NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490656625|ref|WP_004521615|]
View 

sugar ABC transporter ATP-binding protein [Burkholderia pseudomallei]

Protein Classification

sugar ABC transporter ATP-binding protein( domain architecture ID 11438367)

sugar ABC transporter ATP-binding protein is the ATPase component of an ATP-binding cassette (ABC) transporter which facilitates the transport of one or more from of a variety of sugar substrates such as ribose, galactose, methyl galactoside, fructose, and arabinose

CATH:  3.40.50.300
EC:  7.5.2.-
PubMed:  24638992|25750732
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
11-509 0e+00

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


:

Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 686.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  11 DTPTLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG 89
Cdd:COG1129    1 AEPLLEMRGISKSFgGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  90 VRMVMQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDsLDPDTLVGSLGIGHQQMVEIARSLAGDC 169
Cdd:COG1129   81 IAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 170 RVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGR 249
Cdd:COG1129  160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 250 EIAEQAVHGTRTPGAPRLRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAA 329
Cdd:COG1129  240 ELEDLFPKRAAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG--KPVR 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 330 IRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRARGPAQPVAELSG 409
Cdd:COG1129  318 IRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSG 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 410 GNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAVFE 489
Cdd:COG1129  398 GNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELD 477
                        490       500
                 ....*....|....*....|
gi 490656625 490 RGGWTQDALLGAAFAGYARR 509
Cdd:COG1129  478 REEATEEAIMAAATGGAAAA 497
 
Name Accession Description Interval E-value
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
11-509 0e+00

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 686.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  11 DTPTLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG 89
Cdd:COG1129    1 AEPLLEMRGISKSFgGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  90 VRMVMQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDsLDPDTLVGSLGIGHQQMVEIARSLAGDC 169
Cdd:COG1129   81 IAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 170 RVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGR 249
Cdd:COG1129  160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 250 EIAEQAVHGTRTPGAPRLRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAA 329
Cdd:COG1129  240 ELEDLFPKRAAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG--KPVR 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 330 IRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRARGPAQPVAELSG 409
Cdd:COG1129  318 IRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSG 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 410 GNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAVFE 489
Cdd:COG1129  398 GNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELD 477
                        490       500
                 ....*....|....*....|
gi 490656625 490 RGGWTQDALLGAAFAGYARR 509
Cdd:COG1129  478 REEATEEAIMAAATGGAAAA 497
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
11-502 1.01e-169

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 489.04  E-value: 1.01e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  11 DTPTLVVTGIGKTYaeP---VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEA 87
Cdd:PRK11288   1 SSPYLSFDGIGKTF--PgvkALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  88 LGVRMVMQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDsLDPDTLVGSLGIGHQQMVEIARSLAG 167
Cdd:PRK11288  79 AGVAIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVD-IDPDTPLKYLSIGQRQMVEIAKALAR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV-HVDRIDAQPTERLVALM 246
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVaTFDDMAQVDRDQLVQAM 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 247 AGREIAEQAVHGTRTPGAPRLRVERLSrGDAVR-DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpp 325
Cdd:PRK11288 238 VGREIGDIYGYRPRPLGEVRLRLDGLK-GPGLRePISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG-- 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 326 RPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGG-VVDGERENALAARQIDALRIRARGPAQPV 404
Cdd:PRK11288 315 KPIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGcLINNRWEAENADRFIRSLNIKTPSREQLI 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 405 AELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
                        490
                 ....*....|....*...
gi 490656625 485 HAVFERGGWTQDALLGAA 502
Cdd:PRK11288 475 AGELAREQATERQALSLA 492
GguA NF040905
sugar ABC transporter ATP-binding protein;
19-499 1.47e-143

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 422.28  E-value: 1.47e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  19 GIGKTYAePV--LDDVSLALYPGEALALTGENGAGKSTLSKIVAGlVAPT---TGAMRLAGAEYAPHSRAHAEALGVRMV 93
Cdd:NF040905   6 GITKTFP-GVkaLDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVCRFKDIRDSEALGIVII 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 MQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDSlDPDTLVGSLGIGHQQMVEIARSLAGDCRVLI 173
Cdd:NF040905  84 HQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDE-SPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 174 LDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV-HVDRIDAQPTE-RLVALMAGREI 251
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIeTLDCRADEVTEdRIIRGMVGRDL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 252 AEQAVHGTRTPGAPRLRVERLSRGD-------AVRDVSFDVRAGEIFGISGLIGAGRTELLRLV----YGADAAdgGTVS 320
Cdd:NF040905 243 EDRYPERTPKIGEVVFEVKNWTVYHplhperkVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsYGRNIS--GTVF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 321 IGDppRPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRARGP 400
Cdd:NF040905 321 KDG--KEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMNIKTPSV 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 401 AQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMS 480
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478
                        490
                 ....*....|....*....
gi 490656625 481 AGRMHAVFERGGWTQDALL 499
Cdd:NF040905 479 EGRITGELPREEASQERIM 497
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
15-502 1.49e-123

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: 371.08  E-value: 1.49e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTT--GAMRLAGAEYAPHSRAHAEALGVR 91
Cdd:TIGR02633   2 LEMKGIVKTFGGvKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   92 MVMQELNLVPTLTVAENLFL-DRLPHRFGVIDRRRLAADARAAMARVGLDSlDPDTL-VGSLGIGHQQMVEIARSLAGDC 169
Cdd:TIGR02633  82 IIHQELTLVPELSVAENIFLgNEITLPGGRMAYNAMYLRAKNLLRELQLDA-DNVTRpVGDYGGGQQQLVEIAKALNKQA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  170 RVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGR 249
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  250 EIAEQAVHGTRTPGAPRLRVERLSRGDA-------VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGA-DAADGGTVSI 321
Cdd:TIGR02633 241 EITSLYPHEPHEIGDVILEARNLTCWDVinphrkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  322 GDppRPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRARGPA 401
Cdd:TIGR02633 321 NG--KPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPF 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  402 QPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSA 481
Cdd:TIGR02633 399 LPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGE 478
                         490       500
                  ....*....|....*....|.
gi 490656625  482 GRMHAVFERGGWTQDALLGAA 502
Cdd:TIGR02633 479 GKLKGDFVNHALTQEQVLAAA 499
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
263-484 3.10e-79

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: 245.80  E-value: 3.10e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 263 GAPRLRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHGIA 342
Cdd:cd03215    1 GEPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG--KPVTRRSPRDAIRAGIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDRKGEGLLLPQSIAANLSLGQLarvarggvvdgerenalaarqidalrirargpaqpvaeLSGGNQQKVAIGRWLG 422
Cdd:cd03215   79 YVPEDRKREGLVLDLSVAENIALSSL--------------------------------------LSGGNQQKVVLARWLA 120
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 423 RDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03215  121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
29-179 5.58e-31

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: 117.36  E-value: 5.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAlGVRMVMQELNLVPTLTVAEN 108
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVREN 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625  109 LfldRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTL---VGSLGIGHQQMVEIARSLAGDCRVLILDEPTA 179
Cdd:pfam00005  80 L---RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
276-471 4.39e-14

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 70.73  E-value: 4.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAI--RSPADAVrhgialvsedrkgegl 353
Cdd:NF040873   6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVpqRSEVPDS---------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 lLPQSIAANLSLGQLARVARGGVVDGER----ENALAARQIDALRIRargpaqPVAELSGGNQQKVAIGRWLGRDMGVLL 429
Cdd:NF040873  70 -LPLTVRDLVAMGRWARRGLWRRLTRDDraavDDALERVGLADLAGR------QLGELSGGQRQRALLAQGLAQEADLLL 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 490656625 430 FDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELML 471
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR 184
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
21-302 4.56e-11

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 65.53  E-value: 4.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  21 GKTYAepvLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphSRAHAEALGVRMV-M-QEL- 97
Cdd:NF033858  12 GKTVA---LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAVCPRIAyMpQGLg 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  98 -NLVPTLTVAENL-FLDRLphrFGvIDRRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILD 175
Cdd:NF033858  87 kNLYPTLSVFENLdFFGRL---FG-QDAAERRRRIDELLRATGLAPF-ADRPAGKLSGGMKQKLGLCCALIHDPDLLILD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 176 EPTamlTAreVELL-----FDQIARLKADG------VALVYIshrlEELARVAQRVAvLRDGRLvhvdrIDAQPTERL-- 242
Cdd:NF033858 162 EPT---TG--VDPLsrrqfWELIDRIRAERpgmsvlVATAYM----EEAERFDWLVA-MDAGRV-----LATGTPAELla 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 243 -----------VALM-AGREIAEQAVH----GTRTPGAPRLRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRT 302
Cdd:NF033858 227 rtgadtleaafIALLpEEKRRGHQPVVipprPADDDDEPAIEARGLTMrfGDftAVDHVSFRIRRGEIFGFLGSNGCGKS 306
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
154-258 1.97e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 46.65  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 154 GHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDR 233
Cdd:NF000106 148 GMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
                         90       100
                 ....*....|....*....|....*
gi 490656625 234 IDAQPTErlvalMAGREIAEQAVHG 258
Cdd:NF000106 228 VDELKTK-----VGGRTLQIRPAHA 247
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
30-178 4.14e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 46.27  E-value: 4.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  30 DDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAhaealgVRM---VM-QELNLVPTLTV 105
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIA------TRRrvgYMsQAFSLYGELTV 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLFLD-RLPH---------------RFGVIDRrrlaadaraamarvgLDSLdPDTLvgSLGIgHQQMveiarSLAGDC 169
Cdd:NF033858 357 RQNLELHaRLFHlpaaeiaarvaemleRFDLADV---------------ADAL-PDSL--PLGI-RQRL-----SLAVAV 412
                        170
                 ....*....|...
gi 490656625 170 ----RVLILDEPT 178
Cdd:NF033858 413 ihkpELLILDEPT 425
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
257-486 4.92e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 45.50  E-value: 4.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 257 HGTRTPGAPRLRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAG--RTELLRLVYGADAADggtvsigDPPRPAAIRSPA 334
Cdd:NF000106   8 NGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGR-------RPWRF*TWCANR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 335 DAVRHGIALVSEDRKGEglllPQSIAANLSLGQLARVarggvVDGERENALAarQIDALRIR---ARGPAQPVAELSGGN 411
Cdd:NF000106  81 RALRRTIG*HRPVR*GR----RESFSGRENLYMIGR*-----LDLSRKDARA--RADELLERfslTEAAGRAAAKYSGGM 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 412 QQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:NF000106 150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
38-235 8.40e-03

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: 36.97  E-value: 8.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625    38 PGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEyaphsrahaealgvrmvmqelnlvptltvaenlfldrlphr 117
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   118 fgvidrrrlaadarAAMARVGLDSLDPDTLVGSLGIGHQQMVEIARSLA--GDCRVLILDEPTAMLTAREVELLFDQIA- 194
Cdd:smart00382  40 --------------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALArkLKPDVLILDEITSLLDAEQEALLLLLEEl 105
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 490656625   195 -----RLKADGVALVYISHRLEELARvaqRVAVLRDGRLVHVDRID 235
Cdd:smart00382 106 rllllLKSEKNLTVILTTNDEKDLGP---ALLRRRFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
11-509 0e+00

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 686.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  11 DTPTLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG 89
Cdd:COG1129    1 AEPLLEMRGISKSFgGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  90 VRMVMQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDsLDPDTLVGSLGIGHQQMVEIARSLAGDC 169
Cdd:COG1129   81 IAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 170 RVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGR 249
Cdd:COG1129  160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 250 EIAEQAVHGTRTPGAPRLRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAA 329
Cdd:COG1129  240 ELEDLFPKRAAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG--KPVR 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 330 IRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRARGPAQPVAELSG 409
Cdd:COG1129  318 IRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSG 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 410 GNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAVFE 489
Cdd:COG1129  398 GNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELD 477
                        490       500
                 ....*....|....*....|
gi 490656625 490 RGGWTQDALLGAAFAGYARR 509
Cdd:COG1129  478 REEATEEAIMAAATGGAAAA 497
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
11-502 1.01e-169

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 489.04  E-value: 1.01e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  11 DTPTLVVTGIGKTYaeP---VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEA 87
Cdd:PRK11288   1 SSPYLSFDGIGKTF--PgvkALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  88 LGVRMVMQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDsLDPDTLVGSLGIGHQQMVEIARSLAG 167
Cdd:PRK11288  79 AGVAIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVD-IDPDTPLKYLSIGQRQMVEIAKALAR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV-HVDRIDAQPTERLVALM 246
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVaTFDDMAQVDRDQLVQAM 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 247 AGREIAEQAVHGTRTPGAPRLRVERLSrGDAVR-DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpp 325
Cdd:PRK11288 238 VGREIGDIYGYRPRPLGEVRLRLDGLK-GPGLRePISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG-- 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 326 RPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGG-VVDGERENALAARQIDALRIRARGPAQPV 404
Cdd:PRK11288 315 KPIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGcLINNRWEAENADRFIRSLNIKTPSREQLI 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 405 AELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
                        490
                 ....*....|....*...
gi 490656625 485 HAVFERGGWTQDALLGAA 502
Cdd:PRK11288 475 AGELAREQATERQALSLA 492
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
13-502 2.53e-157

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 457.85  E-value: 2.53e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  13 PTLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGlVAPT---TGAMRLAGAEYAPHSRAHAEAL 88
Cdd:PRK13549   4 YLLEMKNITKTFgGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQASNIRDTERA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  89 GVRMVMQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDsLDPDTLVGSLGIGHQQMVEIARSLAGD 168
Cdd:PRK13549  83 GIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLD-INPATPVGNLGLGQQQLVEIAKALNKQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 169 CRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAG 248
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 249 REIAEQAVHGTRTPGAPRLRVERLSRGDA-------VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGA-DAADGGTVS 320
Cdd:PRK13549 242 RELTALYPREPHTIGEVILEVRNLTAWDPvnphikrVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIF 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 321 IGDppRPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRARGP 400
Cdd:PRK13549 322 IDG--KPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASP 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 401 AQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMS 480
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMH 479
                        490       500
                 ....*....|....*....|..
gi 490656625 481 AGRMHAVFERGGWTQDALLGAA 502
Cdd:PRK13549 480 EGKLKGDLINHNLTQEQVMEAA 501
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
12-505 2.64e-157

