.83  E-value: 4.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  27 IAPGEVLAILGENGAGKSTLMKIIYGAARPDegeiSFDGHPLGVE-TPAQARELGIAMVHQHFALFDTLSVTENVA---- 101
Cdd:PLN03211   91 ASPGEILAVLGPSGSGKSTLLNALAGRIQGN----NFTGTILANNrKPTKQILKRTGFVTQDDILYPHLTVRETLVfcsl 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 102 LGLSTGISAAE----IEREIRLLG-EKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLF 176
Cdd:PLN03211  167 LRLPKSLTKQEkilvAESVISELGlTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2549828669 177 KTLHQLSSEGVSILFISHK-LDEIRELADRCVVLRAGK 213
Cdd:PLN03211  247 LTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
261-469 4.97e-13

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: 68.31  E-value: 4.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 261 GSTRVcgIDNVSLAVRAGEIVGIAGISGNGQ-------ARFMAAASGEylceadrVLLFNSPVGELDTHARRISglrYVP 333
Cdd:cd03259    11 GSVRA--LDDLSLTVEPGEFLALLGPSGCGKttllrliAGLERPDSGE-------ILIDGRDVTGVPPERRNIG---MVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 334 EQrlgHAAVPELSLTANTyltgdslvrsGFILRDRARSFAN------LVIERFHVkTPNAEKAAGSLSGGNLQKFIMGRE 407
Cdd:cd03259    79 QD---YALFPHLTVAENI----------AFGLKLRGVPKAEirarvrELLELVGL-EGLLNRYPHELSGGQQQRVALARA 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 408 ILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03259   145 LAREPSLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEG 207
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
5-204 6.00e-13

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 69.04  E-value: 6.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMK-------IIYGAARpdEGEISFDGHPL---GVEtPA 74
Cdd:PRK14243   11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLyapDVD-PV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  75 QARELgIAMVHQHFALFDTlSVTENVALGLST----GISAAEIEREIR---LLGE-KYGLEVDPASvvmeLSMGERQRVE 146
Cdd:PRK14243   88 EVRRR-IGMVFQKPNPFPK-SIYDNIAYGARIngykGDMDELVERSLRqaaLWDEvKDKLKQSGLS----LSGGQQQRLC 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 147 ILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIRELAD 204
Cdd:PRK14243  162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSD 218
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
268-487 1.02e-12

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 68.00  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGLRYVPEQRlghAAVPELSL 347
Cdd:PRK10895   19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEA---SIFRRLSV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 TANtyLTGDSLVRSGFILRDRARSfANLVIERFHVKTPNaEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVG 427
Cdd:PRK10895   96 YDN--LMAVLQIRDDLSAEQREDR-ANELMEEFHIEHLR-DSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 428 AAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGAL-SPAVPKPTISIEEVGR 487
Cdd:PRK10895  172 SVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLiAHGTPTEILQDEHVKR 232
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
5-216 1.08e-12

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 69.38  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAG--KSTLMKIIYGaarPDEGEISFDGHPLGVETPAQARELGIa 82
Cdd:NF000106   14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 mvHQ--HFALFDTLSVTENV-ALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLI 159
Cdd:NF000106   90 --HRpvR*GRRESFSGRENLyMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:NF000106  168 LDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
253-469 1.22e-12

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: 67.53  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 253 EMRHVS-APGSTRVcgIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRisGLRy 331
Cdd:cd03261     2 ELRGLTkSFGGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELY--RLR- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 332 vpeQRLG----HAAvpeL--SLTantylTGDSLvrsGFILRDRARSFANLVIERFHVK------TPNAEKAAGSLSGGNL 399
Cdd:cd03261    77 ---RRMGmlfqSGA---LfdSLT-----VFENV---AFPLREHTRLSEEEIREIVLEKleavglRGAEDLYPAELSGGMK 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 400 QKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03261   143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDG 213
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
9-208 1.64e-12

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: 69.81  E-value: 1.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   9 NITKRYPGItandhvSLDIAPG-----EVLAILGENGAGKSTLMKIIYGAARPDEGE------ISFDGHPLGVETPAQAR 77
Cdd:COG1245   346 DLTKSYGGF------SLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEvdedlkISYKPQYISPDYDGTVE 419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  78 ELgiamvhqhfaLFDTLSVTenvalgLSTGISAAEIEREIRL--LGEKYglevdpasvVMELSMGERQRVEILRALMTKP 155
Cdd:COG1245   420 EF----------LRSANTDD------FGSSYYKTEIIKPLGLekLLDKN---------VKDLSGGELQRVAIAACLSRDA 474
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 156 KLLILDEPTS-------VLTPQAVRKLFKtlhqlsSEGVSILFISHKLDEIRELADRCVV 208
Cdd:COG1245   475 DLYLLDEPSAhldveqrLAVAKAIRRFAE------NRGKTAMVVDHDIYLIDYISDRLMV 528
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
19-214 4.30e-12

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 68.38  E-value: 4.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  19 ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGhplgvetpaqarelGIAMVHQHFALFDTLSVTE 98
Cdd:PRK13545   39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--------------SAALIAISSGLNGQLTGIE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  99 NVAL-GLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFK 177
Cdd:PRK13545  105 NIELkGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2549828669 178 TLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK13545  185 KMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
5-215 6.41e-12

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 67.61  E-value: 6.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFdghplgvetpAQARELGIaMV 84
Cdd:PRK15064  320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW----------SENANIGY-YA 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  85 HQHFALFDT-LSVTENVALGLSTGisaaEIEREIR-LLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDE 162
Cdd:PRK15064  389 QDHAYDFENdLTLFDWMSQWRQEG----DDEQAVRgTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDE 464
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 163 PTSVLTPQAVRKLFKTLHQLssEGvSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK15064  465 PTNHMDMESIESLNMALEKY--EG-TLIFVSHDREFVSSLATRIIEITPDGVV 514
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
23-212 7.99e-12

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: 68.01  E-value: 7.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHplgvetpaqarelgIAMVHQhFALFDTLSVTENVAL 102
Cdd:TIGR01271  445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQ-TSWIMPGTIKDNIIF 509
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  103 GLS-------TGISAAEIEREIRLLGEKyglevdPASVVME----LSMGERQRVEILRALMTKPKLLILDEPTSVLTPQA 171
Cdd:TIGR01271  510 GLSydeyrytSVIKACQLEEDIALFPEK------DKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2549828669  172 VRKLFKT-LHQLSSEGVSILFIShKLDEIRElADRCVVLRAG 212
Cdd:TIGR01271  584 EKEIFEScLCKLMSNKTRILVTS-KLEHLKK-ADKILLLHEG 623
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
268-469 9.63e-12

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: 63.75  E-value: 9.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMaaasgeylceadrvllfnspvgeldthaRRISGLryvpeqrlghaavpeLSL 347
Cdd:cd03229    16 LNDVSLNIEAGEIVALLGPSGSGKSTLL----------------------------RCIAGL---------------EEP 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 TANTYLTGDSLVRSGFILRDRARSFANLVIERFHVkTPN---AEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGV 424
Cdd:cd03229    53 DSGSILIDGEDLTDLEDELPPLRRRIGMVFQDFAL-FPHltvLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2549828669 425 DVGAAAVIRNSLIRLRD-DGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03229   132 DPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDG 177
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
27-172 1.02e-11

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 64.48  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  27 IAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlgVETPAQARElgIAMVHQHFALFDTLSVTENVALglst 106
Cdd:PRK13543   34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT--ATRGDRSRF--MAYLGHLPGLKADLSTLENLHF---- 105
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 107 gISAAEIEREIRLLGEKY---GLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAV 172
Cdd:PRK13543  106 -LCGLHGRRAKQMPGSALaivGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGI 173
PLN03130 PLN03130
ABC transporter C family member; Provisional
22-215 1.12e-11

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 67.84  E-value: 1.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   22 HVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARE-LGIamVHQHFALF--------D 92
Cdd:PLN03130  1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKvLGI--IPQAPVLFsgtvrfnlD 1334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   93 TLSvtENVALGLSTGISAAEIEREIRllGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTS------- 165
Cdd:PLN03130  1335 PFN--EHNDADLWESLERAHLKDVIR--RNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAavdvrtd 1410
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2549828669  166 VLTPQAVRKLFKTlhqlssegVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:PLN03130  1411 ALIQKTIREEFKS--------CTMLIIAHRLNTIID-CDRILVLDAGRVV 1451
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
5-219 1.18e-11

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 64.81  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAA--RPDEGEISFDGHPLGVETPAQARELGIA 82
Cdd:PRK09580    2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MVHQHFALFDTLSVTenvaLGLSTGISAAE----------------IEREIRLLgeKYGLEVDPASVVMELSMGERQRVE 146
Cdd:PRK09580   82 MAFQYPVEIPGVSNQ----FFLQTALNAVRsyrgqepldrfdfqdlMEEKIALL--KMPEDLLTRSVNVGFSGGEKKRND 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 147 ILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHK---LDEIRelADRCVVLRAGKVVASVD 219
Cdd:PRK09580  156 ILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYqriLDYIK--PDYVHVLYQGRIVKSGD 229
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
1-215 1.37e-11

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 64.72  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   1 MTPRLSLRNITKRYPGITAnDHVSLDIAPGEVLAILGENGAGKS----TLMKIIYGAARPDEGEISFDGHPLgveTPAQA 76
Cdd:PRK10418    1 MPQQIELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV---APCAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  77 RELGIAMVHQH----FALFDTLSvtenvALGLSTGISAAEIEREIRLLG--EKYGLEvDPASVV----MELSMGERQRVE 146
Cdd:PRK10418   77 RGRKIATIMQNprsaFNPLHTMH-----THARETCLALGKPADDATLTAalEAVGLE-NAARVLklypFEMSGGMLQRMM 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 147 ILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK10418  151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
2-214 1.74e-11

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 66.73  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   2 TPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFdghplgvetpAQARELGI 81
Cdd:PRK10636  310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----------AKGIKLGY 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  82 AMVHQhfalFDTLSVTENvALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVME-LSMGERQRVEILRALMTKPKLLIL 160
Cdd:PRK10636  380 FAQHQ----LEFLRADES-PLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLL 454
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLhqLSSEGvSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK10636  455 DEPTNHLDLDMRQALTEAL--IDFEG-ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
256-471 2.41e-11

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: 65.69  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 256 HVSAPGSTRVcGIDNVSLAVRAGEIVGIAGISGNGQ---ARFMAAASGEYLCEADRVLLFNSPVGELDTHAR--RISglr 330
Cdd:COG1123    11 SVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKstlALALMGLLPHGGRISGEVLLDGRDLLELSEALRgrRIG--- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 331 YVPEQrlghaavPELSLTANTylTGDSLV---RSGFILRDRARSFANLVIERFHVKTPnAEKAAGSLSGGNLQKFIMGRE 407
Cdd:COG1123    87 MVFQD-------PMTQLNPVT--VGDQIAealENLGLSRAEARARVLELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMA 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 408 ILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:COG1123   157 LALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
6-181 2.74e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 65.91  E-value: 2.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   6 SLRNITKRYPG---ITANdhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEIsfdghplgveTPAQARELGIA 82
Cdd:PRK11819    8 TMNRVSKVVPPkkqILKD--ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA----------RPAPGIKVGYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  83 MvhQHFALFDTLSVTENVALGLS---------TGISA--AEIEREIRLLGEKYG-----------------LEV------ 128
Cdd:PRK11819   76 P--QEPQLDPEKTVRENVEEGVAevkaaldrfNEIYAayAEPDADFDALAAEQGelqeiidaadawdldsqLEIamdalr 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 129 --DPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQ 181
Cdd:PRK11819  154 cpPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHD 208
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
268-469 2.86e-11

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: 62.94  E-value: 2.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAA-------ASGEylceadrVLLFNSPVGELDthaRRISglrYVPEQRLGHA 340
Cdd:cd03235    15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAilgllkpTSGS-------IRVFGKPLEKER---KRIG---YVPQRRSIDR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 341 AVPelsltantyLTGDSLVRSG--------FILRDRARSFANLVIER---FHVktpnAEKAAGSLSGGNLQKFIMGREIL 409
Cdd:cd03235    82 DFP---------ISVRDVVLMGlyghkglfRRLSKADKAKVDEALERvglSEL----ADRQIGELSGGQQQRVLLARALV 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 410 NRPRVLLVHQPTWGVDV-GAAAVIRNsLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03235   149 QDPDLLLLDEPFAGVDPkTQEDIYEL-LRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
9-208 3.13e-11

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 65.60  E-value: 3.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   9 NITKRYPGItandhvSLDIAPG-----EVLAILGENGAGKSTLMKIIYGAARPDEGEISFDghplgvetpaqareLGIAM 83
Cdd:PRK13409  345 DLTKKLGDF------SLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--------------LKISY 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  84 VHQHFALFDTLSVTE---NVALGLSTGISAAEIEREIRL--LGEKYglevdpasvVMELSMGERQRVEILRALMTKPKLL 158
Cdd:PRK13409  405 KPQYIKPDYDGTVEDllrSITDDLGSSYYKSEIIKPLQLerLLDKN---------VKDLSGGELQRVAIAACLSRDADLY 475
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 159 ILDEPTS-------VLTPQAVRKLFKtlhqlsSEGVSILFISHKLDEIRELADRCVV 208
Cdd:PRK13409  476 LLDEPSAhldveqrLAVAKAIRRIAE------EREATALVVDHDIYMIDYISDRLMV 526
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
268-471 3.62e-11

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


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 62.77  E-value: 3.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQ-------ARFMAAASGE-------YLCEADRVllfnspvgeldthARRISglrYVP 333
Cdd:cd03265    16 VRGVSFRVRRGEIFGLLGPNGAGKtttikmlTTLLKPTSGRatvaghdVVREPREV-------------RRRIG---IVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 334 EQRlghAAVPELSLTANTYLTGDSLVRSGFILRDRARSfanlVIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPR 413
Cdd:cd03265    80 QDL---SVDDELTGWENLYIHARLYGVPGAERRERIDE----LLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 414 VLLVHQPTWGVDVGAaaviRNSLIR-----LRDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03265   152 VLFLDEPTIGLDPQT----RAHVWEyieklKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
23-213 3.72e-11

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: 62.49  E-value: 3.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGhplgvetpaqarelGIAMVHQHFALFDTlSVTENVAL 102
Cdd:cd03250    24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWIQNG-TIRENILF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 103 GLS-------TGISAAEIEREIRLL--------GEKyGlevdpasvvMELSMGERQRVEILRALMTKPKLLILDEPTSVL 167
Cdd:cd03250    89 GKPfdeeryeKVIKACALEPDLEILpdgdlteiGEK-G---------INLSGGQKQRISLARAVYSDADIYLLDDPLSAV 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2549828669 168 TPQAVRKLF-KTLHQLSSEGVSILFISHKLDEIRElADRCVVLRAGK 213
Cdd:cd03250   159 DAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
4-214 5.58e-11

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: 65.35  E-value: 5.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669    4 RLSLRNITKRY-PGIT-ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvETPAQARELGI 81
Cdd:TIGR00957 1284 RVEFRNYCLRYrEDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA-KIGLHDLRFKI 1362
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   82 AMVHQHFALFdtlSVTENVALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVME-------LSMGERQRVEILRALMTK 154
Cdd:TIGR00957 1363 TIIPQDPVLF---SGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRK 1439
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  155 PKLLILDEPTSVLTPQAvRKLFKTLHQLSSEGVSILFISHKLDEIRELAdRCVVLRAGKV 214
Cdd:TIGR00957 1440 TKILVLDEATAAVDLET-DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEV 1497
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
19-214 5.66e-11

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 62.91  E-value: 5.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  19 ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHplgvetpaqarelgIAMVHQHFALFDTLSVTE 98
Cdd:PRK13546   39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--------------VSVIAISAGLSGQLTGIE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  99 NVALG-LSTGISAAEIER------EIRLLGEkygLEVDPasvVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQA 171
Cdd:PRK13546  105 NIEFKmLCMGFKRKEIKAmtpkiiEFSELGE---FIYQP---VKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2549828669 172 VRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK13546  179 AQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
3-215 8.49e-11

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 62.81  E-value: 8.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL--- 79
Cdd:PRK14271   20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVlef 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  80 --GIAMVHQHFALFdTLSVTENVAlglsTGISAAEI--EREIRLLGEKYGLEVDPASVVME--------LSMGERQRVEI 147
Cdd:PRK14271  100 rrRVGMLFQRPNPF-PMSIMDNVL----AGVRAHKLvpRKEFRGVAQARLTEVGLWDAVKDrlsdspfrLSGGQQQLLCL 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 148 LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEgVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK14271  175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLV 241
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
2-194 1.08e-10

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 63.88  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   2 TPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGaarpdegeisfdGHPLG----VETPAQAR 77
Cdd:PRK10938  258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG------------DHPQGysndLTLFGRRR 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  78 ELG---------IAMVHQHFALFDTLSVT-ENVAL-GL--STGISAAEIEREiRLLGEKY----GLEVDPA-SVVMELSM 139
Cdd:PRK10938  326 GSGetiwdikkhIGYVSSSLHLDYRVSTSvRNVILsGFfdSIGIYQAVSDRQ-QKLAQQWldilGIDKRTAdAPFHSLSW 404
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 140 GERQRVEILRALMTKPKLLILDEPTSVLTP---QAVRKLfktLHQLSSEG-VSILFISH 194
Cdd:PRK10938  405 GQQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRF---VDVLISEGeTQLLFVSH 460
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
239-469 1.14e-10

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 63.22  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 239 TVREGTAKAGEVVFEMRHVSapgstRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGE 318
Cdd:NF000106    5 TISNGARNAVEVRGLVKHFG-----EVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCAN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 319 LDTHARRISGLRYVpeqRLGHAAvpELSLTANTYLTGDSLVRSgfilRDRARSFANLVIERFHVkTPNAEKAAGSLSGGN 398
Cdd:NF000106   80 RRALRRTIG*HRPV---R*GRRE--SFSGRENLYMIGR*LDLS----RKDARARADELLERFSL-TEAAGRAAAKYSGGM 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 399 LQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:NF000106  150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRG 220
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
4-214 1.25e-10

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


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 62.18  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYP--GITANDHVSLDIAPGEVLAILGENGAGKSTL----MKIIYgaarpDEGEISFDGHPLGVETPAQAR 77
Cdd:cd03289     2 QMTVKDLTAKYTegGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVPLQKWR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  78 ElGIAMVHQHFALFdtlSVTENVALGLSTGISAAEIEREIRLLGEKYGLEVDPASV--VME-----LSMGERQRVEILRA 150
Cdd:cd03289    77 K-AFGVIPQKVFIF---SGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfVLVdggcvLSHGHKQLMCLARS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAVRKLFKTLHQlSSEGVSILFISHKLDEIRElADRCVVLRAGKV 214
Cdd:cd03289   153 VLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
253-466 1.28e-10

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: 61.33  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 253 EMRHVS---APGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQ-------ARFMAAASGEylceadrVLLFNSPVGELDTH 322
Cdd:cd03293     2 EVRNVSktyGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKstllriiAGLERPTSGE-------VLVDGEPVTGPGPD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 323 arrisgLRYVPEQrlgHAAVPELSLTANTYLtGDSLVR-SGFILRDRARSFANLV-IERFHVKTPNAekaagsLSGGNLQ 400
Cdd:cd03293    75 ------RGYVFQQ---DALLPWLTVLDNVAL-GLELQGvPKAEARERAEELLELVgLSGFENAYPHQ------LSGGMRQ 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 401 KFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVM 466
Cdd:cd03293   139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVL 205
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
261-469 1.35e-10

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: 61.40  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 261 GSTRVcgIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGLRYVPEQrlgHA 340
Cdd:cd03218    11 GKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQE---AS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 341 AVPELSLTANTYLtgdsLVRSGFILRDRARSFANLVIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQP 420
Cdd:cd03218    86 IFRKLTVEENILA----VLEIRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2549828669 421 TWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03218   161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEG 209
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
16-217 2.17e-10

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 61.44  E-value: 2.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  16 GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFdghpLGVETPAQARELGIAMVHQHFALFDTLS 95
Cdd:PRK15056   19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI----LGQPTRQALQKNLVAYVPQSEEVDWSFP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  96 V-TENVALGLSTG------ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLT 168
Cdd:PRK15056   95 VlVEDVVMMGRYGhmgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2549828669 169 PQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRaGKVVAS 217
Cdd:PRK15056  175 VKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLAS 222
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
4-201 2.96e-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: 63.01  E-value: 2.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669    4 RLSLRNITKRYP--GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARpDEGEISFDGHPLGVETPAQARElGI 81
Cdd:TIGR01271 1217 QMDVQGLTAKYTeaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRK-AF 1294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   82 AMVHQHFALFdtlSVTENVALGLSTGISAAEIEREIRLLGEKYGLEVDPASV--VME-----LSMGERQRVEILRALMTK 154
Cdd:TIGR01271 1295 GVIPQKVFIF---SGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfVLVdggyvLSNGHKQLMCLARSILSK 1371
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2549828669  155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILfISHKLDEIRE 201
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVIL-SEHRVEALLE 1417
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
253-471 3.38e-10