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 457.57  E-value: 2.64e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  12 TPTLVVTGIGKTYAEPV-LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGV 90
Cdd:COG3845    3 PPALELRGITKRFGGVVaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  91 RMVMQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDsLDPDTLVGSLGIGHQQMVEIARSLAGDCR 170
Cdd:COG3845   83 GMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLD-VDPDAKVEDLSVGEQQRVEILKALYRGAR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 171 VLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGRE 250
Cdd:COG3845  162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGRE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 251 IAEQAVHGTRTPGAPRLRVERLS-----RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpp 325
Cdd:COG3845  242 VLLRVEKAPAEPGEVVLEVENLSvrddrGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG-- 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 326 RPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQL--ARVARGGVVDGERENALAARQIDALRIRARGPAQP 403
Cdd:COG3845  320 EDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYrrPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTP 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 404 VAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:COG3845  400 ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
                        490       500
                 ....*....|....*....|..
gi 490656625 484 MHAVFERGGWTQDAlLGAAFAG 505
Cdd:COG3845  480 IVGEVPAAEATREE-IGLLMAG 500
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
12-502 4.13e-146

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 429.04  E-value: 4.13e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  12 TPTLVVTGIGKTYaeP---VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL 88
Cdd:PRK10762   2 QALLQLKGIDKAF--PgvkALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  89 GVRMVMQELNLVPTLTVAENLFLDRLP-HRFGVIDRRRLAADARAAMARVGLdSLDPDTLVGSLGIGHQQMVEIARSLAG 167
Cdd:PRK10762  80 GIGIIHQELNLIPQLTIAENIFLGREFvNRFGRIDWKKMYAEADKLLARLNL-RFSSDKLVGELSIGEQQMVEIAKVLSF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMA 247
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 248 GREIAEQAVHGTRTPGAPRLRVERLSrGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRP 327
Cdd:PRK10762 239 GRKLEDQYPRLDKAPGEVRLKVDNLS-GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG--HE 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 328 AAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVAR-GGVVDGERENALAARQIDALRIRARGPAQPVAE 406
Cdd:PRK10762 316 VVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRaGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGL 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 407 LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISG 475
                        490
                 ....*....|....*.
gi 490656625 487 VFERGGWTQDALLGAA 502
Cdd:PRK10762 476 EFTREQATQEKLMAAA 491
GguA NF040905
sugar ABC transporter ATP-binding protein;
19-499 1.47e-143

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 422.28  E-value: 1.47e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  19 GIGKTYAePV--LDDVSLALYPGEALALTGENGAGKSTLSKIVAGlVAPT---TGAMRLAGAEYAPHSRAHAEALGVRMV 93
Cdd:NF040905   6 GITKTFP-GVkaLDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVCRFKDIRDSEALGIVII 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 MQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDSlDPDTLVGSLGIGHQQMVEIARSLAGDCRVLI 173
Cdd:NF040905  84 HQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDE-SPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 174 LDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV-HVDRIDAQPTE-RLVALMAGREI 251
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIeTLDCRADEVTEdRIIRGMVGRDL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 252 AEQAVHGTRTPGAPRLRVERLSRGD-------AVRDVSFDVRAGEIFGISGLIGAGRTELLRLV----YGADAAdgGTVS 320
Cdd:NF040905 243 EDRYPERTPKIGEVVFEVKNWTVYHplhperkVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsYGRNIS--GTVF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 321 IGDppRPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRARGP 400
Cdd:NF040905 321 KDG--KEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMNIKTPSV 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 401 AQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMS 480
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478
                        490
                 ....*....|....*....
gi 490656625 481 AGRMHAVFERGGWTQDALL 499
Cdd:NF040905 479 EGRITGELPREEASQERIM 497
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
12-489 1.96e-135

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 401.86  E-value: 1.96e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  12 TPTLVVTGIGKTYAePV--LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG 89
Cdd:PRK09700   3 TPYISMAGIGKSFG-PVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  90 VRMVMQELNLVPTLTVAENLFLDRLPHR--FGV--IDRRRLAADARAAMARVGLdSLDPDTLVGSLGIGHQQMVEIARSL 165
Cdd:PRK09700  82 IGIIYQELSVIDELTVLENLYIGRHLTKkvCGVniIDWREMRVRAAMMLLRVGL-KVDLDEKVANLSISHKQMLEIAKTL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 166 AGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVAL 245
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 246 MAGREI-----AEQAVHGtRTPGAPRLRVERLSRGDA--VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGT 318
Cdd:PRK09700 241 MVGRELqnrfnAMKENVS-NLAHETVFEVRNVTSRDRkkVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 319 VSI-GDPPRPaaiRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVAR----GGVVDGERENALAARQIDAL 393
Cdd:PRK09700 320 IRLnGKDISP---RSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGykgaMGLFHEVDEQRTAENQRELL 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 394 RIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLIC 473
Cdd:PRK09700 397 ALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVC 476
                        490
                 ....*....|....*.
gi 490656625 474 DRIGVMSAGRMHAVFE 489
Cdd:PRK09700 477 DRIAVFCEGRLTQILT 492
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
15-502 1.49e-123

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: 371.08  E-value: 1.49e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTT--GAMRLAGAEYAPHSRAHAEALGVR 91
Cdd:TIGR02633   2 LEMKGIVKTFGGvKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   92 MVMQELNLVPTLTVAENLFL-DRLPHRFGVIDRRRLAADARAAMARVGLDSlDPDTL-VGSLGIGHQQMVEIARSLAGDC 169
Cdd:TIGR02633  82 IIHQELTLVPELSVAENIFLgNEITLPGGRMAYNAMYLRAKNLLRELQLDA-DNVTRpVGDYGGGQQQLVEIAKALNKQA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  170 RVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGR 249
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  250 EIAEQAVHGTRTPGAPRLRVERLSRGDA-------VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGA-DAADGGTVSI 321
Cdd:TIGR02633 241 EITSLYPHEPHEIGDVILEARNLTCWDVinphrkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  322 GDppRPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRARGPA 401
Cdd:TIGR02633 321 NG--KPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPF 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  402 QPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSA 481
Cdd:TIGR02633 399 LPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGE 478
                         490       500
                  ....*....|....*....|.
gi 490656625  482 GRMHAVFERGGWTQDALLGAA 502
Cdd:TIGR02633 479 GKLKGDFVNHALTQEQVLAAA 499
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
12-511 2.06e-117

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 355.90  E-value: 2.06e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  12 TPTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGV 90
Cdd:PRK15439   9 PPLLCARSISKQYSGvEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  91 RMVMQELNLVPTLTVAENLfLDRLPHRfgvidrRRLAADARAAMARVGLdSLDPDTLVGSLGIGHQQMVEIARSLAGDCR 170
Cdd:PRK15439  89 YLVPQEPLLFPNLSVKENI-LFGLPKR------QASMQKMKQLLAALGC-QLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 171 VLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGRE 250
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITPAA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 251 IAEQAV------------HGTRTPGAPRLRVERLSrGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGT 318
Cdd:PRK15439 241 REKSLSasqklwlelpgnRRQQAAGAPVLTVEDLT-GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 319 VSIGDppRPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSlgQLARVARGGVVDGERENALAARQIDALRIRAR 398
Cdd:PRK15439 320 IMLNG--KEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVC--ALTHNRRGFWIKPARENAVLERYRRALNIKFN 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 399 GPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGV 478
Cdd:PRK15439 396 HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLV 475
                        490       500       510
                 ....*....|....*....|....*....|...
gi 490656625 479 MSAGRMHAVFERGGWTQDALLGAAFAGYARRDA 511
Cdd:PRK15439 476 MHQGEISGALTGAAINVDTIMRLAFGEHQAQEA 508
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
18-499 2.61e-117

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 354.81  E-value: 2.61e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  18 TGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVRMVMQE 96
Cdd:PRK10982   2 SNISKSFpGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  97 LNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDsLDPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDE 176
Cdd:PRK10982  82 LNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDID-IDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 177 PTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGREIAEQAV 256
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRFP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 257 HGTRTPGAPRLRVERLS--RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPA 334
Cdd:PRK10982 241 DKENKPGEVILEVRNLTslRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG--KKINNHNAN 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 335 DAVRHGIALVSEDRKGEGlllpqsIAANLSLGQLARVA-------RGGVVDGERENALAARQIDALRIRARGPAQPVAEL 407
Cdd:PRK10982 319 EAINHGFALVTEERRSTG------IYAYLDIGFNSLISnirnyknKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSL 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 408 SGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
                        490
                 ....*....|..
gi 490656625 488 FERGGWTQDALL 499
Cdd:PRK10982 473 VDTKTTTQNEIL 484
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
263-484 3.10e-79

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: 245.80  E-value: 3.10e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 263 GAPRLRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHGIA 342
Cdd:cd03215    1 GEPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG--KPVTRRSPRDAIRAGIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDRKGEGLLLPQSIAANLSLGQLarvarggvvdgerenalaarqidalrirargpaqpvaeLSGGNQQKVAIGRWLG 422
Cdd:cd03215   79 YVPEDRKREGLVLDLSVAENIALSSL--------------------------------------LSGGNQQKVVLARWLA 120
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 423 RDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03215  121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
15-229 1.31e-66

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: 212.29  E-value: 1.31e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVRMV 93
Cdd:cd03216    1 LELRGITKRFgGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 MQelnlvptltvaenlfldrlphrfgvidrrrlaadaraamarvgldsldpdtlvgsLGIGHQQMVEIARSLAGDCRVLI 173
Cdd:cd03216   81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 174 LDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03216  106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
12-483 5.95e-59

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: 203.21  E-value: 5.95e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  12 TPTLVVTGIGKTY---AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPT---TGAMRLAGAEYAPHSRAHA 85
Cdd:COG1123    2 TPLLEVRDLSVRYpggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  86 eALGVRMVMQE--LNLVPtLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVE 160
Cdd:COG1123   82 -GRRIGMVFQDpmTQLNP-VTVGDQI---AEALENLGLSRAEARARVLELLEAVGLERRldrYPHQLSG----GQRQRVA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 161 IARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV---HVDRIDA 236
Cdd:COG1123  153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVedgPPEEILA 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 237 QPteRLVALMAGREIAEQAVHGTRTPGAPRLRVERLSRG---------DAVRDVSFDVRAGEIFGISGLIGAGRTELLRL 307
Cdd:COG1123  233 AP--QALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRypvrgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 308 VYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSEDrkGEGLLLP-QSIAANLSLGQLARvargGVVDGERENALA 386
Cdd:COG1123  311 LLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQD--PYSSLNPrMTVGDIIAEPLRLH----GLLSRAERRERV 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 387 ARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSD 465
Cdd:COG1123  385 AELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHD 464
                        490
                 ....*....|....*...
gi 490656625 466 LRELMLICDRIGVMSAGR 483
Cdd:COG1123  465 LAVVRYIADRVAVMYDGR 482
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
15-236 1.12e-42

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 151.75  E-value: 1.12e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVrmV 93
Cdd:COG1131    1 IEVRGLTKRYGDkTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGY--V 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 MQELNLVPTLTVAENL-FLDRLphrFGvIDRRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVL 172
Cdd:COG1131   79 PQEPALYPDLTVRENLrFFARL---YG-LPRKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELL 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 173 ILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDA 236
Cdd:COG1131  154 ILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE 217
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
15-229 3.08e-38

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 139.88  E-value: 3.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE---YAPHSRAHaeaLGV 90
Cdd:cd03219    1 LEVRGLTKRFGGlVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitgLPPHEIAR---LGI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  91 RMVMQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMA-------RVGLDSLDpDTLVGSLGIGHQQMVEIAR 163
Cdd:cd03219   78 GRTFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREAREraeelleRVGLADLA-DRPAGELSYGQQRRLEIAR 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 164 SLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03219  157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
15-229 7.61e-37

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: 136.10  E-value: 7.61e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG 89
Cdd:cd03257    2 LEVKNLSVSFPTgggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  90 --VRMVMQE----LNlvPTLTVAEnLFLDRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGSLGIGHQQMVEIAR 163
Cdd:cd03257   82 keIQMVFQDpmssLN--PRMTIGE-QIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIAR 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 164 SLAGDCRVLILDEPTAML---TAREVELLFDQIARLKadGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03257  159 ALALNPKLLIADEPTSALdvsVQAQILDLLKKLQEEL--GLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
16-236 1.17e-36

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: 135.25  E-value: 1.17e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  16 VVTGIGKTyaePVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE---YAPHSRAHAealGVRM 92
Cdd:cd03224    6 LNAGYGKS---QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDitgLPPHERARA---GIGY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  93 VMQELNLVPTLTVAENLFLDRLPHRFGVIDRRrlaadaraamarvgLD---SLDP------DTLVGSLGIGHQQMVEIAR 163
Cdd:cd03224   80 VPEGRRIFPELTVEENLLLGAYARRRAKRKAR--------------LErvyELFPrlkerrKQLAGTLSGGEQQMLAIAR 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 164 SLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDA 236
Cdd:cd03224  146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAE 218
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
25-227 1.31e-36

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: 134.90  E-value: 1.31e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  25 AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAeALGVRMVMQ--ELNLVpT 102
Cdd:cd03225   13 ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL-RRKVGLVFQnpDDQFF-G 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENLFldrlphrFGV----IDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAGDCRVLILD 175
Cdd:cd03225   91 PTVEEEVA-------FGLenlgLPEEEIEERVEEALELVGLEGLrdrSPFTLSG----GQKQRVAIAGVLAMDPDILLLD 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490656625 176 EPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:cd03225  160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
11-229 2.79e-36