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: 59.81  E-value: 3.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 253 EMRHVS---APGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGeyLCEAD--RVLLFNSPVGELDTHARriS 327
Cdd:cd03255     2 ELKNLSktyGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG--LDRPTsgEVRVDGTDISKLSEKEL--A 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 328 GLR-----YVPEQrlgHAAVPELSLTANT----YLTGdslvRSGFILRDRARSfanlVIERFHVKTpNAEKAAGSLSGGN 398
Cdd:cd03255    78 AFRrrhigFVFQS---FNLLPDLTALENVelplLLAG----VPKKERRERAEE----LLERVGLGD-RLNHYPSELSGGQ 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 399 LQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEiDELFEISDRIAVMYRGAL 471
Cdd:cd03255   146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
23-212 3.41e-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: 61.03  E-value: 3.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHplgvetpaqarelgIAMVHQhFALFDTLSVTENVAL 102
Cdd:cd03291    56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQ-FSWIMPGTIKENIIF 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 103 GLS-------TGISAAEIEREIRLLGEKYGLEVDPASVVmeLSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKL 175
Cdd:cd03291   121 GVSydeyrykSVVKACQLEEDITKFPEKDNTVLGEGGIT--LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2549828669 176 F-KTLHQLSSEGVSILfISHKLDEIRElADRCVVLRAG 212
Cdd:cd03291   199 FeSCVCKLMANKTRIL-VTSKMEHLKK-ADKILILHEG 234
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
57-217 4.37e-10

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 62.35  E-value: 4.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   57 DEGEISFDGHPLGVETPAQARELgIAMVHQHFALFDtLSVTENVALG--------LSTGISAAEIEREIRLLGEKYGLEV 128
Cdd:PTZ00265  1275 NSGKILLDGVDICDYNLKDLRNL-FSIVSQEPMLFN-MSIYENIKFGkedatredVKRACKFAAIDEFIESLPNKYDTNV 1352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  129 DPASvvMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEG-VSILFISHKLDEIRElADRCV 207
Cdd:PTZ00265  1353 GPYG--KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKR-SDKIV 1429
                          170
                   ....*....|....
gi 2549828669  208 VL----RAGKVVAS 217
Cdd:PTZ00265  1430 VFnnpdRTGSFVQA 1443
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
261-471 4.37e-10

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 60.31  E-value: 4.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 261 GSTRVcgIDNVSLAVRAGEIVGIAGISGNGQARFM------------AAASGEYLCEADRVllFNSPVGELdthARRISG 328
Cdd:PRK14247   14 GQVEV--LDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrlielypeARVSGEVYLDGQDI--FKMDVIEL---RRRVQM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 329 LRYVPEqrlghaAVPELSLTANTYL--TGDSLVRSGFILRDRAR---SFANLVIErfhVKTpNAEKAAGSLSGGNLQKFI 403
Cdd:PRK14247   87 VFQIPN------PIPNLSIFENVALglKLNRLVKSKKELQERVRwalEKAQLWDE---VKD-RLDAPAGKLSGGQQQRLC 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 404 MGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDgAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:PRK14247  157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQI 223
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
268-471 5.60e-10

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: 59.14  E-value: 5.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRiSGLRYVPEQrlghaavPEL-- 345
Cdd:cd03245    20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLR-RNIGYVPQD-------VTLfy 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 346 -SLTANTYLtGDSLVRSGFILrdRARSFAnlVIERFHVKTPN------AEKAAGsLSGGNLQKFIMGREILNRPRVLLVH 418
Cdd:cd03245    92 gTLRDNITL-GAPLADDERIL--RAAELA--GVTDFVNKHPNgldlqiGERGRG-LSGGQRQAVALARALLNDPPILLLD 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 419 QPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEidELFEISDRIAVMYRGAL 471
Cdd:cd03245   166 EPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP--SLLDLVDRIIVMDSGRI 216
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
253-487 7.01e-10

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 59.17  E-value: 7.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 253 EMRHVS-APGSTRVcgIDNVSLAVRAGEIVGIAGISGNGQ-------ARFMAAASGEylceadrVLLFNSPVGELDTHAR 324
Cdd:cd03300     2 ELENVSkFYGGFVA--LDGVSLDIKEGEFFTLLGPSGCGKttllrliAGFETPTSGE-------ILLDGKDITNLPPHKR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 325 RISGL--RYvpeqrlghAAVPELSLTANTyltgdslvrsGFILRDRARSFANL---VIERFH-VKTPN-AEKAAGSLSGG 397
Cdd:cd03300    73 PVNTVfqNY--------ALFPHLTVFENI----------AFGLRLKKLPKAEIkerVAEALDlVQLEGyANRKPSQLSGG 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 398 NLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRGalspavp 476
Cdd:cd03300   135 QQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKG------- 207
                         250
                  ....*....|.
gi 2549828669 477 kptiSIEEVGR 487
Cdd:cd03300   208 ----KIQQIGT 214
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
258-471 8.69e-10

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 61.57  E-value: 8.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  258 SAPGSTRVCgidnvsLAVRAGEIVGIAGISGNGQARFMAAASGEY-LCEADRVLLFNSPVGEL-DTHarriSGLRYVPEq 335
Cdd:TIGR01257 1951 SSPAVDRLC------VGVRPGECFGLLGVNGAGKTTTFKMLTGDTtVTSGDATVAGKSILTNIsDVH----QNMGYCPQ- 2019
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  336 rlgHAAVPELsltantyLTGdslvRSGFILRDRARSFANLVIER---FHVK----TPNAEKAAGSLSGGNLQKFIMGREI 408
Cdd:TIGR01257 2020 ---FDAIDDL-------LTG----REHLYLYARLRGVPAEEIEKvanWSIQslglSLYADRLAGTYSGGNKRKLSTAIAL 2085
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669  409 LNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAF 2148
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
266-471 1.11e-09

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: 58.36  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 266 CGIDNVSLAVRAGeIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGlrYVPEQRLGHAavpel 345
Cdd:cd03264    14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIG--YLPQEFGVYP----- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 346 SLTANTYLtgDSLVRSGFILRDRARSFANLVIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVD 425
Cdd:cd03264    86 NFTVREFL--DYIAWLKGIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2549828669 426 VGAAAVIRNSLIRLRDDgaAIIVVSEEIDELFE-ISDRIAVMYRGAL 471
Cdd:cd03264   163 PEERIRFRNLLSELGED--RIVILSTHIVEDVEsLCNQVAVLNKGKL 207
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
264-469 1.28e-09

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 58.74  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 264 RVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDThaRRIsglryvpeQRLGHAAVP 343
Cdd:PRK11614   17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT--AKI--------MREAVAIVP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 344 ELSLTANTYLTGDSLVRSGFIL-RDRARSFANLVIERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTW 422
Cdd:PRK11614   87 EGRRVFSRMTVEENLAMGGFFAeRDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSL 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2549828669 423 GVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK11614  167 GLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENG 213
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
22-215 1.40e-09

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 60.89  E-value: 1.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   22 HVSLDIAPGEVLAILGENGAGKSTLMKII----YGAARPDEGEISFDGHPLGVETPAQAREL---GIAMVH-QHFALFDT 93
Cdd:TIGR00956   79 PMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRGDVvynAETDVHfPHLTVGET 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   94 LsvteNVALGLST------GISAAE-IEREIRLLGEKYGLEVDPASVVME-----LSMGERQRVEILRALMTKPKLLILD 161
Cdd:TIGR00956  159 L----DFAARCKTpqnrpdGVSREEyAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWD 234
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669  162 EPT----SVLTPQAVRKLFKTLHQL-SSEGVSILFIShklDEIRELADRCVVLRAGKVV 215
Cdd:TIGR00956  235 NATrgldSATALEFIRALKTSANILdTTPLVAIYQCS---QDAYELFDKVIVLYEGYQI 290
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
3-164 1.92e-09

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 59.75  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRL-----SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISfdghpLGvETpaqar 77
Cdd:PRK11819  318 PRLgdkviEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-----IG-ET----- 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  78 eLGIAMVHQ-HFALFDTLSVTENVALGLstgisaaeierEIRLLGEKyglEV--------------DPASVVMELSMGER 142
Cdd:PRK11819  387 -VKLAYVDQsRDALDPNKTVWEEISGGL-----------DIIKVGNR---EIpsrayvgrfnfkggDQQKKVGVLSGGER 451
                         170       180
                  ....*....|....*....|..
gi 2549828669 143 QRVEILRALMTKPKLLILDEPT 164
Cdd:PRK11819  452 NRLHLAKTLKQGGNVLLLDEPT 473
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
15-212 2.03e-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: 57.73  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  15 PGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG---IAMVHQHFALF 91
Cdd:cd03290    12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQKPWLL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  92 DTlSVTENVALG-------LSTGISAAEIEREIRLLgeKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:cd03290    92 NA-TVEENITFGspfnkqrYKAVTDACSLQPDIDLL--PFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2549828669 165 SVLTPQAVRKLFKT--LHQLSSEGVSILFISHKLDEIRElADRCVVLRAG 212
Cdd:cd03290   169 SALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
268-469 2.55e-09

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


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 57.67  E-value: 2.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEAD---RVLLFNSPVgELDTHARRISglrYVPEQrlgHAAVPe 344
Cdd:cd03234    23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTtsgQILFNGQPR-KPDQFQKCVA---YVRQD---DILLP- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 345 lSLTANTYLTGDSLVRSGFILRDRARSFANLVIERFHVK-TPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWG 423
Cdd:cd03234    95 -GLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLAlTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2549828669 424 VDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03234   174 LDSFTALNLVSTLSQLaRRNRIVILTIHQPRSDLFRLFDRILLLSSG 220
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
23-227 3.49e-09

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 59.66  E-value: 3.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISF-DGHPLGVETPAQARElGIAMVHQHFALFDTlSVTENVA 101
Cdd:PTZ00265   404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRS-KIGVVSQDPLLFSN-SIKNNIK 481
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  102 LGL----------------------------------------------STGISAAEIERE------------------- 116
Cdd:PTZ00265   482 YSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdSNELIEMRKNYQtikdsevvdvskkvlihdf 561
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  117 IRLLGEKYGLEVdpASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLS-SEGVSILFISHK 195
Cdd:PTZ00265   562 VSALPDKYETLV--GSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHR 639
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2549828669  196 LDEIRE------LADRCVVLRAGKVVASVDPKAESEEN 227
Cdd:PTZ00265   640 LSTIRYantifvLSNRERGSTVDVDIIGEDPTKDNKEN 677
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
26-167 3.65e-09