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: 135.17  E-value: 2.79e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  11 DTPTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEY---APHSRAHae 86
Cdd:COG0411    1 SDPLLEVRGLTKRFGGlVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglPPHRIAR-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  87 aLGVRMVMQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMAR------------VGLDSLdPDTLVGSLGIG 154
Cdd:COG0411   79 -LGIARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLPRARREEReareraeellerVGLADR-ADEPAGNLSYG 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 155 HQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG0411  157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
15-228 2.86e-36

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: 132.52  E-value: 2.86e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVrmV 93
Cdd:cd03230    1 IEVRNLSKRYGKkTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGY--L 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 MQELNLVPTLTVAENLFLdrlphrfgvidrrrlaadaraamarvgldsldpdtlvgSLGIghQQMVEIARSLAGDCRVLI 173
Cdd:cd03230   79 PEEPSLYENLTVRENLKL--------------------------------------SGGM--KQRLALAQALLHDPELLI 118
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 174 LDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:cd03230  119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
5-229 3.97e-36

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: 140.81  E-value: 3.97e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   5 DPDSTPDTPTLVVTGIGKTYAE------PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA 78
Cdd:COG1123  251 APAAAAAEPLLEVRNLSKRYPVrgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLT 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  79 PHSRAHAEALG--VRMVMQ--ELNLVPTLTVAENlfLDRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGSLGIG 154
Cdd:COG1123  331 KLSRRSLRELRrrVQMVFQdpYSSLNPRMTVGDI--IAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGG 408
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 155 HQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG1123  409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
12-233 4.95e-36

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 133.63  E-value: 4.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  12 TPTLVVTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRA 83
Cdd:COG1136    2 SPLLELRNLTKSYGTgegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdiSSLSERELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  84 H--AEALGvrMVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEI 161
Cdd:COG1136   82 RlrRRHIG--FVFQFFNLLPELTALENV---ALPLLLAGVSRKERRERARELLERVGLGDRL-DHRPSQLSGGQQQRVAI 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 162 ARSLAGDCRVLILDEPTAML---TAREVELLFDQIARlkADGVALVYISHRlEELARVAQRVAVLRDGRLVHVDR 233
Cdd:COG1136  156 ARALVNRPKLILADEPTGNLdskTGEEVLELLRELNR--ELGTTIVMVTHD-PELAARADRVIRLRDGRIVSDER 227
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
15-236 1.26e-34

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: 130.36  E-value: 1.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVrmV 93
Cdd:COG4555    2 IEVENLSKKYgKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV--L 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 MQELNLVPTLTVAENL-FLDRLpHRfgvIDRRRLAADARAAMARVGLDSlDPDTLVGSLGIGHQQMVEIARSLAGDCRVL 172
Cdd:COG4555   80 PDERGLYDRLTVRENIrYFAEL-YG---LFDEELKKRIEELIELLGLEE-FLDRRVGELSTGMKKKVALARALVHDPKVL 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 173 ILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDA 236
Cdd:COG4555  155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
15-232 8.76e-34

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: 127.25  E-value: 8.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRahaealGV 90
Cdd:cd03259    1 LELKGLSKTYGSvRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvTGVPPERR------NI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  91 RMVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAG 167
Cdd:cd03259   75 GMVFQDYALFPHLTVAENI---AFGLKLRGVPKAEIRARVRELLELVGLEGLlnrYPHELSG----GQQQRVALARALAR 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:cd03259  148 EPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
26-229 3.73e-33

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: 125.91  E-value: 3.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHS-RAHAEALGvrMVMQ--ELNLVpT 102
Cdd:COG1122   14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlRELRRKVG--LVFQnpDDQLF-A 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENL-FLdrlPHRFGViDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPT 178
Cdd:COG1122   91 PTVEEDVaFG---PENLGL-PREEIRERVEEALELVGLEHLadrPPHELSG----GQKQRVAIAGVLAMEPEVLVLDEPT 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490656625 179 AMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG1122  163 AGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
15-228 4.21e-33

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: 125.29  E-value: 4.21e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRAHAE 86
Cdd:cd03255    1 IELKNLSKTYGGggekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdiSKLSEKELAAFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  87 ALGVRMVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLA 166
Cdd:cd03255   81 RRHIGFVFQSFNLLPDLTALENV---ELPLLLAGVPKKERRERAEELLERVGLGDRL-NHYPSELSGGQQQRVAIARALA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 167 GDCRVLILDEPTAML---TAREV-ELLFDQiarLKADGVALVYISHRlEELARVAQRVAVLRDGRL 228
Cdd:cd03255  157 NDPKIILADEPTGNLdseTGKEVmELLREL---NKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
16-230 1.58e-32

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: 124.32  E-value: 1.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  16 VVTGIGKTyaePVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE---YAPHSRAHaeaLGVRM 92
Cdd:COG0410    9 LHAGYGGI---HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDitgLPPHRIAR---LGIGY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  93 VMQELNLVPTLTVAENLFLDRLPHRfgvidrrrlaadaraaMARVGLDSLD------P------DTLVGSLGIGHQQMVE 160
Cdd:COG0410   83 VPEGRRIFPSLTVEENLLLGAYARR----------------DRAEVRADLErvyelfPrlkerrRQRAGTLSGGEQQMLA 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 161 IARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:COG0410  147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVL 216
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
15-229 3.24e-32

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: 123.76  E-value: 3.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYaPHSRAHAEALG 89
Cdd:COG1124    2 LEVRNLSVSYGQggrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV-TRRRRKAFRRR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  90 VRMVMQE----LNlvPTLTVAENLFLDRLPHRFGVIDRRRLAADARaamarVGLDS--LD--PDTLVGslgiGHQQMVEI 161
Cdd:COG1124   81 VQMVFQDpyasLH--PRHTVDRILAEPLRIHGLPDREERIAELLEQ-----VGLPPsfLDryPHQLSG----GQRQRVAI 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 162 ARSLAGDCRVLILDEPTAML----TAREVELLfdqiARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG1124  150 ARALILEPELLLLDEPTSALdvsvQAEILNLL----KDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
27-503 9.08e-32

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: 128.26  E-value: 9.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKS--TLSkiVAGLVAP----TTGAMRLAGAEYAPHSRahAEALGVR-----MVMQ 95
Cdd:COG4172   24 EAVKGVSFDIAAGETLALVGESGSGKSvtALS--ILRLLPDpaahPSGSILFDGQDLLGLSE--RELRRIRgnriaMIFQ 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  96 E----LNlvPTLTV----AENLFLdrlpHRfgVIDRRRLAADARAAMARVGLDslDPDTLVGS----LGIGHQQMVEIAR 163
Cdd:COG4172  100 EpmtsLN--PLHTIgkqiAEVLRL----HR--GLSGAAARARALELLERVGIP--DPERRLDAyphqLSGGQRQRVMIAM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 164 SLAGDCRVLILDEPTamlTAREV-------ELLfdqiARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV---HVD 232
Cdd:COG4172  170 ALANEPDLLIADEPT---TALDVtvqaqilDLL----KDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVeqgPTA 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 233 RIDAQP----TERLVALMAGREIAEQAvhgtrTPGAPRLRVERLS------RG---------DAVRDVSFDVRAGEIFGI 293
Cdd:COG4172  243 ELFAAPqhpyTRKLLAAEPRGDPRPVP-----PDAPPLLEARDLKvwfpikRGlfrrtvghvKAVDGVSLTLRRGETLGL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 294 SGLIGAGRTEL----LRLVygadaADGGTVSIGDPP----RPAAIRspadAVRHGIALVSEDRKGeglllpqSIAANLSL 365
Cdd:COG4172  318 VGESGSGKSTLglalLRLI-----PSEGEIRFDGQDldglSRRALR----PLRRRMQVVFQDPFG-------SLSPRMTV 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 366 GQLA----RVARGGVVDGEREnalaARQIDALR-------IRARGPaqpvAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:COG4172  382 GQIIaeglRVHGPGLSAAERR----ARVAEALEevgldpaARHRYP----HEFSGGQRQRIAIARALILEPKLLVLDEPT 453
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 435 RGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRM------HAVFE--RGGWTQdALLGAAF 503
Cdd:COG4172  454 SALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVveqgptEQVFDapQHPYTR-ALLAAAP 530
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
267-484 2.31e-31

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 121.32  E-value: 2.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpAAIRSPADAVRHGIA 342
Cdd:COG1131    1 IEVRGLTKryGDktALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLG----EDVARDPAEVRRRIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEdrkgEGLLLPqsiaaNLSLGQ-LARVARGGVVDGERENALAARQIDALRIRARgPAQPVAELSGGNQQKVAIGRWL 421
Cdd:COG1131   77 YVPQ----EPALYP-----DLTVREnLRFFARLYGLPRKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALAL 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 422 GRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:COG1131  147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
29-179 5.58e-31

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: 117.36  E-value: 5.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAlGVRMVMQELNLVPTLTVAEN 108
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVREN 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625  109 LfldRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTL---VGSLGIGHQQMVEIARSLAGDCRVLILDEPTA 179
Cdd:pfam00005  80 L---RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
13-216 1.14e-30

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: 118.35  E-value: 1.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  13 PTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVr 91
Cdd:COG4133    1 MMLEAENLSCRRGErLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAY- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  92 mVMQELNLVPTLTVAENL-FLDRLphrFGVidrRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCR 170
Cdd:COG4133   80 -LGHADGLKPELTVRENLrFWAAL---YGL---RADREAIDEALEAVGLAGLA-DLPVRQLSAGQKRRVALARLLLSPAP 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 490656625 171 VLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARV 216
Cdd:COG4133  152 LWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAA 197
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
17-485 1.26e-30

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 124.79  E-value: 1.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  17 VTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyaphsrahaealGVRM--V 93
Cdd:COG0488    1 LENLSKSFgGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK--------------GLRIgyL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 MQELNLVPTLTVAENLF-----------------------------LDRLPHRFGVIDRRRLAADARAAMARVGLDSLDP 144
Cdd:COG0488   67 PQEPPLDDDLTVLDTVLdgdaelraleaeleeleaklaepdedlerLAELQEEFEALGGWEAEARAEEILSGLGFPEEDL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 145 DTLVGSLGiGHQQM-VEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAdgvALVYISHRLEELARVAQRVAVL 223
Cdd:COG0488  147 DRPVSELS-GGWRRrVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG---TVLVVSHDRYFLDRVATRILEL 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 224 RDGRLVH------------------------------------VDRIDA------QPTERLVALMAGREIAEQAVHGT-- 259
Cdd:COG0488  223 DRGKLTLypgnysayleqraerleqeaaayakqqkkiakeeefIRRFRAkarkakQAQSRIKALEKLEREEPPRRDKTve 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 260 -RTPGAPR-----LRVERLSRGDA----VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGdpprpaa 329
Cdd:COG0488  303 iRFPPPERlgkkvLELEGLSKSYGdktlLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG------- 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 330 irspaDAVRhgIALVSEDRkgEGLLLPQSIAANLSlgqlaRVARGGvvdGEREnalaARQI---------DALrirargp 400
Cdd:COG0488  376 -----ETVK--IGYFDQHQ--EELDPDKTVLDELR-----DGAPGG---TEQE----VRGYlgrflfsgdDAF------- 427
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 401 aQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAkfdIYALLDALAR-EGrAIVVVSSDlRELM-LICDRIGV 478
Cdd:COG0488  428 -KPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET---LEALEEALDDfPG-TVLLVSHD-RYFLdRVATRILE 501

                 ....*..
gi 490656625 479 MSAGRMH 485
Cdd:COG0488  502 FEDGGVR 508
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
13-229 6.62e-30

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 117.47  E-value: 6.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  13 PTLVVTGIGKTYA--EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL-- 88
Cdd:COG3638    1 PMLELRNLSKRYPggTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  89 GVRMVMQELNLVPTLTVAENLFLDRLPHR------FGVIDRRRLAAdaraamarvGLDSLD-----------PDTLVGsl 151
Cdd:COG3638   81 RIGMIFQQFNLVPRLSVLTNVLAGRLGRTstwrslLGLFPPEDRER---------ALEALErvgladkayqrADQLSG-- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 152 giGHQQMVEIARSLAGDCRVLILDEPTAML---TAREVELLFDQIARlkADGVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:COG3638  150 --GQQQRVAIARALVQEPKLILADEPVASLdpkTARQVMDLLRRIAR--EDGITVVVNLHQVDLARRYADRIIGLRDGRV 225

                 .
gi 490656625 229 V 229
Cdd:COG3638  226 V 226
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
9-253 1.63e-29

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 116.73  E-value: 1.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   9 TPDTPTLVVTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRa 83
Cdd:COG1116    2 SAAAPALELRGVSKRFPTggggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  84 haealGVRMVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGL-DSLD--PDTLVGslgiGHQQMVE 160
Cdd:COG1116   81 -----DRGVVFQEPALLPWLTVLDNV---ALGLELRGVPKAERRERARELLELVGLaGFEDayPHQLSG----GMRQRVA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 161 IARSLAGDCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVL--RDGRLVHVDRIDAq 237
Cdd:COG1116  149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEEIDVDL- 227
                        250
                 ....*....|....*.
gi 490656625 238 PTERLVALMAGREIAE 253
Cdd:COG1116  228 PRPRDRELRTSPEFAA 243
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
15-235 2.32e-29

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: 115.26  E-value: 2.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAhaealg 89
Cdd:cd03293    1 LEVRNVSKTYGGgggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  90 VRMVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLA 166
Cdd:cd03293   75 RGYVFQQDALLPWLTVLDNV---ALGLELQGVPKAEARERAEELLELVGLSGFEnayPHQLSG----GMRQRVALARALA 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 167 GDCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVL--RDGRLVHVDRID 235
Cdd:cd03293  148 VDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVEVD 219
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
267-487 3.36e-29

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: 115.34  E-value: 3.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpAAIRSPADAVRHGIA 342
Cdd:COG4555    2 IEVENLSKkyGKvpALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG----EDVRKEPREARRQIG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDRkgeGLLLPQSIAANLSLgqLARVARggvVDGERENALAARQIDALRIRaRGPAQPVAELSGGNQQKVAIGRWLG 422
Cdd:COG4555   78 VLPDER---GLYDRLTVRENIRY--FAELYG---LFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALV 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 423 RDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:COG4555  149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQ 213
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
15-227 6.32e-29

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: 112.67  E-value: 6.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG-VRM 92
Cdd:cd03229    1 LELKNVSKRYGQkTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRrIGM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  93 VMQELNLVPTLTVAENLFLdrlphrfgvidrrrlaadaraamarvgldsldpdtlvgSLGIGHQQMVEIARSLAGDCRVL 172
Cdd:cd03229   81 VFQDFALFPHLTVLENIAL--------------------------------------GLSGGQQQRVALARALAMDPDVL 122
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 173 ILDEPTAML---TAREVELLFDQIARLkaDGVALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:cd03229  123 LLDEPTSALdpiTRREVRALLKSLQAQ--LGITVVLVTHDLDEAARLADRVVVLRDGK 178
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
15-230 1.80e-28

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: 112.60  E-value: 1.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE---PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVr 91
Cdd:cd03263    1 LQIRNLTKTYKKgtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGY- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  92 mVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSlDPDTLVGSLGIGHQQMVEIARSLAGDCRV 171
Cdd:cd03263   80 -CPQFDALFDELTVREHL---RFYARLKGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSV 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 172 LILDEPTAMLTAREVELLFDQIARLKAdGVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:cd03263  155 LLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRC 212
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
17-227 2.71e-28

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: 110.03  E-value: 2.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  17 VTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRaHAEALGVRMVMQ 95
Cdd:cd00267    2 IENLSFRYGGrTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL-EELRRRIGYVPQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  96 elnlvptltvaenlfldrlphrfgvidrrrlaadaraamarvgldsldpdtLVGslgiGHQQMVEIARSLAGDCRVLILD 175
Cdd:cd00267   81 ---------------------------------------------------LSG----GQRQRVALARALLLNPDLLLLD 105
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490656625 176 EPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:cd00267  106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
15-230 4.77e-28

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: 112.44  E-value: 4.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAH-AEALGVrm 92
Cdd:COG1120    2 LEAENLSVGYGGrPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElARRIAY-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  93 VMQELNLVPTLTVAENLFLDRLPHR-FGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRV 171
Cdd:COG1120   80 VPQEPPAPFGLTVRELVALGRYPHLgLFGRPSAEDREAVEEALERTGLEHLA-DRPVDELSGGERQRVLIARALAQEPPL 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 172 LILDEPTAML-TAREVELLfDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:COG1120  159 LLLDEPTSHLdLAHQLEVL-ELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
15-228 5.74e-28

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: 109.61  E-value: 5.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYA---EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyAPHSRAHAEALGVR 91
Cdd:cd03246    1 LEVENVSFRYPgaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG---ADISQWDPNELGDH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  92 M--VMQELNLVPTlTVAENLfldrlphrfgvidrrrlaadaraamarvgldsldpdtlvgsLGIGHQQMVEIARSLAGDC 169
Cdd:cd03246   78 VgyLPQDDELFSG-SIAENI-----------------------------------------LSGGQRQRLGLARALYGNP 115
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 170 RVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARvAQRVAVLRDGRL 228
Cdd:cd03246  116 RILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
28-229 1.53e-27

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: 109.65  E-value: 1.53e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAealgVRMVMQELNL-VPTLTVA 106
Cdd:cd03226   15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS----IGYVMQDVDYqLFTDSVR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 107 ENLFL--DRLPHRFGVIDRRrlaadaraamarvgLDSLDPDTLVG----SLGIGHQQMVEIARSLAGDCRVLILDEPTAM 180
Cdd:cd03226   91 EELLLglKELDAGNEQAETV--------------LKDLDLYALKErhplSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490656625 181 LTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03226  157 LDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
267-484 2.20e-27

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: 108.25  E-value: 2.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLS----RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAAIRspadaVRHGI 341
Cdd:cd03230    1 IEVRNLSkrygKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIKKEPEE-----VKRRI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 342 ALVSEDRKgegllLPQsiaaNLSLgqlarvarggvvdgeRENAlaarqidalrirargpaqpvaELSGGNQQKVAIGRWL 421
Cdd:cd03230   76 GYLPEEPS-----LYE----NLTV---------------RENL---------------------KLSGGMKQRLALAQAL 110
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 422 GRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03230  111 LHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
15-229 2.46e-27

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: 109.23  E-value: 2.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphsrAHAEALGVRMV 93
Cdd:cd03268    1 LKTNDLTKTYGKkRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ----KNIEALRRIGA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 MQEL-NLVPTLTVAENLFLDRLPHRFG------VIDrrrlaadaraamaRVGLDSlDPDTLVGSLGIGHQQMVEIARSLA 166
Cdd:cd03268   77 LIEApGFYPNLTARENLRLLARLLGIRkkrideVLD-------------VVGLKD-SAKKKVKGFSLGMKQRLGIALALL 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 167 GDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03268  143 GNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
10-230 4.29e-27

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 109.41  E-value: 4.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  10 PDTPTLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRahaeal 88
Cdd:COG1121    2 MMMPAIELENLTVSYgGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR------ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  89 gvRM--VMQELNLVPT--LTVAENLFLDRLPHR-FGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIAR 163
Cdd:COG1121   76 --RIgyVPQRAEVDWDfpITVRDVVLMGRYGRRgLFRRPSRADREAVDEALERVGLEDLA-DRPIGELSGGQQQRVLLAR 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 164 SLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:COG1121  153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH 219
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
15-244 7.20e-27

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: 108.48  E-value: 7.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYA-EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA---PHSRahaealGV 90
Cdd:cd03300    1 IELENVSKFYGgFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITnlpPHKR------PV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  91 RMVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAG 167
Cdd:cd03300   75 NTVFQNYALFPHLTVFENI---AFGLRLKKLPKAEIKERVAEALDLVQLEGYanrKPSQLSG----GQQQRVAIARALVN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVDR---IDAQPTERLV 243
Cdd:cd03300  148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTpeeIYEEPANRFV 227

                 .
gi 490656625 244 A 244
Cdd:cd03300  228 A 228
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
15-229 1.05e-26

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: 108.42  E-value: 1.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE--PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYapHSRAHAEALGVR- 91
Cdd:cd03256    1 IEVENLSKTYPNgkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDI--NKLKGKALRQLRr 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  92 ---MVMQELNLVPTLTVAENLFLDRLPHR---------FGVIDrrrlAADARAAMARVGLDSL---DPDTLVGslgiGHQ 156
Cdd:cd03256   79 qigMIFQQFNLIERLSVLENVLSGRLGRRstwrslfglFPKEE----KQRALAALERVGLLDKayqRADQLSG----GQQ 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 157 QMVEIARSLAGDCRVLILDEPTAML---TAREVELLFDQIARlkADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03256  151 QRVAIARALMQQPKLILADEPVASLdpaSSRQVMDLLKRINR--EEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
11-232 1.42e-26

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 110.57  E-value: 1.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  11 DTPTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA---PHSRahae 86
Cdd:COG3842    2 AMPALELENVSKRYGDvTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglpPEKR---- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  87 alGVRMVMQELNLVPTLTVAENLfldrlphRFG----VIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMV 159
Cdd:COG3842   78 --NVGMVFQDYALFPHLTVAENV-------AFGlrmrGVPKAEIRARVAELLELVGLEGLAdryPHQLSG----GQQQRV 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 160 EIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:COG3842  145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVG 218
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
8-229 2.08e-26

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: 107.13  E-value: 2.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   8 STPDTPTLVVTGIGKTYAEP-----VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHS- 81
Cdd:COG4181    2 SSSSAPIIELRGLTKTVGTGageltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDe 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  82 --RAHAEALGVRMVMQELNLVPTLTVAEN----LFLDRLPHRFGvidrrrlaaDARAAMARVGL-DSLD--PDTLVGslg 152
Cdd:COG4181   82 daRARLRARHVGFVFQSFQLLPTLTALENvmlpLELAGRRDARA---------RARALLERVGLgHRLDhyPAQLSG--- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 153 iGHQQMVEIARSLAGDCRVLILDEPTAMLTARE----VELLFDQIARLkadGVALVYISHRlEELARVAQRVAVLRDGRL 228
Cdd:COG4181  150 -GEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRER---GTTLVLVTHD-PALAARCDRVLRLRAGRL 224

                 .
gi 490656625 229 V 229
Cdd:COG4181  225 V 225
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
25-229 4.65e-26

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: 112.23  E-value: 4.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  25 AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHS-RAHaealgVRMVMQELNLV 100
Cdd:COG2274  487 SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlRQIDPASlRRQ-----IGVVLQDVFLF 561
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 101 PTlTVAENL-----------------------FLDRLPHRFgvidrrrlaadaraamarvgldsldpDTLVGSLGI---G 154
Cdd:COG2274  562 SG-TIRENItlgdpdatdeeiieaarlaglhdFIEALPMGY--------------------------DTVVGEGGSnlsG 614
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 155 HQ-QMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAdGVALVYISHRLeELARVAQRVAVLRDGRLV 229
Cdd:COG2274  615 GQrQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLDKGRIV 688
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
28-228 1.06e-25

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: 103.67  E-value: 1.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVRMV----MQELnLVPTL 103
Cdd:cd03215   15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVpedrKREG-LVLDL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLFLDRLphrfgvidrrrlaadaraamarvgldsldpdtLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAMLTA 183
Cdd:cd03215   94 SVAENIALSSL--------------------------------LSG----GNQQKVVLARWLARDPRVLILDEPTRGVDV 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 490656625 184 REVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:cd03215  138 GAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
15-251 1.28e-25

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: 105.11  E-value: 1.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSrahAEALGVRMVM 94
Cdd:cd03299    1 LKVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP---PEKRDISYVP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  95 QELNLVPTLTVAENLfldrlphRFGV----IDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAG 167
Cdd:cd03299   78 QNYALFPHMTVYKNI-------AYGLkkrkVDKKEIERKVLEIAEMLGIDHLlnrKPETLSG----GEQQRVAIARALVV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLVHV---DRIDAQPTERLV 243
Cdd:cd03299  147 NPKILLLDEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVgkpEEVFKKPKNEFV 226

                 ....*...
gi 490656625 244 ALMAGREI 251
Cdd:cd03299  227 AEFLGFNN 234
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
19-233 1.84e-25

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 104.36  E-value: 1.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  19 GIGKTYAE--PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALgvR----M 92
Cdd:COG2884    6 NVSKRYPGgrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL--RrrigV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  93 VMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDC 169
Cdd:COG2884   84 VFQDFRLLPDRTVYENV---ALPLRVTGKSRKEIRRRVREVLDLVGLSDKAkalPHELSG----GEQQRVAIARALVNRP 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 170 RVLILDEPTAML---TAREVELLFDQIARLkadGVALVYISHRLEELARVAQRVAVLRDGRLVHVDR 233
Cdd:COG2884  157 ELLLADEPTGNLdpeTSWEIMELLEEINRR---GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
15-231 1.97e-25

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: 103.90  E-value: 1.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLagaEYAPHSRAHAEALGvrMV 93
Cdd:cd03269    1 LEVENVTKRFGRvTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF---DGKPLDIAARNRIG--YL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 MQELNLVPTLTVAENLF----------------LDRLPHRFGVIDRRrlaadaraamarvgldsldpDTLVGSLGIGHQQ 157
Cdd:cd03269   76 PEERGLYPKMKVIDQLVylaqlkglkkeearrrIDEWLERLELSEYA--------------------NKRVEELSKGNQQ 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 158 MVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHV 231
Cdd:cd03269  136 KVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
267-486 2.90e-25

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: 104.06  E-value: 2.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHGIA 342
Cdd:cd03219    1 LEVRGLTKrfGGlvALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG--EDITGLPPHEIARLGIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 ----LVSedrkgeglLLPQ-SIAANLSLGQLARVARG----GVVDGERE-NALAARQIDALRIRARGpAQPVAELSGGNQ 412
Cdd:cd03219   79 rtfqIPR--------LFPElTVLENVMVAAQARTGSGlllaRARREEREaRERAEELLERVGLADLA-DRPAGELSYGQQ 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 413 QKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:cd03219  150 RRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIA 223
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
278-486 4.61e-25

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: 101.74  E-value: 4.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHgIALVsedrkgeglllPQ 357
Cdd:cd03214   15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG--KDLASLSPKELARK-IAYV-----------PQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 siaanlslgqlarvarggvvdgerenALAARQIDALRIRargpaqPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGI 437
Cdd:cd03214   81 --------------------------ALELLGLAHLADR------PFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490656625 438 DVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:cd03214  129 DIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
277-487 5.76e-25

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: 102.83  E-value: 5.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPprpAAIRSPAdAVRHGIALVSEdrkGEGLLLP 356
Cdd:cd03266   20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF---DVVKEPA-EARRRLGFVSD---STGLYDR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLS-LGQLARVARGGVVDgeRENALAAR-QIDALRIRargpaqPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:cd03266   93 LTARENLEyFAGLYGLKGDELTA--RLEELADRlGMEELLDR------RVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490656625 435 RGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:cd03266  165 TGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
267-487 6.31e-25