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 57.42  E-value: 3.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  26 DIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGE-------ISFDGHPLGVETPAQARELgiamvhqhfaLFdtlSVTE 98
Cdd:cd03237    21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDieieldtVSYKPQYIKADYEGTVRDL----------LS---SITK 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669  99 NVAlglstgiSAAEIEREIrllGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVL 167
Cdd:cd03237    88 DFY-------THPYFKTEI---AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
268-471 3.70e-09

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: 56.74  E-value: 3.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGlrYVPEqrlgHAAVPELsL 347
Cdd:cd03263    18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLG--YCPQ----FDALFDE-L 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 TANTYLTGDSLVRSGFilRDRARSFANLVIErfHVK-TPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDV 426
Cdd:cd03263    91 TVREHLRFYARLKGLP--KSEIKEEVELLLR--VLGlTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2549828669 427 GAAAVIRNSLIRLRDdGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03263   167 ASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKL 210
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
265-469 8.53e-09

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 57.04  E-value: 8.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 265 VCGIDNVSLAVRAGEIVGIAGISGNG--QARF----MAAASGEYLCEAdrvlLFNspvgeldthARRISGLryvPEQRLG 338
Cdd:PRK09473   29 VTAVNDLNFSLRAGETLGIVGESGSGksQTAFalmgLLAANGRIGGSA----TFN---------GREILNL---PEKELN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 339 HAAVPELSL-------TANTYL-TGDSLVRsgfILR-----DRARSFANLVIERFHVKTPNAEKAAG----SLSGGNLQK 401
Cdd:PRK09473   93 KLRAEQISMifqdpmtSLNPYMrVGEQLME---VLMlhkgmSKAEAFEESVRMLDAVKMPEARKRMKmyphEFSGGMRQR 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 402 FIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK09473  170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 238
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
137-220 9.76e-09

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 58.10  E-value: 9.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 137 LSMGERQRVEILRALM---TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRElADRCVVL---- 209
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKT-ADYIIDLgpeg 908
                          90
                  ....*....|...
gi 2549828669 210 --RAGKVVASVDP 220
Cdd:TIGR00630 909 gdGGGTVVASGTP 921
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
136-220 1.26e-08

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 56.08  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 136 ELSMGERQRVEILRALM---TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIReLADRCVVL--- 209
Cdd:cd03271   169 TLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CADWIIDLgpe 247
                          90
                  ....*....|....
gi 2549828669 210 ---RAGKVVASVDP 220
Cdd:cd03271   248 ggdGGGQVVASGTP 261
PTZ00243 PTZ00243
ABC transporter; Provisional
23-214 1.26e-08

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 57.87  E-value: 1.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   23 VSLDIAPGEVLAILGENGAGKSTL----MKIIYGAArpdeGEISFDGHPLGVETPAQARELgIAMVHQHFALFDTlSVTE 98
Cdd:PTZ00243  1329 VSFRIAPREKVGIVGRTGSGKSTLlltfMRMVEVCG----GEIRVNGREIGAYGLRELRRQ-FSMIPQDPVLFDG-TVRQ 1402
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   99 NVALGLSTgiSAAEIEREIRLLG-------EKYGLEvdpaSVVME----LSMGERQRVEILRALMTKPKLLIL-DEPTSV 166
Cdd:PTZ00243  1403 NVDPFLEA--SSAEVWAALELVGlrervasESEGID----SRVLEggsnYSVGQRQLMCMARALLKKGSGFILmDEATAN 1476
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2549828669  167 LTPQAVRKLFKTLHQLSSeGVSILFISHKLDEIRELaDRCVVLRAGKV 214
Cdd:PTZ00243  1477 IDPALDRQIQATVMSAFS-AYTVITIAHRLHTVAQY-DKIIVMDHGAV 1522
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
268-471 1.53e-08

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: 55.18  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELD-THARRISGlrYVPEQRLghaaVPELS 346
Cdd:cd03252    18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADpAWLRRQVG--VVLQENV----LFNRS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 347 LTANTYLTGDSLVRSGFILRDR---ARSFANLVIERFhvKTPNAEKAAGsLSGGNLQKFIMGREILNRPRVLLVHQPTWG 423
Cdd:cd03252    92 IRDNIALADPGMSMERVIEAAKlagAHDFISELPEGY--DTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIFDEATSA 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2549828669 424 VDVGAAAVIRNSLIRLRdDGAAIIVVSEEIDELfEISDRIAVMYRGAL 471
Cdd:cd03252   169 LDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTV-KNADRIIVMEKGRI 214
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
268-486 2.06e-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: 55.04  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISglrYVPEQrlgHAAVPELSL 347
Cdd:cd03296    18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVG---FVFQH---YALFRHMTV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 TANTyltgdslvrsGFILRDRARSF---ANLVIERFH-----VKTPN-AEKAAGSLSGGNLQKFIMGREILNRPRVLLVH 418
Cdd:cd03296    92 FDNV----------AFGLRVKPRSErppEAEIRAKVHellklVQLDWlADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 419 QPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRGAlspavpkptisIEEVG 486
Cdd:cd03296   162 EPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGR-----------IEQVG 219
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
28-204 3.08e-08

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


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 54.68  E-value: 3.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  28 APGEVLAILGENGAGKSTLMKIIYGAARPDEGEisFDGHP---------LGVETP---AQARELGIAMVH--QHFALFDT 93
Cdd:cd03236    24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeildefRGSELQnyfTKLLEGDVKVIVkpQYVDLIPK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  94 lSVTENVALGLSTGISAAEIEREIRLLGEKYGLEVDpasvVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVR 173
Cdd:cd03236   102 -AVKGKVGELLKKKDERGKLDELVDQLELRHVLDRN----IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2549828669 174 KLFKTLHQLSSEGVSILFISHKLDEIRELAD 204
Cdd:cd03236   177 NAARLIRELAEDDNYVLVVEHDLAVLDYLSD 207
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
21-205 3.15e-08

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 56.33  E-value: 3.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHP----LGVETPA--------------QAREL--- 79
Cdd:PRK10636   18 DNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWqlawVNQETPAlpqpaleyvidgdrEYRQLeaq 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  80 -----------GIAMVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRllgekyglevdpasvvmELSMGERQRVEI 147
Cdd:PRK10636   98 lhdanerndghAIATIHGKLDAIDAWTIRSRAASLLHgLGFSNEQLERPVS-----------------DFSGGWRMRLNL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 148 LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHqlSSEGVSILfISHKLDEIRELADR 205
Cdd:PRK10636  161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLK--SYQGTLIL-ISHDRDFLDPIVDK 215
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
268-421 3.25e-08

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: 52.65  E-value: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRiSGLRYVPEQrlgHAAVPELSL 347
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLR-KEIGYVFQD---PQLFPRLTV 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 348 TANTYLTGDSLVRSGFILRDRARSFANLVIERFHVKTPnAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPT 421
Cdd:pfam00005  77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRP-VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
7-167 4.43e-08

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 55.73  E-value: 4.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   7 LRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISfdghplgVETpaqarELGIAMVHQ 86
Cdd:PRK11147  322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-------CGT-----KLEVAYFDQ 389
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  87 HFALFD-TLSVTENVALGLSTgISAAEIEREIrlLGEKYGLEVDPASV---VMELSMGERQRVeILRALMTKP-KLLILD 161
Cdd:PRK11147  390 HRAELDpEKTVMDNLAEGKQE-VMVNGRPRHV--LGYLQDFLFHPKRAmtpVKALSGGERNRL-LLARLFLKPsNLLILD 465

                  ....*.
gi 2549828669 162 EPTSVL 167
Cdd:PRK11147  466 EPTNDL 471
PLN03073 PLN03073
ABC transporter F family; Provisional
33-214 4.70e-08

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 55.64  E-value: 4.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  33 LAILGENGAGKSTLMKIIYGAARPDEGeisfdghplgveTPAQARELGIAMVHQHFAlfDTLSVTENVALGLSTGISAAe 112
Cdd:PLN03073  538 IAMVGPNGIGKSTILKLISGELQPSSG------------TVFRSAKVRMAVFSQHHV--DGLDLSSNPLLYMMRCFPGV- 602
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 113 IEREIRLLGEKYGLEVDPASVVM-ELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSegvSILF 191
Cdd:PLN03073  603 PEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG---GVLM 679
                         170       180
                  ....*....|....*....|...
gi 2549828669 192 ISHKLDEIRELADRCVVLRAGKV 214
Cdd:PLN03073  680 VSHDEHLISGSVDELWVVSEGKV 702
cbiO PRK13644
energy-coupling factor transporter ATPase;
268-469 6.29e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 53.84  E-value: 6.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDT--HARRISGLRYV-PE-QRLGHAAVP 343
Cdd:PRK13644   18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlqGIRKLVGIVFQnPEtQFVGRTVEE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 344 ELSLTAntyltgDSLVRSGFILRDRA-RSFANLVIERFHVKTPNaekaagSLSGGNLQKFIMGREILNRPRVLLVHQPTW 422
Cdd:PRK13644   98 DLAFGP------ENLCLPPIEIRKRVdRALAEIGLEKYRHRSPK------TLSGGQGQCVALAGILTMEPECLIFDEVTS 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2549828669 423 GVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELfEISDRIAVMYRG 469
Cdd:PRK13644  166 MLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRG 211
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
253-471 9.16e-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: 52.80  E-value: 9.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 253 EMRHVSAPGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELdtHARRISGLRyv 332
Cdd:cd03292     2 EFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDL--RGRAIPYLR-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 333 peQRLGHA-----AVPELSLTANTYLtgdSLVRSGFILRDRARSFANlVIERFHVKTPNAEKAAGsLSGGNLQKFIMGRE 407
Cdd:cd03292    78 --RKIGVVfqdfrLLPDRNVYENVAF---ALEVTGVPPREIRKRVPA-ALELVGLSHKHRALPAE-LSGGEQQRVAIARA 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 408 ILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAiIVVSEEIDELFE-ISDRIAVMYRGAL 471
Cdd:cd03292   151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTT-VVVATHAKELVDtTRHRVIALERGKL 214
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
3-217 1.33e-07