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: 102.60  E-value: 6.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSR----GDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPAdavRHGIA 342
Cdd:cd03259    1 LELKGLSKtygsVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG--RDVTGVPPE---RRNIG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDRkgeGLLLPQSIAANLSLGqlarVARGGVVDGEREnALAARQIDALRIRARGPAQPvAELSGGNQQKVAIGRWLG 422
Cdd:cd03259   76 MVFQDY---ALFPHLTVAENIAFG----LKLRGVPKAEIR-ARVRELLELVGLEGLLNRYP-HELSGGQQQRVALARALA 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 423 RDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:cd03259  147 REPSLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
28-229 7.34e-25

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: 102.64  E-value: 7.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLV-----APTTGAMRLAGAE-YAPHSRAHAEALGVRMVMQELNLVP 101
Cdd:cd03260   15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDiYDLDVDVLELRRRVGMVFQKPNPFP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 102 tLTVAENLfldRLPHR-FGVIDRRRLAADARAAMARVGL-----DSLDPDTLVGslgiGHQQMVEIARSLAGDCRVLILD 175
Cdd:cd03260   95 -GSIYDNV---AYGLRlHGIKLKEELDERVEEALRKAALwdevkDRLHALGLSG----GQQQRLCLARALANEPEVLLLD 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 176 EPTAML---TAREVELLfdqIARLKADgVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03260  167 EPTSALdpiSTAKIEEL---IAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
17-229 1.18e-24

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: 102.27  E-value: 1.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  17 VTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVR 91
Cdd:cd03258    4 LKNVSKVFGDtggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARRR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  92 --MVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGL-DSLD--PDTLVGslgiGHQQMVEIARSLA 166
Cdd:cd03258   84 igMIFQHFNLLSSRTVFENV---ALPLEIAGVPKAEIEERVLELLELVGLeDKADayPAQLSG----GQKQRVGIARALA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 167 GDCRVLILDEPTAML---TAREV-ELLFDQIARLkadGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03258  157 NNPKVLLCDEATSALdpeTTQSIlALLRDINREL---GLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
267-483 1.67e-24

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: 100.34  E-value: 1.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSRG----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHgIA 342
Cdd:cd03229    1 LELKNVSKRygqkTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRR-IG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDrkgeGLLLPQ-SIAANLSLGqlarvarggvvdgerenalaarqidalrirargpaqpvaeLSGGNQQKVAIGRWL 421
Cdd:cd03229   80 MVFQD----FALFPHlTVLENIALG----------------------------------------LSGGQQQRVALARAL 115
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 422 GRDMGVLLFDEPTRGIDVGAKFDIYALLDAL-AREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03229  116 AMDPDVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
14-231 1.86e-24

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: 102.03  E-value: 1.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  14 TLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYaphSRAHAEALGVRM 92
Cdd:cd03296    2 SIEVRNVSKRFGDfVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQERNVGF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  93 VMQELNLVPTLTVAENL-FLDRLPHRFGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGD 168
Cdd:cd03296   79 VFQHYALFRHMTVFDNVaFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLAdryPAQLSG----GQRQRVALARALAVE 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 169 CRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHV 231
Cdd:cd03296  155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQV 218
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
277-484 1.90e-24

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: 99.43  E-value: 1.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHGIALVSedrkgeglllp 356
Cdd:cd03216   15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--KEVSFASPRDARRAGIAMVY----------- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 qsiaanlslgqlarvarggvvdgerenalaarqidalrirargpaqpvaELSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:cd03216   82 -------------------------------------------------QLSVGERQMVEIARALARNARLLILDEPTAA 112
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 490656625 437 IDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03216  113 LTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
27-229 1.97e-24

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 102.12  E-value: 1.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRAHaealgVRMVM-QELNLVPT 102
Cdd:COG4559   15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplAAWSPWELAR-----RRAVLpQHSSLAFP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENLFLDRLPHRFGvidRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLA-------GDCRVL 172
Cdd:COG4559   90 FTVEEVVALGRAPHGSS---AAQDRQIVREALALVGLAHLagrSYQTLSG----GEQQRVQLARVLAqlwepvdGGPRWL 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 173 ILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG4559  163 FLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
267-483 2.31e-24

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: 100.97  E-value: 2.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSRG----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHGIA 342
Cdd:cd03224    1 LEVENLNAGygksQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG--RDITGLPPHERARAGIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDRKgeglLLPQ-SIAANLSLGqlARVARGGVVDGERENALAArqIDALRIRARgpaQPVAELSGGNQQKVAIGRWL 421
Cdd:cd03224   79 YVPEGRR----IFPElTVEENLLLG--AYARRRAKRKARLERVYEL--FPRLKERRK---QLAGTLSGGEQQMLAIARAL 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 422 GRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03224  148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
27-491 2.32e-24

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 106.33  E-value: 2.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGL-----VAPTTGAMRLAGaeyapHSRAHAEA---LGVR-----MV 93
Cdd:PRK15134  23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHG-----ESLLHASEqtlRGVRgnkiaMI 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 MQE--LNLVPTLTVAENLFLDRLPHRfgvidrrrlaADARAAMARVGLDSLD--------------PDTLVGslgiGHQQ 157
Cdd:PRK15134  98 FQEpmVSLNPLHTLEKQLYEVLSLHR----------GMRREAARGEILNCLDrvgirqaakrltdyPHQLSG----GERQ 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 158 MVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDA 236
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAAT 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 237 ---QP----TERLV-ALMAGREIAEQAvhgtrtPGAPRLRVERLS------RG---------DAVRDVSFDVRAGEIFGI 293
Cdd:PRK15134 244 lfsAPthpyTQKLLnSEPSGDPVPLPE------PASPLLDVEQLQvafpirKGilkrtvdhnVVVKNISFTLRPGETLGL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 294 SGLIGAGRT----ELLRLVygadaADGGTVSIGDPPRPAAIRSPADAVRHGIALVSEDrkgeglllPQSiAANLSLGQLA 369
Cdd:PRK15134 318 VGESGSGKSttglALLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQD--------PNS-SLNPRLNVLQ 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 370 RVARGGVVDGERENALA--ARQIDALR-------IRARGPaqpvAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVG 440
Cdd:PRK15134 384 IIEEGLRVHQPTLSAAQreQQVIAVMEevgldpeTRHRYP----AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT 459
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490656625 441 AKFDIYALLDALAREGR-AIVVVSSDLRELMLICDRIGVMSAGRmhaVFERG 491
Cdd:PRK15134 460 VQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGE---VVEQG 508
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
271-486 3.24e-24

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: 100.30  E-value: 3.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 271 RLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairSPADAVRHGIALVsedrkg 350
Cdd:cd03235    8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG--------KPLEKERKRIGYV------ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 351 eglllPQSIAAN----------LSLGQLARVARGGVVDGER----ENALAARQIDALRIRargpaqPVAELSGGNQQKVA 416
Cdd:cd03235   74 -----PQRRSIDrdfpisvrdvVLMGLYGHKGLFRRLSKADkakvDEALERVGLSELADR------QIGELSGGQQQRVL 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 417 IGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIgVMSAGRMHA 486
Cdd:cd03235  143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVA 211
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
277-484 3.51e-24

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: 100.43  E-value: 3.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRpaairspADAVRHGIALVSEDRkgeGLLLP 356
Cdd:cd03269   15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-------DIAARNRIGYLPEER---GLYPK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLS-LGQLARVARggvvdgeREnalAARQID----ALRIRARGpAQPVAELSGGNQQKVAIGRWLGRDMGVLLFD 431
Cdd:cd03269   85 MKVIDQLVyLAQLKGLKK-------EE---ARRRIDewleRLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490656625 432 EPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03269  154 EPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
266-486 4.21e-24

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: 101.27  E-value: 4.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 266 RLRVERLS----RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHgI 341
Cdd:COG1120    1 MLEAENLSvgygGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG--RDLASLSRRELARR-I 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 342 ALVsedrkgeglllPQSIAANLSLG-----QLARVARGGVVDGER-------ENALAARQIDALRIRargpaqPVAELSG 409
Cdd:COG1120   78 AYV-----------PQEPPAPFGLTvrelvALGRYPHLGLFGRPSaedreavEEALERTGLEHLADR------PVDELSG 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 410 GNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:COG1120  141 GERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
267-517 4.49e-24

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: 101.03  E-value: 4.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLS--------RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAAIRspadAV 337
Cdd:COG1124    2 LEVRNLSvsygqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdGRPVTRRRRK----AF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 338 RHGIALVSEDrkGEGLLLP-QSIAAnlSLGQLARVARGGVVDGERENALAARQIDAlRIRARGPAQpvaeLSGGNQQKVA 416
Cdd:COG1124   78 RRRVQMVFQD--PYASLHPrHTVDR--ILAEPLRIHGLPDREERIAELLEQVGLPP-SFLDRYPHQ----LSGGQRQRVA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 417 IGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHAVFERggwtq 495
Cdd:COG1124  149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTV----- 223
                        250       260
                 ....*....|....*....|....
gi 490656625 496 DALLGAAFAGYARR--DAALHPPG 517
Cdd:COG1124  224 ADLLAGPKHPYTREllAASLAFER 247
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
17-229 5.22e-24

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: 100.65  E-value: 5.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  17 VTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVRMVM- 94
Cdd:cd03261    3 LRGLTKSFGGrTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMl 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  95 -QELNLVPTLTVAEN--LFLdrlpHRFGVIDRRRLAADARAAMARVGL---DSLDPDTLVGslgiGHQQMVEIARSLAGD 168
Cdd:cd03261   83 fQSGALFDSLTVFENvaFPL----REHTRLSEEEIREIVLEKLEAVGLrgaEDLYPAELSG----GMKKRVALARALALD 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 169 CRVLILDEPTAML---TAREVELLfdqIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03261  155 PELLLYDEPTAGLdpiASGVIDDL---IRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
17-229 7.22e-24

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 100.47  E-value: 7.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  17 VTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL-----GV 90
Cdd:COG4161    5 LKNINCFYGShQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIrllrqKV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  91 RMVMQELNLVPTLTVAENLFldRLPHRFGVIDRRRLAADARAAMARVGL-DSLD--PDTLVGslgiGHQQMVEIARSLAG 167
Cdd:COG4161   85 GMVFQQYNLWPHLTVMENLI--EAPCKVLGLSKEQAREKAMKLLARLRLtDKADrfPLHLSG----GQQQRVAIARALMM 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 168 DCRVLILDEPTAML----TAREVELlfdqIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG4161  159 EPQVLLFDEPTAALdpeiTAQVVEI----IRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
15-229 9.07e-24

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: 99.36  E-value: 9.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAEP-----VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG 89
Cdd:cd03266    2 ITADALTKRFRDVkktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  90 VrmVMQELNLVPTLTVAENL-------------FLDRLPHRFGVIDRRRLAadaraamarvgldsldpDTLVGSLGIGHQ 156
Cdd:cd03266   82 F--VSDSTGLYDRLTARENLeyfaglyglkgdeLTARLEELADRLGMEELL-----------------DRRVGGFSTGMR 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 157 QMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03266  143 QKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
26-229 9.22e-24

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: 99.14  E-value: 9.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyaphsrAHAEALGVRM--VMQELNLVPT- 102
Cdd:cd03235   12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG--------KPLEKERKRIgyVPQRRSIDRDf 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 -LTVAENLFLDRLPH-RFGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAM 180
Cdd:cd03235   84 pISVRDVVLMGLYGHkGLFRRLSKADKAKVDEALERVGLSELA-DRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490656625 181 LTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLrDGRLV 229
Cdd:cd03235  163 VDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
26-227 1.48e-23

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 97.45  E-value: 1.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRAHAEALgvrmVMQELNLVPT 102
Cdd:cd03228   15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlRDLDLESLRKNIAY----VPQDPFLFSG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 lTVAENLfldrlphrfgvidrrrlaadaraamarvgldsldpdtlvgsLGIGHQQMVEIARSLAGDCRVLILDEPTAMLT 182
Cdd:cd03228   91 -TIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALD 128
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 490656625 183 AREVELLFDQIARLkADGVALVYISHRLEELARvAQRVAVLRDGR 227
Cdd:cd03228  129 PETEALILEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
277-489 1.81e-23

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: 98.70  E-value: 1.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRSPadavRHGIALVSEDrkgeGLLLP 356
Cdd:cd03293   19 ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP----VTGP----GPDRGYVFQQ----DALLP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 -QSIAANLSLGQLARvargGVVDGEREnALAARQIDALRIRARGPAQPvAELSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:cd03293   87 wLTVLDNVALGLELQ----GVPKAEAR-ERAEELLELVGLSGFENAYP-HQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 436 GIDVGAKFDIYA-LLDALAREGRAIVVVSSDLRELMLICDRIGVMSA--GRMHAVFE 489
Cdd:cd03293  161 ALDALTREQLQEeLLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVE 217
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
12-227 2.21e-23

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: 98.66  E-value: 2.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  12 TPTLVVTGIGKTY--------AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMR---------LAG 74
Cdd:COG4778    2 TTLLEVENLSKTFtlhlqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwvdLAQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  75 AEyaPHsrahaEALGVR-----MVMQELNLVPTLT----VAENLFLD------------RLPHRFGVIDRrrlaadaraa 133
Cdd:COG4778   82 AS--PR-----EILALRrrtigYVSQFLRVIPRVSaldvVAEPLLERgvdreearararELLARLNLPER---------- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 134 marvgLDSLDPDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEEL 213
Cdd:COG4778  145 -----LWDLPPATFSG----GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVR 215
                        250
                 ....*....|....
gi 490656625 214 ARVAQRVAVLRDGR 227
Cdd:COG4778  216 EAVADRVVDVTPFS 229
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
277-484 2.42e-23

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: 98.35  E-value: 2.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSEDrkgeglllP 356
Cdd:cd03257   20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRKEIQMVFQD--------P 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSiAAN--LSLG-QLARVARggVVDGERENALAARQIDALRIRARGPAQ-----PvAELSGGNQQKVAIGRWLGRDMGVL 428
Cdd:cd03257   92 MS-SLNprMTIGeQIAEPLR--IHGKLSKKEARKEAVLLLLVGVGLPEEvlnryP-HELSGGQRQRVAIARALALNPKLL 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 429 LFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03257  168 IADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
27-230 2.69e-23

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: 96.74  E-value: 2.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRAhaealgvrmvmQELNLVPTL 103
Cdd:cd03214   13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGkdlASLSPKELA-----------RKIAYVPQA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 tvaenlfLDRlphrfgvidrrrlaadaraamarVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAML-T 182
Cdd:cd03214   82 -------LEL-----------------------LGLAHLA-DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLdI 130
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490656625 183 AREVELLfDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:cd03214  131 AHQIELL-ELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
14-232 3.09e-23

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 100.99  E-value: 3.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  14 TLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphSRAHAEALGVRM 92
Cdd:COG1118    2 SIEVRNISKRFGSfTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF--TNLPPRERRVGF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  93 VMQELNLVPTLTVAENL--FLDRLPHRFGVIDrrrlaADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAG 167
Cdd:COG1118   80 VFQHYALFPHMTVAENIafGLRVRPPSKAEIR-----ARVEELLELVQLEGLAdryPSQLSG----GQRQRVALARALAV 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 168 DCRVLILDEPTAMLTA---REVELLFDQIarLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:COG1118  151 EPEVLLLDEPFGALDAkvrKELRRWLRRL--HDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVG 216
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
10-235 4.25e-23

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: 98.13  E-value: 4.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  10 PDTPTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL 88
Cdd:COG1127    1 MSEPMIEVRNLTKSFGDrVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  89 GVR--MVMQELNLVPTLTVAENLfldRLP-HRFGVIDRRRLAADARAAMARVGLDS---LDPDTLVGslgiGHQQMVEIA 162
Cdd:COG1127   81 RRRigMLFQGGALFDSLTVFENV---AFPlREHTDLSEAEIRELVLEKLELVGLPGaadKMPSELSG----GMRKRVALA 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 163 RSLAGDCRVLILDEPTAML---TAREVELLfdqIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVDRID 235
Cdd:COG1127  154 RALALDPEILLYDEPTAGLdpiTSAVIDEL---IRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPE 227
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
277-484 7.45e-23

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: 96.81  E-value: 7.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRSPADAVRHGIALVSEDRkgegLLLP 356
Cdd:cd03263   17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS----IRTDRKAARQSLGYCPQFD----ALFD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 Q-SIAANLSLgqLARVaRGGVVDGERENALAARQIDALRIRARGPAQpvaELSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:cd03263   89 ElTVREHLRF--YARL-KGLPKSEIKEEVELLLRVLGLTDKANKRAR---TLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490656625 436 GIDVGAKFDIYALLDALaREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03263  163 GLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
267-484 7.73e-23

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 96.42  E-value: 7.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSRGDAVR----DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAairSPADAVRHGIA 342
Cdd:COG4619    1 LELEGLSFRVGGKpilsPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA---MPPPEWRRQVA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEdrkgEGLLLPQSIAANLSLgqlARVARGGVVDGERENALAAR---QIDALrirargpAQPVAELSGGNQQKVAIGR 419
Cdd:COG4619   78 YVPQ----EPALWGGTVRDNLPF---PFQLRERKFDRERALELLERlglPPDIL-------DKPVERLSGGERQRLALIR 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 420 WLGRDMGVLLFDEPTRGIDVGAKFDIYALLDAL-AREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:COG4619  144 ALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
268-482 1.41e-22

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: 95.40  E-value: 1.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 268 RVERLSRG-----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRspadavRHGIA 342
Cdd:cd03226    1 RIENISFSykkgtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER------RKSIG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDRKGEglLLPQSIAANLSLGQLARVARGGVVdgerENALAARQIDALRIRargpaQPvAELSGGNQQKVAIGRWLG 422
Cdd:cd03226   75 YVMQDVDYQ--LFTDSVREELLLGLKELDAGNEQA----ETVLKDLDLYALKER-----HP-LSLSGGQKQRLAIAAALL 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 423 RDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAG 482
Cdd:cd03226  143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
15-228 2.22e-22

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: 95.69  E-value: 2.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE---YAPHSRAHaeaLGV 90
Cdd:cd03218    1 LRAENLSKRYGKrKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitkLPMHKRAR---LGI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  91 RMVMQELNLVPTLTVAENLFLdrlphrfgVIDRRRLAADARAAMARVGLDSLDPDTLVGSLGI----GHQQMVEIARSLA 166
Cdd:cd03218   78 GYLPQEASIFRKLTVEENILA--------VLEIRGLSKKEREEKLEELLEEFHITHLRKSKASslsgGERRRVEIARALA 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 167 GDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:cd03218  150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
28-247 2.24e-22

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 95.67  E-value: 2.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE---YAPHSRAHAealGVRMVMQELNLVPTLT 104
Cdd:TIGR03410  15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDitkLPPHERARA---GIAYVPQGREIFPRLT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  105 VAENLF--LDRLPHRFGVIDRRrlaadaraamarvgLDSLDP------DTLVGSLGIGHQQMVEIARSLAGDCRVLILDE 176
Cdd:TIGR03410  92 VEENLLtgLAALPRRSRKIPDE--------------IYELFPvlkemlGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625  177 PTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMA 247
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLA 229
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
2-229 2.67e-22

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: 100.23  E-value: 2.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   2 DSTDPDSTPDTPTLVVTGIGKTY---AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA 78
Cdd:COG4987  321 EPAEPAPAPGGPSLELEDVSFRYpgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR 400
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  79 PHSRAHAEALgVRMVMQELNLVPTlTVAENL-----------------------FLDRLPHrfgvidrrrlaadaraama 135
Cdd:COG4987  401 DLDEDDLRRR-IAVVPQRPHLFDT-TLRENLrlarpdatdeelwaalervglgdWLAALPD------------------- 459
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 136 rvGLDsldpdTLVGSLGI----GHQQMVEIARSLAGDCRVLILDEPTAML---TAREV-ELLFDQiarlkADGVALVYIS 207
Cdd:COG4987  460 --GLD-----TWLGEGGRrlsgGERRRLALARALLRDAPILLLDEPTEGLdaaTEQALlADLLEA-----LAGRTVLLIT 527
                        250       260
                 ....*....|....*....|..
gi 490656625 208 HRLEELARvAQRVAVLRDGRLV 229
Cdd:COG4987  528 HRLAGLER-MDRILVLEDGRIV 548
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
14-229 2.69e-22

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 97.10  E-value: 2.69e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  14 TLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAH----AEAL 88
Cdd:COG4152    1 MLELKGLTKRFGDkTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylPEER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  89 GvrmvmqelnLVPTLTVAENL-FLDRLpH----------------RFGVIDRRrlaadaraamarvgldsldpDTLVGSL 151
Cdd:COG4152   81 G---------LYPKMKVGEQLvYLARL-KglskaeakrradewleRLGLGDRA--------------------NKKVEEL 130
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 152 GIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG4152  131 SKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
2-229 3.30e-22

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: 100.22  E-value: 3.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   2 DSTDPDSTPDTPTLVVTGIGKTYAE--PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAP 79
Cdd:COG4988  324 AGTAPLPAAGPPSIELEDVSFSYPGgrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  80 HSRAHaealgvrmVMQELNLV---PTL---TVAENLfldrlphRFGVIDrrRLAADARAAMARVGLDSL------DPDTL 147
Cdd:COG4988  404 LDPAS--------WRRQIAWVpqnPYLfagTIRENL-------RLGRPD--ASDEELEAALEAAGLDEFvaalpdGLDTP 466
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 148 VGSLGI----GHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLkADGVALVYISHRLEELARvAQRVAVL 223
Cdd:COG4988  467 LGEGGRglsgGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQ-ADRILVL 544

                 ....*.
gi 490656625 224 RDGRLV 229
Cdd:COG4988  545 DDGRIV 550
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
256-483 3.73e-22

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: 96.17  E-value: 3.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 256 VHGTRTPGAPRLRVERLSRGD---------AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPR 326
Cdd:cd03294    9 IFGKNPQKAFKLLAKGKSKEEilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 327 PAAIRSPADAVR-HGIALVSEDRKgeglLLPQ-SIAANLSLG-QLArvargGVVDGEREnALAARQIDALRIRARGPAQP 403
Cdd:cd03294   89 AAMSRKELRELRrKKISMVFQSFA----LLPHrTVLENVAFGlEVQ-----GVPRAERE-ERAAEALELVGLEGWEHKYP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 404 vAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAG 482
Cdd:cd03294  159 -DELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDG 237

                 .
gi 490656625 483 R 483
Cdd:cd03294  238 R 238
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
27-229 3.87e-22

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 95.61  E-value: 3.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRAhaealGVRMVM-QELNLVPT 102
Cdd:PRK13548  16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrplADWSPAELA-----RRRAVLpQHSSLSFP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGslgiGHQQMVEIARSLA------GDCRVLILDE 176
Cdd:PRK13548  91 FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSG----GEQQRVQLARVLAqlwepdGPPRWLLLDE 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 177 PTAMLTAREVELLFdQIAR--LKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13548 167 PTSALDLAHQHHVL-RLARqlAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
277-483 4.98e-22

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: 92.69  E-value: 4.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPaaiRSPADAVRHGIALVsedrkgeglllP 356
Cdd:cd00267   14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA---KLPLEELRRRIGYV-----------P 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QsiaanlslgqlarvarggvvdgerenalaarqidalrirargpaqpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:cd00267   80 Q-------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 490656625 437 IDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd00267  111 LDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
38-232 5.12e-22

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: 94.28  E-value: 5.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  38 PGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEY---------APHSRahaealGVRMVMQELNLVPTLTVAEN 108
Cdd:cd03297   22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkinlPPQQR------KIGLVFQQYALFPHLNVREN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 109 L-----FLDRLPHRFGVidrrrlaadaRAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAM 180
Cdd:cd03297   96 LafglkRKRNREDRISV----------DELLDLLGLDHLLnryPAQLSG----GEKQRVALARALAAQPELLLLDEPFSA 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490656625 181 LTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:cd03297  162 LDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
240-479 6.15e-22

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


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 98.90  E-value: 6.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  240 ERLVALMAGREIAEQAVHGTRTPGAPRLRVERLS-----RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAA 314
Cdd:TIGR02857 295 EALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSvaypgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDP 374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  315 DGGTVSIGDPPRPAAirsPADAVRHGIALVSEdrkgEGLLLPQSIAANLslgqlaRVARGGVVDGERENALAARQID-AL 393
Cdd:TIGR02857 375 TEGSIAVNGVPLADA---DADSWRDQIAWVPQ----HPFLFAGTIAENI------RLARPDASDAEIREALERAGLDeFV 441
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  394 RIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAReGRAIVVVSSDLrEL 469
Cdd:TIGR02857 442 AALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRL-AL 519
                         250
                  ....*....|
gi 490656625  470 MLICDRIGVM 479
Cdd:TIGR02857 520 AALADRIVVL 529
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
22-228 1.05e-21

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: 93.24  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  22 KTYAE--PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYApHSRAHAEALGVR---MVMQE 96
Cdd:cd03292    8 KTYPNgtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS-DLRGRAIPYLRRkigVVFQD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  97 LNLVPTLTVAEN----LFLDRLPHRfgvidrrRLAADARAAMARVGLDSlDPDTLVGSLGIGHQQMVEIARSLAGDCRVL 172
Cdd:cd03292   87 FRLLPDRNVYENvafaLEVTGVPPR-------EIRKRVPAALELVGLSH-KHRALPAELSGGEQQRVAIARAIVNSPTIL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 173 ILDEPTAML---TAREVELLFDQIarlKADGVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:cd03292  159 IADEPTGNLdpdTTWEIMNLLKKI---NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
240-483 1.10e-21

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: 98.29  E-value: 1.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 240 ERLVALMAGREIAEQAVHGTRT-PGAPRLRVERLS-----RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADA 313
Cdd:COG4988  309 EKIFALLDAPEPAAPAGTAPLPaAGPPSIELEDVSfsypgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP 388
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 314 ADGGTVSIGDPPRPAAirsPADAVRHGIALVSEDrkgeGLLLPQSIAANLSLGqlarvaRGGVVDGERENALAARQIDAL 393
Cdd:COG4988  389 PYSGSILINGVDLSDL---DPASWRRQIAWVPQN----PYLFAGTIRENLRLG------RPDASDEELEAALEAAGLDEF 455
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 394 rIRA--RGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAReGRAIVVVSSDLr 467
Cdd:COG4988  456 -VAAlpDGLDTPLGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRL- 532
                        250
                 ....*....|....*.
gi 490656625 468 ELMLICDRIGVMSAGR 483
Cdd:COG4988  533 ALLAQADRILVLDDGR 548
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
277-491 1.32e-21

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: 93.41  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPP----RPAAIRspadAVRHGIALVSEdrkGEG 352
Cdd:cd03258   20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltllSGKELR----KARRRIGMIFQ---HFN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 353 LLLPQSIAANLSLG-QLARVARGGVvdGERENALaarqIDALRIRARGPAQPvAELSGGNQQKVAIGRWLGRDMGVLLFD 431
Cdd:cd03258   93 LLSSRTVFENVALPlEIAGVPKAEI--EERVLEL----LELVGLEDKADAYP-AQLSGGQKQRVGIARALANNPKVLLCD 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 432 EPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRmhaVFERG 491
Cdd:cd03258  166 EATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGE---VVEEG 223
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
264-483 1.44e-21

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: 93.51  E-value: 1.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 264 APRLRVERLS----RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRH 339
Cdd:COG0410    1 MPMLEVENLHagygGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG--EDITGLPPHRIARL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 340 GIALVSEDRKgeglLLPQ-SIAANLSLGQLARVARGGVvdgerenalaARQIDA-------LRIRARgpaQPVAELSGGN 411
Cdd:COG0410   79 GIGYVPEGRR----IFPSlTVEENLLLGAYARRDRAEV----------RADLERvyelfprLKERRR---QRAGTLSGGE 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 412 QQKVAIGRWLgrdMG---VLLFDEPTRG-----IDvgakfDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:COG0410  142 QQMLAIGRAL---MSrpkLLLLDEPSLGlapliVE-----EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
261-489 1.44e-21