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 51.55  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   3 PRLSLRNITKrypgitandhVSLDIAPGEVLAILGENGAGKSTLMK-IIY--GAARPDEGEISFDGHPLgvetpaqarel 79
Cdd:cd03238     4 SGANVHNLQN----------LDVSIPLNVLVVVTGVSGSGKSTLVNeGLYasGKARLISFLPKFSRNKL----------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  80 giamvhqhfALFDTLSVTENVALGLSTgisaaeiereirlLGEKYGlevdpasvvmELSMGERQRVEILRALM--TKPKL 157
Cdd:cd03238    63 ---------IFIDQLQFLIDVGLGYLT-------------LGQKLS----------TLSGGELQRVKLASELFsePPGTL 110
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRElADRCVVL------RAGKVVAS 217
Cdd:cd03238   111 FILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVFS 175
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
390-471 1.90e-07

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: 51.80  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 390 AAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDgAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03260   138 HALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNG 216

                  ..
gi 2549828669 470 AL 471
Cdd:cd03260   217 RL 218
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
26-209 1.99e-07

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 51.03  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  26 DIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGhplgvETPAqarelgiamvhqhfalfdtlsvtenvalgls 105
Cdd:cd03222    21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-----ITPV------------------------------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 106 tgisaaeiereirllgekygleVDPASVvmELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE 185
Cdd:cd03222    65 ----------------------YKPQYI--DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
                         170       180
                  ....*....|....*....|....*
gi 2549828669 186 GV-SILFISHKLDEIRELADRCVVL 209
Cdd:cd03222   121 GKkTALVVEHDLAVLDYLSDRIHVF 145
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
378-471 2.08e-07

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: 50.50  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 378 ERFHVKTPNAEKAAG-----SLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEE 452
Cdd:cd03216    62 KEVSFASPRDARRAGiamvyQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHR 141
                          90
                  ....*....|....*....
gi 2549828669 453 IDELFEISDRIAVMYRGAL 471
Cdd:cd03216   142 LDEVFEIADRVTVLRDGRV 160
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
268-476 3.08e-07

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 53.13  E-value: 3.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADR---VLLFNSPVGEldTHARRISGlrYVPEQRLghaAVPe 344
Cdd:TIGR00955  41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGsgsVLLNGMPIDA--KEMRAISA--YVQQDDL---FIP- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 345 lSLTANTYLTGDSLVRSG--------------FILRDRARSFANLVIerfhvKTPNAEKaagSLSGGNLQKFIMGREILN 410
Cdd:TIGR00955 113 -TLTVREHLMFQAHLRMPrrvtkkekrervdeVLQALGLRKCANTRI-----GVPGRVK---GLSGGERKRLAFASELLT 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 411 RPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVV----SEEIDELFeisDRIAVM------YRGALSPAVP 476
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFELF---DKIILMaegrvaYLGSPDQAVP 256
PLN03130 PLN03130
ABC transporter C family member; Provisional
22-178 4.66e-07

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 52.82  E-value: 4.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   22 HVSLDIAPGEVLAILGENGAGKSTLMKIIYG--AARPDeGEISFDGHplgvetpaqarelgIAMVHQHFALFDTlSVTEN 99
Cdd:PLN03130   635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGelPPRSD-ASVVIRGT--------------VAYVPQVSWIFNA-TVRDN 698
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  100 VALGLStgISAAEIEREIRLLGEKYGLEVDPASVVME-------LSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAV 172
Cdd:PLN03130   699 ILFGSP--FDPERYERAIDVTALQHDLDLLPGGDLTEigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVG 776

                   ....*.
gi 2549828669  173 RKLFKT 178
Cdd:PLN03130   777 RQVFDK 782
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
137-204 5.05e-07

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 52.34  E-value: 5.05e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 137 LSMGERQRVEILRALM---TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIReLAD 204
Cdd:COG0178   827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVIK-TAD 896
cbiO PRK13641
energy-coupling factor transporter ATPase;
256-501 5.11e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 51.37  E-value: 5.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 256 HVSAPGST-RVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVgELDTHARRISGLRyvpe 334
Cdd:PRK13641   10 YIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI-TPETGNKNLKKLR---- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 335 QRLGHA-AVPELSLTANTYLTGDSLVRSGF-ILRDRARSFANLVIERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRP 412
Cdd:PRK13641   85 KKVSLVfQFPEAQLFENTVLKDVEFGPKNFgFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 413 RVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGAL-SPAVPKPTISIEEvgrWMSG 491
Cdd:PRK13641  165 EILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLiKHASPKEIFSDKE---WLKK 241
                         250
                  ....*....|
gi 2549828669 492 LWPDSPFTQK 501
Cdd:PRK13641  242 HYLDEPATSR 251
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
261-476 5.76e-07

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 51.77  E-value: 5.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 261 GSTRVcgIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDthARRISglRYVpeqrlghA 340
Cdd:PRK09536   14 GDTTV--LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS--ARAAS--RRV-------A 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 341 AVP-ELSLTANtyLTGDSLVRSG-------FILRDRA-RSFANLVIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNR 411
Cdd:PRK09536   81 SVPqDTSLSFE--FDVRQVVEMGrtphrsrFDTWTETdRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQA 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 412 PRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALSPAVP 476
Cdd:PRK09536  158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGP 222
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
268-469 5.78e-07

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 51.34  E-value: 5.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGLryVPE-QRLGhaavPELS 346
Cdd:PRK13537   23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV--VPQfDNLD----PDFT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 347 LTANTYLTGDSLVRSGFILRDRARSFanLVIERFHVKtpnAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDV 426
Cdd:PRK13537   97 VRENLLVFGRYFGLSAAAARALVPPL--LEFAKLENK---ADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2549828669 427 GAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK13537  172 QARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
268-469 6.10e-07

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: 51.21  E-value: 6.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQ---AR-FM------AAASGEylceadrVLLFNSPVGELDTHARRisglryvpEQRL 337
Cdd:COG0444    21 VDGVSFDVRRGETLGLVGESGSGKstlARaILgllpppGITSGE-------ILFDGEDLLKLSEKELR--------KIRG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 338 GHAAV----PELSLtaNTYLT-GDSLVRSGFILRDRARSFA-NLVIERF-HVKTPNAEKAAGS----LSGGNLQKFIMGR 406
Cdd:COG0444    86 REIQMifqdPMTSL--NPVMTvGDQIAEPLRIHGGLSKAEArERAIELLeRVGLPDPERRLDRypheLSGGMRQRVMIAR 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 407 EILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:COG0444   164 ALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAG 227
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
261-453 8.07e-07

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 50.50  E-value: 8.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 261 GSTRVcgIDNVSLAVRAGEIVGIAGISGNGQARFMaaasgeylceadRVLLfnSPVGELDTHARRISGLR--YVPeQRLg 338
Cdd:PRK09544   15 GQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLV------------RVVL--GLVAPDEGVIKRNGKLRigYVP-QKL- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 339 HAAvPELSLTANTYLTGDSLVRSGFILRDRARSFANLVIERFHVKtpnaekaagsLSGGNLQKFIMGREILNRPRVLLVH 418
Cdd:PRK09544   77 YLD-TTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQK----------LSGGETQRVLLARALLNRPQLLVLD 145
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2549828669 419 QPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEI 453
Cdd:PRK09544  146 EPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
268-469 8.52e-07

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 50.99  E-value: 8.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGLRYvpeqrlGHAAVPELSL 347
Cdd:PRK11607   35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ------SYALFPHMTV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 TANTY--LTGDSLVRSGfiLRDRARSFANLV-IERFHVKTPNaekaagSLSGGNLQKFIMGREILNRPRVLLVHQPTWGV 424
Cdd:PRK11607  109 EQNIAfgLKQDKLPKAE--IASRVNEMLGLVhMQEFAKRKPH------QLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 425 DVgaaavirnsliRLRDD------------GAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK11607  181 DK-----------KLRDRmqlevvdilervGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
268-471 9.31e-07

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 49.99  E-value: 9.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQA-------RFMAAASGEylceadrVLLFNSPVGELD-THARRISGlrYVPeQRLGh 339
Cdd:cd03295    17 VNNLNLEIAKGEFLVLIGPSGSGKTttmkminRLIEPTSGE-------IFIDGEDIREQDpVELRRKIG--YVI-QQIG- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 340 aAVPELSLTANTYLTGDSLVRSGFILRDRARSFANLV---IERFhvktpnAEKAAGSLSGGNLQKFIMGREILNRPRVLL 416
Cdd:cd03295    86 -LFPHMTVEENIALVPKLLKWPKEKIRERADELLALVgldPAEF------ADRYPHELSGGQQQRVGVARALAADPPLLL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 417 VHQPTWGVDvgaaAVIRNSL----IRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03295   159 MDEPFGALD----PITRDQLqeefKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
268-464 9.53e-07

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 50.42  E-value: 9.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARF------MAAASGEYLCEAdRVLLFNSPVGELDTHARRISglRYV----PEQRL 337
Cdd:PRK14258   23 LEGVSMEIYQSKVTAIIGPSGCGKSTFlkclnrMNELESEVRVEG-RVEFFNQNIYERRVNLNRLR--RQVsmvhPKPNL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 338 GHAAVPElSLTANTYLTG-------DSLVRSGFilrdRARSFANLVIERFHvktpnaeKAAGSLSGGNLQKFIMGREILN 410
Cdd:PRK14258  100 FPMSVYD-NVAYGVKIVGwrpkleiDDIVESAL----KDADLWDEIKHKIH-------KSALDLSGGQQQRLCIARALAV 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 411 RPRVLLVHQPTWGVDVGAAAVIRNSL--IRLRDDgAAIIVVSEEIDELFEISDRIA 464
Cdd:PRK14258  168 KPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSE-LTMVIVSHNLHQVSRLSDFTA 222
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
29-196 1.10e-06

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: 51.32  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  29 PGEVLAILGENGAGKSTLMKIIYGAARPDEGEISfdghplgvetpaqaRELGIAMVHQHFA---LFDTLsvtENVALGls 105
Cdd:COG1245    98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYD--------------EEPSWDEVLKRFRgteLQDYF---KKLANG-- 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 106 tGISAA------------------EI-----ER-EIRLLGEKYGLE--VDPAsvVMELSMGERQRVEILRALMTKPKLLI 159
Cdd:COG1245   159 -EIKVAhkpqyvdlipkvfkgtvrELlekvdERgKLDELAEKLGLEniLDRD--ISELSGGELQRVAIAAALLRDADFYF 235
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2549828669 160 LDEPTSVLTpqaVR---KLFKTLHQLSSEGVSILFISHKL 196
Cdd:COG1245   236 FDEPSSYLD---IYqrlNVARLIRELAEEGKYVLVVEHDL 272
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
394-471 1.20e-06

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: 49.18  E-value: 1.20e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 394 LSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03301   131 LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
268-471 1.28e-06