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 94.00  E-value: 1.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 261 TPGAPRLRVERLSRG--------DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairS 332
Cdd:COG1116    2 SAAAPALELRGVSKRfptggggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG--------K 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 333 PADAVRHGIALV-SEDRkgeglLLP-QSIAANLSLGQLARvargGVVDGEREnALAARQIDALRIRARGPAQPvAELSGG 410
Cdd:COG1116   74 PVTGPGPDRGVVfQEPA-----LLPwLTVLDNVALGLELR----GVPKAERR-ERARELLELVGLAGFEDAYP-HQLSGG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 411 NQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYA-LLDALAREGRAIVVVSSDLRELMLICDRIGVMSA--GRMHAV 487
Cdd:COG1116  143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDeLLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222

                 ..
gi 490656625 488 FE 489
Cdd:COG1116  223 ID 224
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
33-258 1.46e-21

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 93.49  E-value: 1.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  33 SLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEY---APHSRAhaealgVRMVMQELNLVPTLTVAENL 109
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHtttPPSRRP------VSMLFQENNLFSHLTVAQNI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 110 FLDRLPhrfGVIDRRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTA---REV 186
Cdd:PRK10771  93 GLGLNP---GLKLNAAQREKLHAIARQMGIEDL-LARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPalrQEM 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 187 ELLFDQIARLKadGVALVYISHRLEELARVAQRVAVLRDGRLVHvdriDAqPTERLVAlmagREIAEQAVHG 258
Cdd:PRK10771 169 LTLVSQVCQER--QLTLLMVSHSLEDAARIAPRSLVVADGRIAW----DG-PTDELLS----GKASASALLG 229
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
267-489 1.56e-21

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: 93.40  E-value: 1.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSRG-----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGI 341
Cdd:cd03256    1 IEVENLSKTypngkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 342 ALVSEDRkgeGLLLPQSIAANLSLGQLA-----RVARGGVVDGERENALAARQIDALRIRARgpaQPVAELSGGNQQKVA 416
Cdd:cd03256   81 GMIFQQF---NLIERLSVLENVLSGRLGrrstwRSLFGLFPKEEKQRALAALERVGLLDKAY---QRADQLSGGQQQRVA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 417 IGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMhaVFE 489
Cdd:cd03256  155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRI--VFD 226
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
31-229 1.67e-21

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: 92.56  E-value: 1.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  31 DVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA---PHSRAhaealgVRMVMQELNLVPTLTVAE 107
Cdd:cd03298   16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTaapPADRP------VSMLFQENNLFAHLTVEQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NLFLDRLPhrfGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAML-TA 183
Cdd:cd03298   90 NVGLGLSP---GLKLTAEDRQAIEVALARVGLAGLEkrlPGELSG----GERQRVALARVLVRDKPVLLLDEPFAALdPA 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 490656625 184 REVELLfDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03298  163 LRAEML-DLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
12-248 1.88e-21

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 96.06  E-value: 1.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  12 TPTLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA---PHSRAhaea 87
Cdd:PRK11607  17 TPLLEIRNLTKSFdGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLShvpPYQRP---- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  88 lgVRMVMQELNLVPTLTVAEN----LFLDRLPHrfGVIDRRRLAADARAAMARVGldSLDPDTLVGslgiGHQQMVEIAR 163
Cdd:PRK11607  93 --INMMFQSYALFPHMTVEQNiafgLKQDKLPK--AEIASRVNEMLGLVHMQEFA--KRKPHQLSG----GQRQRVALAR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 164 SLAGDCRVLILDEPTAMLTAR-----EVELLfDQIARLkadGVALVYISHRLEELARVAQRVAVLRDGRLVHV---DRID 235
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKlrdrmQLEVV-DILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIgepEEIY 238
                        250
                 ....*....|...
gi 490656625 236 AQPTERLVALMAG 248
Cdd:PRK11607 239 EHPTTRYSAEFIG 251
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
33-244 1.90e-21

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 92.90  E-value: 1.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  33 SLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRahaealGVRMVMQELNLVPTLTVAENL 109
Cdd:COG3840   19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdlTALPPAER------PVSMLFQENNLFPHLTVAQNI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 110 FLDRLPH-RFGVIDrrrlAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTA------ 179
Cdd:COG3840   93 GLGLRPGlKLTAEQ----RAQVEQALERVGLAGLLdrlPGQLSG----GQRQRVALARCLVRKRPILLLDEPFSaldpal 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 180 ---MLTarevelLFDQIARlkADGVALVYISHRLEELARVAQRVAVLRDGRlVHVDridaQPTERLVA 244
Cdd:COG3840  165 rqeMLD------LVDELCR--ERGLTVLMVTHDPEDAARIADRVLLVADGR-IAAD----GPTAALLD 219
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
21-229 2.47e-21

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 93.60  E-value: 2.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  21 GKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL--GVRMVMQE-L 97
Cdd:PRK10419  20 GKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFrrDIQMVFQDsI 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  98 NLV-PTLTVAENLfldRLPHR-FGVIDRRRLAADARAAMARVGLDSLDPDTLVGSLGIGHQQMVEIARSLAGDCRVLILD 175
Cdd:PRK10419 100 SAVnPRKTVREII---REPLRhLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 176 EPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
26-229 2.66e-21

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 97.16  E-value: 2.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHS-RAHaealgVRMVMQElnlvP 101
Cdd:COG1132  353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRDLTLESlRRQ-----IGVVPQD----T 423
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 102 TL---TVAENL-----------------------FLDRLPHrfgvidrrrlaadaraamarvGLdsldpDTLVGSLGI-- 153
Cdd:COG1132  424 FLfsgTIRENIrygrpdatdeeveeaakaaqaheFIEALPD---------------------GY-----DTVVGERGVnl 477
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 154 --GHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVyISHRLeELARVAQRVAVLRDGRLV 229
Cdd:COG1132  478 sgGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIV-IAHRL-STIRNADRILVLDDGRIV 553
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
12-227 2.93e-21

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 94.49  E-value: 2.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  12 TPTLVVTGIGKTYAEP-VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaEYAPhSRAHAEALGV 90
Cdd:PRK13537   5 VAPIDFRNVEKRYGDKlVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVP-SRARHARQRV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  91 RMVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSlDPDTLVGSLGIGHQQMVEIARSLAGDCR 170
Cdd:PRK13537  83 GVVPQFDNLDPDFTVRENL---LVFGRYFGLSAAAARALVPPLLEFAKLEN-KADAKVGELSGGMKRRLTLARALVNDPD 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 171 VLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
17-227 2.98e-21

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 94.90  E-value: 2.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  17 VTGIGKTYA-EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVrmVMQ 95
Cdd:PRK13536  44 LAGVSKSYGdKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGV--VPQ 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  96 ELNLVPTLTVAENLFLdrlphrFGVIDRRRLAADARAAMARVGLDSLD--PDTLVGSLGIGHQQMVEIARSLAGDCRVLI 173
Cdd:PRK13536 122 FDNLDLEFTVRENLLV------FGRYFGMSTREIEAVIPSLLEFARLEskADARVSDLSGGMKRRLTLARALINDPQLLI 195
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490656625 174 LDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
154-484 4.24e-21

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: 96.41  E-value: 4.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  154 GHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQI-ARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVd 232
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEE- 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  233 ridAQPTERLVALMAGREIAEQAVHGTRtpGAPRLRVERLS-------RG--DAVRDVSFDVRAGEIFGISGLIGAGRTE 303
Cdd:TIGR03269 251 ---GTPDEVVAVFMEGVSEVEKECEVEV--GEPIIKVRNVSkryisvdRGvvKAVDNVSLEVKEGEIFGIVGTSGAGKTT 325
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  304 LLRLVYGADAADGGT--VSIGDpprpaairSPADAVRHGIALVSEDRKGEGLLLPQ-------SIAANL--SLG-----Q 367
Cdd:TIGR03269 326 LSKIIAGVLEPTSGEvnVRVGD--------EWVDMTKPGPDGRGRAKRYIGILHQEydlyphrTVLDNLteAIGlelpdE 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  368 LARvaRGGVVdgerenALAARQIDALRIRARGPAQPvAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDI-Y 446
Cdd:TIGR03269 398 LAR--MKAVI------TLKMVGFDEEKAEEILDKYP-DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVtH 468
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 490656625  447 ALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:TIGR03269 469 SILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
277-483 4.28e-21

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: 91.37  E-value: 4.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHgIALVSEDrkgeglllP 356
Cdd:cd03225   16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDG--KDLTKLSLKELRRK-VGLVFQN--------P 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QS----------IA---ANLSLGQLARVARggvvdgeRENALAARQIDALRIRargpaqPVAELSGGNQQKVAIGRWLGR 423
Cdd:cd03225   85 DDqffgptveeeVAfglENLGLPEEEIEER-------VEEALELVGLEGLRDR------SPFTLSGGQKQRVAIAGVLAM 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 424 DMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03225  152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
277-483 5.47e-21

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: 91.16  E-value: 5.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADavrHGIALVSEDRKgeglLLP 356
Cdd:cd03301   15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG--RDVTDLPPKD---RDIAMVFQNYA----LYP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 Q-SIAANLSLGQLARVARGGVVDGERENALAARQIDALRirARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:cd03301   86 HmTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLL--DRKPKQ----LSGGQRQRVALGRAIVREPKVFLMDEPLS 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490656625 436 GIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03301  160 NLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
27-229 5.78e-21

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: 93.58  E-value: 5.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAP---TTGAMRLAGAEYAPHSRAHAEALGVR---MVMQE---- 96
Cdd:COG0444   19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIRGReiqMIFQDpmts 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  97 LNlvPTLTV----AENLfldrlpHRFGVIDRRRLAADARAAMARVGLDslDPDTLVGS----LGIGHQQMVEIARSLAGD 168
Cdd:COG0444   99 LN--PVMTVgdqiAEPL------RIHGGLSKAEARERAIELLERVGLP--DPERRLDRypheLSGGMRQRVMIARALALE 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 169 CRVLILDEPTAML---TAREV-ELLfdqiARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG0444  169 PKLLIADEPTTALdvtIQAQIlNLL----KDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
27-230 6.27e-21

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: 92.07  E-value: 6.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGA-MRLAGAEYAPHS----RAHaeaLG-VRMVMQElNLV 100
Cdd:COG1119   17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDvwelRKR---IGlVSPALQL-RFP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 101 PTLTVAENLfldrLPHRFGVIDRRRLAADARAAM-----ARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILD 175
Cdd:COG1119   93 RDETVLDVV----LSGFFDSIGLYREPTDEQRERarellELLGLAHLA-DRPFGTLSQGEQRRVLIARALVKDPELLILD 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 176 EPTAMLTAREVELLFDQIARLKADG-VALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:COG1119  168 EPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
17-228 8.04e-21

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: 90.67  E-value: 8.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  17 VTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYaPHSRAHAEAL--GVRMV 93
Cdd:cd03262    3 IKNLHKSFGDfHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELrqKVGMV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 MQELNLVPTLTVAENLFLDrlPHRFGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDCR 170
Cdd:cd03262   82 FQQFNLFPHLTVLENITLA--PIKVKGMSKAEAEERALELLEKVGLADKAdayPAQLSG----GQQQRVAIARALAMNPK 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 171 VLILDEPTAML---TAREVEllfDQIARLKADGVALVYISHRLeELAR-VAQRVAVLRDGRL 228
Cdd:cd03262  156 VMLFDEPTSALdpeLVGEVL---DVMKDLAEEGMTMVVVTHEM-GFAReVADRVIFMDDGRI 213
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
14-232 9.60e-21

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 93.60  E-value: 9.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  14 TLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRahaealG 89
Cdd:COG3839    3 SLELENVSKSYgGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvTDLPPKDR------N 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  90 VRMVMQELNLVPTLTVAENL-FldrlPHRFGVIDRRRLAADARAAMARVGLDS-LD--PDTLVGslgiGHQQMVEIARSL 165
Cdd:COG3839   77 IAMVFQSYALYPHMTVYENIaF----PLKLRKVPKAEIDRRVREAAELLGLEDlLDrkPKQLSG----GQRQRVALGRAL 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 166 AGDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:COG3839  149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVG 216
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
27-229 1.21e-20

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 90.34  E-value: 1.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAlGVRMVMQELNLVPTlTVA 106
Cdd:cd03245   18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-NIGYVPQDVTLFYG-TLR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 107 ENLFLDRLPHrfgvidrrrLAADARAAMARVGLDSL---DP---DTLVG----SLGIGHQQMVEIARSLAGDCRVLILDE 176
Cdd:cd03245   96 DNITLGAPLA---------DDERILRAAELAGVTDFvnkHPnglDLQIGergrGLSGGQRQAVALARALLNDPPILLLDE 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490656625 177 PTAMLTAREVELLFDQIARLKADgVALVYISHRLEELArVAQRVAVLRDGRLV 229
Cdd:cd03245  167 PTSAMDMNSEERLKERLRQLLGD-KTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
31-232 1.59e-20

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: 91.17  E-value: 1.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  31 DVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAhaEALGVR-----MVMQELNLVPTLTV 105
Cdd:cd03294   42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRK--ELRELRrkkisMVFQSFALLPHRTV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLfldrlphRFGV----IDRRRLAADARAAMARVGLDSlDPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEP-TAM 180
Cdd:cd03294  120 LENV-------AFGLevqgVPRAEREERAAEALELVGLEG-WEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAfSAL 191
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 181 --LTAREVEllfDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:cd03294  192 dpLIRREMQ---DELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
267-483 2.45e-20