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: 48.75  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRisglryvpeQRLGhaavpelsl 347
Cdd:cd03246    18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG---------DHVG--------- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 tantYLTGDSLVRSGFIlrdrarsfanlvierfhvktpnaekAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVG 427
Cdd:cd03246    80 ----YLPQDDELFSGSI-------------------------AENILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2549828669 428 AAAVIRNSLIRLRDDGAAIIVVSEEIdELFEISDRIAVMYRGAL 471
Cdd:cd03246   131 GERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
265-500 1.43e-06

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 50.19  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 265 VCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASG----EYLCEADRvLLFNSpvgeldtharrISGLRYVPEQR---L 337
Cdd:PRK15093   20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdNWRVTADR-MRFDD-----------IDLLRLSPRERrklV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 338 GHAAV-----PELSLTANTYLtGDSLVRS--GFILRDRARSFANL----VIERFH-VKTPNAEKAAGS----LSGGNLQK 401
Cdd:PRK15093   88 GHNVSmifqePQSCLDPSERV-GRQLMQNipGWTYKGRWWQRFGWrkrrAIELLHrVGIKDHKDAMRSfpyeLTEGECQK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 402 FIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG-ALSPAVPKPT 479
Cdd:PRK15093  167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGqTVETAPSKEL 246
                         250       260
                  ....*....|....*....|.
gi 2549828669 480 ISIeevgrwmsglwPDSPFTQ 500
Cdd:PRK15093  247 VTT-----------PHHPYTQ 256
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
391-471 1.67e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 49.66  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 391 AGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDgAAIIVVSEEIDELFEISDRIAVMYRGA 470
Cdd:PRK14246  151 ASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGE 229

                  .
gi 2549828669 471 L 471
Cdd:PRK14246  230 L 230
PLN03232 PLN03232
ABC transporter C family member; Provisional
2-214 1.72e-06

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 51.13  E-value: 1.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669    2 TPRLSLRNITKRYPGITAN---DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPdegeisfdghplgVETPAQARE 78
Cdd:PLN03232   612 APAISIKNGYFSWDSKTSKptlSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-------------AETSSVVIR 678
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   79 LGIAMVHQHFALFDTlSVTENVALG-------LSTGISAAEIEREIRLLGEKYGLEVDPASVvmELSMGERQRVEILRAL 151
Cdd:PLN03232   679 GSVAYVPQVSWIFNA-TVRENILFGsdfeserYWRAIDVTALQHDLDLLPGRDLTEIGERGV--NISGGQKQRVSMARAV 755
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669  152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLdEIRELADRCVVLRAGKV 214
Cdd:PLN03232   756 YSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGMI 817
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
37-194 1.91e-06

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 50.28  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  37 GENGAGKSTLMKIIYGAARPDEGEISFD-GHPLGVETPAQarelgiamvhqhFAlFDTLSVTENVALGLST--------- 106
Cdd:PRK15064   34 GANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQDQ------------FA-FEEFTVLDTVIMGHTElwevkqerd 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 107 ------------GISAAEIE----------REIR----LLGekYGLEVDPASVVM-ELSMGERQRVEILRALMTKPKLLI 159
Cdd:PRK15064  101 riyalpemseedGMKVADLEvkfaemdgytAEARagelLLG--VGIPEEQHYGLMsEVAPGWKLRVLLAQALFSNPDILL 178
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSegvSILFISH 194
Cdd:PRK15064  179 LDEPTNNLDINTIRWLEDVLNERNS---TMIIISH 210
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
391-471 3.12e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 48.68  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 391 AGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDgAAIIVVSEEIDELFEISDRIAVMYRGA 470
Cdd:PRK14267  147 PSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGK 225

                  .
gi 2549828669 471 L 471
Cdd:PRK14267  226 L 226
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
267-469 3.12e-06

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 48.77  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 267 GIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGE---------Y------------LCEADRVLLFNSPVGELDTHARr 325
Cdd:PRK11701   21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARlapdagevhYrmrdgqlrdlyaLSEAERRRLLRTEWGFVHQHPR- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 326 iSGLRyvpeqrlghaavPELSLTANTyltGDSLVRSGFILRDRARSFANLVIERFHVKTPNAEKAAGSLSGGNLQKFIMG 405
Cdd:PRK11701  100 -DGLR------------MQVSAGGNI---GERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIA 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 406 REILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK11701  164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
264-500 3.43e-06

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 49.85  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 264 RVCGIDNVSLAVRAGEIVGIAGISGNGQA-------RFMAAASGEYLCEADRVLLFNSPVGEL----DTHARRISG--LR 330
Cdd:PRK10261   28 KIAAVRNLSFSLQRGETLAIVGESGSGKSvtalalmRLLEQAGGLVQCDKMLLRRRSRQVIELseqsAAQMRHVRGadMA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 331 YVPEQrlghaavPELSLTAnTYLTGDSLVRS-----GFIlRDRARSFANLVIERfhVKTPNAEKAAG----SLSGGNLQK 401
Cdd:PRK10261  108 MIFQE-------PMTSLNP-VFTVGEQIAESirlhqGAS-REEAMVEAKRMLDQ--VRIPEAQTILSryphQLSGGMRQR 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 402 FIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNsLIRL--RDDGAAIIVVSEEIDELFEISDRIAVMYRGAlspAVpkPT 479
Cdd:PRK10261  177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQ-LIKVlqKEMSMGVIFITHDMGVVAEIADRVLVMYQGE---AV--ET 250
                         250       260
                  ....*....|....*....|.
gi 2549828669 480 ISIEEVGRwmsglWPDSPFTQ 500
Cdd:PRK10261  251 GSVEQIFH-----APQHPYTR 266
uvrA PRK00349
excinuclease ABC subunit UvrA;
137-217 3.77e-06

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 49.69  E-value: 3.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 137 LSMGERQRVEILRALMTKPK---LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRElADRCVVL---- 209
Cdd:PRK00349  831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKT-ADWIIDLgpeg 909
                          90
                  ....*....|
gi 2549828669 210 --RAGKVVAS 217
Cdd:PRK00349  910 gdGGGEIVAT 919
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
268-471 5.57e-06

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


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 47.71  E-value: 5.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGeylceadrvLLFNSPvGELdtharRISGlrYVP-EQRLGHAAVPELS 346
Cdd:cd03267    37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSG---------LLQPTS-GEV-----RVAG--LVPwKRRKKFLRRIGVV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 347 LTANTYLTGDSLVRSGFIL------------RDRARSFANLV-IERFhVKTPnaekaAGSLSGGNLQKFIMGREILNRPR 413
Cdd:cd03267   100 FGQKTQLWWDLPVIDSFYLlaaiydlpparfKKRLDELSELLdLEEL-LDTP-----VRQLSLGQRMRAEIAAALLHEPE 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 414 VLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03267   174 ILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
270-492 7.06e-06

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 47.57  E-value: 7.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 270 NVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGEldthARRISGLRYVPEQRLGHAAVPelSLTA 349
Cdd:PRK15056   25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNLVAYVPQSEEVDWSFP--VLVE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 350 NTYLTGdSLVRSGFILRDRA--RSFANLVIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVG 427
Cdd:PRK15056   99 DVVMMG-RYGHMGWLRRAKKrdRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 428 AAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDrIAVMYRGALSPAVP-KPTISIEEVGRWMSGL 492
Cdd:PRK15056  177 TEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPtETTFTAENLELAFSGV 241
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
390-471 8.14e-06

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 47.46  E-value: 8.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 390 AAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDgAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK14239  145 SALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDG 223

                  ..
gi 2549828669 470 AL 471
Cdd:PRK14239  224 DL 225
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
23-214 8.26e-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: 48.79  E-value: 8.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGhplgvetpaqarelGIAMVHQHfALFDTLSVTENVAL 102
Cdd:TIGR00957  657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------------SVAYVPQQ-AWIQNDSLRENILF 721
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  103 G-------LSTGISAAEIEREIRLLGEKYGLEVDPASVvmELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKL 175
Cdd:TIGR00957  722 GkalnekyYQQVLEACALLPDLEILPSGDRTEIGEKGV--NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2549828669  176 FKtlHQLSSEGV----SILFISHKLDEIRELaDRCVVLRAGKV 214
Cdd:TIGR00957  800 FE--HVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKI 839
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
29-465 1.00e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 48.27  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  29 PGEVLAILGENGAGKSTLMKIIYGAARPDEGEisfdghplgVETPAQARElgiamVHQHFA---LFDTLSvtenvalGLS 105
Cdd:PRK13409   98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGD---------YEEEPSWDE-----VLKRFRgteLQNYFK-------KLY 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 106 TG-ISAA------------------EI-----EREIRL-LGEKYGLE--VDPAsvVMELSMGERQRVEILRALMTKPKLL 158
Cdd:PRK13409  157 NGeIKVVhkpqyvdlipkvfkgkvrELlkkvdERGKLDeVVERLGLEniLDRD--ISELSGGELQRVAIAAALLRDADFY 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 159 ILDEPTSVL-------TPQAVRKLfktlhqlsSEGVSILFISHKLDEIRELADRCVVLRaGK-----VVAsvDPKAE--- 223
Cdd:PRK13409  235 FFDEPTSYLdirqrlnVARLIREL--------AEGKYVLVVEHDLAVLDYLADNVHIAY-GEpgaygVVS--KPKGVrvg 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 224 ---------SEENLaRlmIGNDPPTVREGTAKagEVVFEMRHVSAPGSTRvcGIDNVSLAV-----RAGEIVGIAGISGN 289
Cdd:PRK13409  304 ineylkgylPEENM-R--IRPEPIEFEERPPR--DESERETLVEYPDLTK--KLGDFSLEVeggeiYEGEVIGIVGPNGI 376
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 290 GQARFMAAASGEYlcEADRvllfnspvGELDThARRISglrYVPEqrlghaavpelsltantYLTGDSLVRSGFILRDRA 369
Cdd:PRK13409  377 GKTTFAKLLAGVL--KPDE--------GEVDP-ELKIS---YKPQ-----------------YIKPDYDGTVEDLLRSIT 425
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 370 RSFA-----NLVIERFHVKtPNAEKAAGSLSGGNLQKFI----MGRE----ILNRPRVLL-VHQptwgvDVGAAAVIRNs 435
Cdd:PRK13409  426 DDLGssyykSEIIKPLQLE-RLLDKNVKDLSGGELQRVAiaacLSRDadlyLLDEPSAHLdVEQ-----RLAVAKAIRR- 498
                         490       500       510
                  ....*....|....*....|....*....|
gi 2549828669 436 LIRLRDdgAAIIVVSEEIDELFEISDRIAV 465
Cdd:PRK13409  499 IAEERE--ATALVVDHDIYMIDYISDRLMV 526
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
252-469 1.16e-05

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: 47.91  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 252 FEMRHVS---APGSTRVcgIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRiSG 328
Cdd:COG2274   474 IELENVSfryPGDSPPV--LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLR-RQ 550
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 329 LRYVPeQrlghaavpelsltaNTYLTGDSlVRSGFILRDRARSFANLV-------IERFHVKTPN------AEKAAGsLS 395
Cdd:COG2274   551 IGVVL-Q--------------DVFLFSGT-IRENITLGDPDATDEEIIeaarlagLHDFIEALPMgydtvvGEGGSN-LS 613
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 396 GGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRdDGAAIIVVSEEiDELFEISDRIAVMYRG 469
Cdd:COG2274   614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHR-LSTIRLADRIIVLDKG 685
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
29-205 1.26e-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: 45.06  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   29 PGEVLAILGENGAGKSTLMKIIYGAARPDEGEIsfdghplgvetpaqarelgiamvhqhfalfdtlsvtenVALGLSTGI 108
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------------IYIDGEDIL 42
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  109 SAAEIEREIRLLGEKYGLEVDpasvvmelsmGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLH------QL 182
Cdd:smart00382  43 EEVLDQLLLIIVGGKKASGSG----------ELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllllLK 112
                          170       180
                   ....*....|....*....|...
gi 2549828669  183 SSEGVSILFISHKLDEIRELADR 205
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPALLR 135
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
24-205 1.65e-05

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 45.04  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  24 SLDIAPGEVLAILGENGAGKSTLMK-IIYGaarpdegeisfdghplgvetpaqareLGIAMVHQHFALFdtlsvtenval 102
Cdd:cd03227    15 DVTFGEGSLTIITGPNGSGKSTILDaIGLA--------------------------LGGAQSATRRRSG----------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 103 GLSTGISAAEiereirllgekyglEVDPASVVMELSMGERQRVE---ILRALMTKPK-LLILDEPTSVLTPQAVRKLFKT 178
Cdd:cd03227    58 VKAGCIVAAV--------------SAELIFTRLQLSGGEKELSAlalILALASLKPRpLYILDEIDRGLDPRDGQALAEA 123
                         170       180
                  ....*....|....*....|....*..
gi 2549828669 179 LHQLSSEGVSILFISHKLdEIRELADR 205
Cdd:cd03227   124 ILEHLVKGAQVIVITHLP-ELAELADK 149
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
23-217 1.72e-05

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 46.10  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTL-MKIIYGaarpdEGEISFdghplgVET-PAQARELGIAMVHQHFALFDTLSVTENV 100
Cdd:cd03270    14 VDVDIPRNKLVVITGVSGSGKSSLaFDTIYA-----EGQRRY------VESlSAYARQFLGQMDKPDVDSIEGLSPAIAI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 ALGL------STGISAAEIEREIRLLGEKYGLE-------------VDPASVVMELSMGERQRVEILRALMTKPK--LLI 159
Cdd:cd03270    83 DQKTtsrnprSTVGTVTEIYDYLRLLFARVGIRerlgflvdvglgyLTLSRSAPTLSGGEAQRIRLATQIGSGLTgvLYV 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIReLADRCVVL------RAGKVVAS 217
Cdd:cd03270   163 LDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIR-AADHVIDIgpgagvHGGEIVAQ 225
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
137-221 2.06e-05

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 47.52  E-value: 2.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  137 LSMGERQRVEI---LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLdEIRELADRCVVL---- 209
Cdd:PRK00635   810 LSGGEIQRLKLayeLLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVADYVLELgpeg 888
                           90
                   ....*....|....
gi 2549828669  210 --RAGKVVASVDPK 221
Cdd:PRK00635   889 gnLGGYLLASCSPE 902
PTZ00243 PTZ00243
ABC transporter; Provisional
23-249 2.14e-05

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 47.47  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEI----SFdghplgVETPAQARELGiAMVHQHFALFDtlsvtE 98
Cdd:PTZ00243   679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaerSI------AYVPQQAWIMN-ATVRGNILFFD-----E 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   99 NVALGLSTGISAAEIEREIRLLGEkyGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQA----VRK 174
Cdd:PTZ00243   747 EDAARLADAVRVSQLEADLAQLGG--GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgervVEE 824
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669  175 LFktLHQLSseGVSILFISHKLdEIRELADRCVVLRAGKVVASVDPKAESEENLARLMIGN--DPPTVREGTAKAGE 249
Cdd:PTZ00243   825 CF--LGALA--GKTRVLATHQV-HVVPRADYVVALGDGRVEFSGSSADFMRTSLYATLAAElkENKDSKEGDADAEV 896
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
88-290 2.28e-05

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 47.32  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  88 FALFDTLSVTENVALglstgiSAAEIEREIRllgEKYGLEVD-------PASVVMELSMGERQRVEILRALMTKPK--LL 158
Cdd:TIGR00630 442 HEFFNQLTLTPEEKK------IAEEVLKEIR---ERLGFLIDvgldylsLSRAAGTLSGGEAQRIRLATQIGSGLTgvLY 512
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRElADRCVVL--RAGK----VVASVDPKAeseenlarLM 232
Cdd:TIGR00630 513 VLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRA-ADYVIDIgpGAGEhggeVVASGTPEE--------IL 583
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 233 IGNDPPTvreGTAKAGEV---VFEMRHVSAPGSTRVCG-----IDNVSLAVRAGEIVGIAGISGNG 290
Cdd:TIGR00630 584 ANPDSLT---GQYLSGRKkieVPAERRPGNGKFLTLKGarennLKNITVSIPLGLFTCITGVSGSG 646
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
394-495 3.60e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 45.47  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 394 LSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRnSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALSP 473
Cdd:PRK14271  164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE-EFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVE 242
                          90       100
                  ....*....|....*....|....*.
gi 2549828669 474 AVPKPTI----SIEEVGRWMSGLWPD 495
Cdd:PRK14271  243 EGPTEQLfsspKHAETARYVAGLSGD 268
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
264-469 4.40e-05

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 45.67  E-value: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 264 RVCGIDNVSLAVRAGEIVGIAGISGNGQARF----MAAASGEYLCEADRvLLFNSpvgeldtharrISGLRYVPEQR--- 336
Cdd:COG4170    19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIakaiCGITKDNWHVTADR-FRWNG-----------IDLLKLSPRERrki 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 337 LGHaavpELSLT---ANTYL-----TGDSLVRS-------GFILRdRARSFANLVIERFH-VKTPNAEKAAGS----LSG 396
Cdd:COG4170    87 IGR----EIAMIfqePSSCLdpsakIGDQLIEAipswtfkGKWWQ-RFKWRKKRAIELLHrVGIKDHKDIMNSypheLTE 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 397 GNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:COG4170   162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYCG 235
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
394-469 5.14e-05

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 45.32  E-value: 5.14e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 394 LSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK09452  145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
271-476 8.50e-05

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 44.19  E-value: 8.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 271 VSLAVRAGEIVGIAGISGNGQARFM-------AAASGEYLCEADRVLLFNSPVGEL---DTHARRISGLR----YVPEQR 336
Cdd:PRK10619   24 VSLQANAGDVISIIGSSGSGKSTFLrcinfleKPSEGSIVVNGQTINLVRDKDGQLkvaDKNQLRLLRTRltmvFQHFNL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 337 LGHAAVPELSLTANTYLTGDSLVRSgfilRDRARSFANLV--IERFHVKTPNaekaagSLSGGNLQKFIMGREILNRPRV 414
Cdd:PRK10619  104 WSHMTVLENVMEAPIQVLGLSKQEA----RERAVKYLAKVgiDERAQGKYPV------HLSGGQQQRVSIARALAMEPEV 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 415 LLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALSPAVP 476
Cdd:PRK10619  174 LLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
cbiO PRK13645
energy-coupling factor transporter ATPase;
267-469 9.28e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 44.23  E-value: 9.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 267 GIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLL--FNSPVG-----ELDTHARRISGLRYVPEQRLGH 339
Cdd:PRK13645   26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdYAIPANlkkikEVKRLRKEIGLVFQFPEYQLFQ 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 340 AAVPELSLTANTYLTGDslvrsgfilRDRARSFANLVIERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQ 419
Cdd:PRK13645  106 ETIEKDIAFGPVNLGEN---------KQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 420 PTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK13645  177 PTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEG 227
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
268-325 1.13e-04

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 43.99  E-value: 1.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTH--ARR 325
Cdd:PRK13548   18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelARR 77
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
271-469 1.15e-04

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 43.85  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 271 VSLAVRAGEIVGIAGISGNGQARFMAAASGeyLCEAD-----RVLLFNSPVGELDTHARRISGLR----YVPEQrlgHAA 341
Cdd:PRK09984   23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSG--LITGDksagsHIELLGRTVQREGRLARDIRKSRantgYIFQQ---FNL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 342 VPELSLTANTY---LTGDSLVRSGF-----ILRDRA-RSFANLVIERFhvktpnAEKAAGSLSGGNLQKFIMGREILNRP 412
Cdd:PRK09984   98 VNRLSVLENVLigaLGSTPFWRTCFswftrEQKQRAlQALTRVGMVHF------AHQRVSTLSGGQQQRVAIARALMQQA 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 413 RVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK09984  172 KVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQG 229
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
394-469 1.27e-04

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 43.84  E-value: 1.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 394 LSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK13638  137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQG 212
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
268-484 1.42e-04

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 44.05  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRisglryvpeqRLGhaAVPELSL 347
Cdd:PRK13536   57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARA----------RIG--VVPQFDN 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 TANTYLTGDSLVRSGFILRDRARSFANLV--IERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVD 425
Cdd:PRK13536  125 LDLEFTVRENLLVFGRYFGMSTREIEAVIpsLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 426 VGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGAlSPAVPKPTISIEE 484
Cdd:PRK13536  205 PHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR-KIAEGRPHALIDE 262
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
267-469 1.55e-04

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 44.25  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 267 GIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGLRYVPEQRLGHAAVPELS 346
Cdd:PRK10070   43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMT 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 347 LTANTYLTGDSLVRSGFILRDRA-RSFANLVIERFHVKTPNaekaagSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVD 425
Cdd:PRK10070  123 VLDNTAFGMELAGINAEERREKAlDALRQVGLENYAHSYPD------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2549828669 426 VGAAAVIRNSLIRLR-DDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK10070  197 PLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
15-195 1.60e-04

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: 44.35  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  15 PGITANDHV-----SLDIAPGEVLAILGENGAGKSTLMKI------IYGAAR--PDEGEISF-------------DG--H 66
Cdd:TIGR00954 458 PLVTPNGDVlieslSFEVPSGNNLLICGPNGCGKSSLFRIlgelwpVYGGRLtkPAKGKLFYvpqrpymtlgtlrDQiiY 537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  67 PLGVETpaqarelgiaMVHQHFALFDTLSVTENVALGlstgisaaeiereiRLLGEKYGLEVdPASVVMELSMGERQRVE 146
Cdd:TIGR00954 538 PDSSED----------MKRRGLSDKDLEQILDNVQLT--------------HILEREGGWSA-VQDWMDVLSGGEKQRIA 592
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2549828669 147 ILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLsseGVSILFISHK 195
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF---GITLFSVSHR 638
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
370-467 2.05e-04

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


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 43.12  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 370 RSFANLVIERFHVKtPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVG----AAAVIRnsliRLRDDGAA 445
Cdd:cd03236   117 RGKLDELVDQLELR-HVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlnAARLIR----ELAEDDNY 191
                          90       100
                  ....*....|....*....|..
gi 2549828669 446 IIVVSEEIDELFEISDRIAVMY 467
Cdd:cd03236   192 VLVVEHDLAVLDYLSDYIHCLY 213
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
394-469 2.24e-04

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 43.19  E-value: 2.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 394 LSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK11022  154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAG 230
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
253-471 2.27e-04

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: 42.57  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 253 EMRHVS---APGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELD----THARR 325
Cdd:cd03258     3 ELKNVSkvfGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelRKARR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 326 ISGL----------RYVpeqrLGHAAVP-ELSLTANTYLtgdslvrsgfilRDRARSFANLV-IERFHVKTPnaekaaGS 393
Cdd:cd03258    83 RIGMifqhfnllssRTV----FENVALPlEIAGVPKAEI------------EERVLELLELVgLEDKADAYP------AQ 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 394 LSGGNLQKFIMGREILNRPRVLLVHQPTWGVDvgaAAVIRNSLIRLRDD----GAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03258   141 LSGGQKQRVGIARALANNPKVLLCDEATSALD---PETTQSILALLRDInrelGLTIVLITHEMEVVKRICDRVAVMEKG 217

                  ..
gi 2549828669 470 AL 471
Cdd:cd03258   218 EV 219
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
368-465 2.76e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 43.86  E-value: 2.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  368 RARSFAnlVIERFHVKTPNAEKA-----AGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD 442
Cdd:PTZ00265  1330 RACKFA--AIDEFIESLPNKYDTnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK 1407
                           90       100
                   ....*....|....*....|....
gi 2549828669  443 G-AAIIVVSEEIDELfEISDRIAV 465
Cdd:PTZ00265  1408 AdKTIITIAHRIASI-KRSDKIVV 1430
cbiO PRK13637
energy-coupling factor transporter ATPase;
387-469 2.85e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 42.73  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 387 AEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAV 465
Cdd:PRK13637  138 KDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIV 217

                  ....
gi 2549828669 466 MYRG 469
Cdd:PRK13637  218 MNKG 221
cbiO PRK13643
energy-coupling factor transporter ATPase;
258-469 3.01e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 42.80  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 258 SAPGSTRvcGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGeYLCEADRVLLFNSPVGELDTHARRISGLRyvpeQRL 337
Cdd:PRK13643   14 NSPFASR--ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNG-LLQPTEGKVTVGDIVVSSTSKQKEIKPVR----KKV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 338 GHA-AVPELSLTANTYLTGDSLVRSGF-ILRDRARSFANLVIERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVL 415
Cdd:PRK13643   87 GVVfQFPESQLFEETVLKDVAFGPQNFgIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVL 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 416 LVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK13643  167 VLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
130-207 5.33e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 42.89  E-value: 5.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  130 PASVVMELSMGERQRVEILRALMTKPK--LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKlDEIRELADRCV 207
Cdd:PRK00635   470 PERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRII 548
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
111-194 6.74e-04

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 41.61  E-value: 6.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 111 AEIEREIRLLGEKYGLEVDPAsvvmELSMGERQ---RVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGV 187
Cdd:pfam13304 215 RLRERGLILLENGGGGELPAF----ELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGA 290

                  ....*..
gi 2549828669 188 SILFISH 194
Cdd:pfam13304 291 QLILTTH 297
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
395-483 7.79e-04

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 41.62  E-value: 7.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 395 SGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG---- 469
Cdd:PRK15079  163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGhave 242
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2549828669 470 -----------------ALSPAVPKPTISIE 483
Cdd:PRK15079  243 lgtydevyhnplhpytkALMSAVPIPDPDLE 273
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
23-194 7.84e-04

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 40.63  E-value: 7.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEI---------------SFDGHPLGVETpaqarelgiamvhqH 87
Cdd:PRK13541   19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyykncninniakpycTYIGHNLGLKL--------------E 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  88 FALFDTLSVTENVALGLSTGISAAEIEREIRLLGEKyglevdpasvVMELSMGERQRVEILRALMTKPKLLILDEPTSVL 167
Cdd:PRK13541   85 MTVFENLKFWSEIYNSAETLYAAIHYFKLHDLLDEK----------CYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL 154
                         170       180
                  ....*....|....*....|....*...
gi 2549828669 168 TPQAvRKLFKTLHQL-SSEGVSILFISH 194
Cdd:PRK13541  155 SKEN-RDLLNNLIVMkANSGGIVLLSSH 181
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
387-487 8.05e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 41.22  E-value: 8.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 387 AEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVM 466
Cdd:PRK13639  131 ENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVM 210
                          90       100
                  ....*....|....*....|..
gi 2549828669 467 YRGA-LSPAVPKPTISIEEVGR 487
Cdd:PRK13639  211 SDGKiIKEGTPKEVFSDIETIR 232
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
4-62 1.24e-03

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 40.75  E-value: 1.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669   4 RLSLRNItKRYpgitANDHVSLDIAPGeVLAILGENGAGKSTLMKIIYGAARPDEGEIS 62
Cdd:COG3950     5 SLTIENF-RGF----EDLEIDFDNPPR-LTVLVGENGSGKTTLLEAIALALSGLLSRLD 57
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
391-471 1.25e-03

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 41.92  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  391 AGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRdDGAAIIVVSEEIDELFEISDRIAVMYRGA 470
Cdd:TIGR01257 1059 AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGR 1137

                   .
gi 2549828669  471 L 471
Cdd:TIGR01257 1138 L 1138
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
236-333 2.88e-03

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 40.15  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 236 DPPTVREGTAKAGEVVFEmrHVSA--PGSTRVcgIDNVSLAVRAGEIVGIAGISGNGQ-------ARFMAAASGeylcea 306
Cdd:COG1132   326 DPPGAVPLPPVRGEIEFE--NVSFsyPGDRPV--LKDISLTIPPGETVALVGPSGSGKstlvnllLRFYDPTSG------ 395
                          90       100
                  ....*....|....*....|....*....
gi 2549828669 307 dRVLLFNSPVGELDTHA--RRISglrYVP 333
Cdd:COG1132   396 -RILIDGVDIRDLTLESlrRQIG---VVP 420
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
366-469 4.14e-03

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 38.84  E-value: 4.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 366 RDRARSFANLVIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAA 445
Cdd:PRK11124  115 KDQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGIT 193
                          90       100
                  ....*....|....*....|....
gi 2549828669 446 IIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK11124  194 QVIVTHEVEVARKTASRVVYMENG 217
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
394-469 5.63e-03

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: 38.24  E-value: 5.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 394 LSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNsLIRLRDDGAAIIVVSEEIDELFEiSDRIAVMYRG 469
Cdd:cd03244   140 LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQK-TIREAFKDCTVLTIAHRLDTIID-SDRILVLDKG 213
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
235-290 7.70e-03

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 38.79  E-value: 7.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 235 NDPPTVREGTAKAGEVVFEMRHVSAPGSTRvcGIDNVSLAVRAGEIVGIAGISGNG 290
Cdd:PRK13657  320 RDPPGAIDLGRVKGAVEFDDVSFSYDNSRQ--GVEDVSFEAKPGQTVAIVGPTGAG 373
AAA_29 pfam13555
P-loop containing region of AAA domain;
18-47 8.20e-03

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 34.88  E-value: 8.20e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2549828669  18 TANDHVsLDIAPGEVLAILGENGAGKSTLM 47
Cdd:pfam13555  11 TFDGHT-IPIDPRGNTLLTGPSGSGKSTLL 39
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
387-469 8.75e-03

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: 37.89  E-value: 8.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 387 AEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVM 466
Cdd:cd03262   129 ADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFM 208

                  ...
gi 2549828669 467 YRG 469
Cdd:cd03262   209 DDG 211
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
249-454 9.05e-03

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 38.23  E-value: 9.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 249 EVVFEMRHVS--APGSTRvcgIDNVSLAVRAGEIVGIAGISGNGQA-------RFMAAASGEylceadrVLLFNSPVGEL 319
Cdd:PRK10575    9 DTTFALRNVSfrVPGRTL---LHPLSLTFPAGKVTGLIGHNGSGKStllkmlgRHQPPSEGE-------ILLDAQPLESW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 320 DTH--ARRISglrYVPEQrLGHA---AVPELsLTANTYLTGDSLVRSGFILRDRARSFANLVierfhVKTPNAEKAAGSL 394
Cdd:PRK10575   79 SSKafARKVA---YLPQQ-LPAAegmTVREL-VAIGRYPWHGALGRFGAADREKVEEAISLV-----GLKPLAHRLVDSL 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 395 SGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEID 454
Cdd:PRK10575  149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDIN 209
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
394-469 9.28e-03

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 38.53  E-value: 9.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 394 LSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK15134  157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNG 233
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
4-204 9.59e-03

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 37.59  E-value: 9.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669   4 RLSLRNITKRYpgitanDHVSLDIAPGeVLAILGENGAGKSTLMKII----YGAARPDEGEISFDGHPLGV-ETPAQare 78
Cdd:cd03240     3 KLSIRNIRSFH------ERSEIEFFSP-LTLIVGQNGAGKTTIIEALkyalTGELPPNSKGGAHDPKLIREgEVRAQ--- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669  79 lgiamVHQHFALFD--------TLSVTENVALgLSTGISAAEIEREIRLlgekyglevdpasvvmeLSMGERQ------R 144
Cdd:cd03240    73 -----VKLAFENANgkkytitrSLAILENVIF-CHQGESNWPLLDMRGR-----------------CSGGEKVlasliiR 129
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 145 VEILRALMTKPKLLILDEPTSVLTPQAVR-KLFKTLHQLSSEGVS-ILFISHKlDEIRELAD 204
Cdd:cd03240   130 LALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQKNFqLIVITHD-EELVDAAD 190
 
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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