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: 89.99  E-value: 2.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaiRSPADAVRHGIA 342
Cdd:cd03300    1 IELENVSKfyGGfvALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD-----ITNLPPHKRPVN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDRKgeglLLPQ-SIAANLSLG-QLARVARGGVvdgERENALAARQIDALRIRARGPAQpvaeLSGGNQQKVAIGRW 420
Cdd:cd03300   76 TVFQNYA----LFPHlTVFENIAFGlRLKKLPKAEI---KERVAEALDLVQLEGYANRKPSQ----LSGGQQQRVAIARA 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 421 LGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03300  145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGK 208
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
15-229 4.65e-20

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 89.28  E-value: 4.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEalgVR-- 91
Cdd:COG1126    2 IEIENLHKSFgDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINK---LRrk 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  92 --MVMQELNLVPTLTVAENL---------------------FLDRlphrfgvidrrrlaadaraamarVGL-DSLD--PD 145
Cdd:COG1126   79 vgMVFQQFNLFPHLTVLENVtlapikvkkmskaeaeerameLLER-----------------------VGLaDKADayPA 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 146 TLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAML---TAREVEllfDQIARLKADGVALVYISHrleEL--AR-VAQR 219
Cdd:COG1126  136 QLSG----GQQQRVAIARALAMEPKVMLFDEPTSALdpeLVGEVL---DVMRDLAKEGMTMVVVTH---EMgfAReVADR 205
                        250
                 ....*....|
gi 490656625 220 VAVLRDGRLV 229
Cdd:COG1126  206 VVFMDGGRIV 215
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
27-230 5.54e-20

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: 93.27  E-value: 5.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRahaEALGvRMV---MQELNLVPTl 103
Cdd:COG4618  346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR---EELG-RHIgylPQDVELFDG- 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENL--FLD--------------------RLPHRFgvidrrrlaadaraamarvgldsldpDTLVGSLGI----GHQQ 157
Cdd:COG4618  421 TIAENIarFGDadpekvvaaaklagvhemilRLPDGY--------------------------DTRIGEGGArlsgGQRQ 474
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 158 MVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELArVAQRVAVLRDGRLVH 230
Cdd:COG4618  475 RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRVQA 546
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
240-483 5.88e-20

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 93.29  E-value: 5.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 240 ERLVALMAGREIAEQAVHGTRTPGAPRLRVERLS------RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADA 313
Cdd:COG4987  307 RRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSfrypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 314 ADGGTVSIGDPPrpaaIRS-PADAVRHGIALVSEDrkgeGLLLPQSIAANLslgqlaRVARGGVVDGERENALAARQIDA 392
Cdd:COG4987  387 PQSGSITLGGVD----LRDlDEDDLRRRIAVVPQR----PHLFDTTLRENL------RLARPDATDEELWAALERVGLGD 452
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 393 LrIRA--RGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAReGRAIVVVSSDL 466
Cdd:COG4987  453 W-LAAlpDGLDTWLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRL 530
                        250
                 ....*....|....*..
gi 490656625 467 RELMLiCDRIGVMSAGR 483
Cdd:COG4987  531 AGLER-MDRILVLEDGR 546
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
25-229 7.40e-20

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 89.69  E-value: 7.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  25 AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHS----RAHaealgVRMVMQ----- 95
Cdd:PRK13635  19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdvRRQ-----VGMVFQnpdnq 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  96 --------------ELNLVPTLTVAENL-----------FLDRLPHRfgvidrrrlaadaraamarvgldsldpdtlvgs 150
Cdd:PRK13635  94 fvgatvqddvafglENIGVPREEMVERVdqalrqvgmedFLNREPHR--------------------------------- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 151 LGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARvAQRVAVLRDGRLV 229
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
15-232 7.99e-20

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: 88.08  E-value: 7.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRahaealGV 90
Cdd:cd03301    1 VELENVTKRFGNvTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvTDLPPKDR------DI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  91 RMVMQELNLVPTLTVAEN----LFLDRLPHRfgVIDRRRLAADARAAMARVgLDSLdPDTLVGslgiGHQQMVEIARSLA 166
Cdd:cd03301   75 AMVFQNYALYPHMTVYDNiafgLKLRKVPKD--EIDERVREVAELLQIEHL-LDRK-PKQLSG----GQRQRVALGRAIV 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 167 GDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:cd03301  147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
277-486 9.91e-20

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: 88.16  E-value: 9.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRH-GI-----------ALV 344
Cdd:COG1122   16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDG--KDITKKNLRELRRKvGLvfqnpddqlfaPTV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 345 SEDrkgeglllpqsIA---ANLSLGQ---LARVarggvvdgerENALAARQIDALRirargpAQPVAELSGGNQQKVAIG 418
Cdd:COG1122   94 EED-----------VAfgpENLGLPReeiRERV----------EEALELVGLEHLA------DRPPHELSGGQKQRVAIA 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 419 RWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:COG1122  147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
15-232 1.39e-19

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: 87.43  E-value: 1.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAEPV-LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVrmV 93
Cdd:cd03265    1 IEVENLVKKYGDFEaVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGI--V 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 MQELNLVPTLTVAENLFLD-RLphrFGVidrRRLAADARAAMARVGLDSLD-PDTLVGSLGIGHQQMVEIARSLAGDCRV 171
Cdd:cd03265   79 FQDLSVDDELTGWENLYIHaRL---YGV---PGAERRERIDELLDFVGLLEaADRLVKTYSGGMRRRLEIARSLVHRPEV 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 172 LILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:cd03265  153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
265-469 1.97e-19

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 86.76  E-value: 1.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLS--RGDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRSPADAVRHG 340
Cdd:COG4133    1 MMLEAENLScrRGERLlfSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP----IRDAREDYRRR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 341 IALVSEDrkgEGLLLPQSIAANLslgQLARVARGGVVDGERENALaarqIDALRIRARGpAQPVAELSGGNQQKVAIGRW 420
Cdd:COG4133   77 LAYLGHA---DGLKPELTVRENL---RFWAALYGLRADREAIDEA----LEAVGLAGLA-DLPVRQLSAGQKRRVALARL 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490656625 421 LGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLREL 469
Cdd:COG4133  146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLEL 194
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
31-229 2.30e-19

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: 89.39  E-value: 2.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  31 DVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGA----EYAPHSR-AHAEALGvrMVMQELNLVPTLTV 105
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLpPHRRRIG--YVFQEARLFPHLSV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLfldrlphRFGVidrrrlaadaraAMARVGLDSLDPDTLVGSLGIGH-------------QQMVEIARSLAGDCRVL 172
Cdd:COG4148   95 RGNL-------LYGR------------KRAPRAERRISFDEVVELLGIGHlldrrpatlsggeRQRVAIGRALLSSPRLL 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 173 ILDEPTAML-TAREVELLfDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG4148  156 LMDEPLAALdLARKAEIL-PYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
17-229 2.58e-19

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 87.38  E-value: 2.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  17 VTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL-----GV 90
Cdd:PRK11124   5 LNGINCFYgAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIrelrrNV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  91 RMVMQELNLVPTLTVAENLFldRLPHRFGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAG 167
Cdd:PRK11124  85 GMVFQQYNLWPHLTVQQNLI--EAPCRVLGLSKDQALARAEKLLERLRLKPYAdrfPLHLSG----GQQQRVAIARALMM 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 168 DCRVLILDEPTAML----TAREVELlfdqIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK11124 159 EPQVLLFDEPTAALdpeiTAQIVSI----IRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
9-223 5.32e-19

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: 90.04  E-value: 5.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625    9 TPDTPTLVVTGIGKTY--AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAE 86
Cdd:TIGR02857 316 AAPASSLEFSGVSVAYpgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWR 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   87 AlGVRMVMQELNLVPTlTVAENLFLDRlphrfgvidRRRLAADARAAMARVGLDSLDP------DTLVGS----LGIGHQ 156
Cdd:TIGR02857 396 D-QIAWVPQHPFLFAG-TIAENIRLAR---------PDASDAEIREALERAGLDEFVAalpqglDTPIGEggagLSGGQA 464
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625  157 QMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLkADGVALVYISHRLeELARVAQRVAVL 223
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRL-ALAALADRIVVL 529
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
276-484 6.38e-19

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 85.33  E-value: 6.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIR--SPADaVRHGIALVSEDrkgeGL 353
Cdd:cd03245   18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTD----IRqlDPAD-LRRNIGYVPQD----VT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 LLPQSIAANLSLG-------QLARVARGGVVDgerenALAARQID--ALRIRARGpaqpvAELSGGNQQKVAIGRWLGRD 424
Cdd:cd03245   89 LFYGTLRDNITLGapladdeRILRAAELAGVT-----DFVNKHPNglDLQIGERG-----RGLSGGQRQAVALARALLND 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 425 MGVLLFDEPTRGIDVGAKFDIYALLDALAReGRAIVVVSSDLRELMLiCDRIGVMSAGRM 484
Cdd:cd03245  159 PPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLLDL-VDRIIVMDSGRI 216
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
278-483 8.70e-19

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 87.58  E-value: 8.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRspadAVRHGIALVSEdrkGEGLLLPQ 357
Cdd:PRK13536  57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR----LARARIGVVPQ---FDNLDLEF 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 SIAANLslgqlarvarggVVDGeRENALAARQIDAL--------RIRARGPAqPVAELSGGNQQKVAIGRWLGRDMGVLL 429
Cdd:PRK13536 130 TVRENL------------LVFG-RYFGMSTREIEAVipsllefaRLESKADA-RVSDLSGGMKRRLTLARALINDPQLLI 195
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490656625 430 FDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
29-241 9.55e-19

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: 85.21  E-value: 9.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphsrahaEALGVRMVM-QELNLVPTLTVAE 107
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-------EPGPDRMVVfQNYSLLPWLTVRE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  108 NLFL--DR-LPHRfgviDRRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAR 184
Cdd:TIGR01184  74 NIALavDRvLPDL----SKSERRAIVEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625  185 EVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTER 241
Cdd:TIGR01184 149 TRGNLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVPFPR 206
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
19-465 9.80e-19

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: 89.22  E-value: 9.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   19 GIGKTYA--EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLagaeyaphsrahAEALGVRMVMQE 96
Cdd:TIGR03719   9 RVSKVVPpkKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP------------QPGIKVGYLPQE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   97 LNLVPTLTVAENLF------------LDRLPHRFGVIDRRRLAADARAAMARVGLDSLD-------------------PD 145
Cdd:TIGR03719  77 PQLDPTKTVRENVEegvaeikdaldrFNEISAKYAEPDADFDKLAAEQAELQEIIDAADawdldsqleiamdalrcppWD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  146 TLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAdgvALVYISHRLEELARVAQRVAVLRD 225
Cdd:TIGR03719 157 ADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTHDRYFLDNVAGWILELDR 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  226 GRLV------------HVDRI---DAQPTERLVALMAGREIAEQAVHGTRT----------------------------P 262
Cdd:TIGR03719 234 GRGIpwegnysswleqKQKRLeqeEKEESARQKTLKRELEWVRQSPKGRQAkskarlaryeellsqefqkrnetaeiyiP 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  263 GAPRL-----RVERLSR--GDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGdpprpaairsp 333
Cdd:TIGR03719 314 PGPRLgdkviEAENLTKafGDKLliDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----------- 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  334 aDAVRhgIALVSEDRKGeglllpqsIAANLSLGQLarvarggVVDGERENALAARQIDAlriRA-------RGPAQ--PV 404
Cdd:TIGR03719 383 -ETVK--LAYVDQSRDA--------LDPNKTVWEE-------ISGGLDIIKLGKREIPS---RAyvgrfnfKGSDQqkKV 441
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625  405 AELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAkfdIYALLDALAREGRAIVVVSSD 465
Cdd:TIGR03719 442 GQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET---LRALEEALLNFAGCAVVISHD 499
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
15-230 1.07e-18

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: 84.55  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAEP-VLDDVSLALYPGeALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGvrMV 93
Cdd:cd03264    1 LQLENLTKRYGKKrALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIG--YL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 MQELNLVPTLTVAEnlFLDRLPhRFGVIDRRRLAADARAAMARVGL-DSLdpDTLVGSLGIGHQQMVEIARSLAGDCRVL 172
Cdd:cd03264   78 PQEFGVYPNFTVRE--FLDYIA-WLKGIPSKEVKARVDEVLELVNLgDRA--KKKIGSLSGGMRRRVGIAQALVGDPSIL 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 173 ILDEPTAMLTAREVELLFDQIARLKADGVALVYiSHRLEELARVAQRVAVLRDGRLVH 230
Cdd:cd03264  153 IVDEPTAGLDPEERIRFRNLLSELGEDRIVILS-THIVEDVESLCNQVAVLNKGKLVF 209
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
8-229 1.11e-18

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 87.09  E-value: 1.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   8 STPDTPTLVVTGIGKTYaePV--------------LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLA 73
Cdd:COG4608    1 AAMAEPLLEVRDLKKHF--PVrgglfgrtvgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  74 GAEYAPHSRAHAEAL--GVRMVMQE----LNlvPTLTVAENLfldRLPHR-FGVIDRRRLAADARAAMARVGLDSLD--- 143
Cdd:COG4608   79 GQDITGLSGRELRPLrrRMQMVFQDpyasLN--PRMTVGDII---AEPLRiHGLASKAERRERVAELLELVGLRPEHadr 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 144 -PDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAML----TAREVELLFDQIARLkadGVALVYISHRLEELARVAQ 218
Cdd:COG4608  154 yPHEFSG----GQRQRIGIARALALNPKLIVCDEPVSALdvsiQAQVLNLLEDLQDEL---GLTYLFISHDLSVVRHISD 226
                        250
                 ....*....|.
gi 490656625 219 RVAVLRDGRLV 229
Cdd:COG4608  227 RVAVMYLGKIV 237
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
267-484 1.26e-18

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 86.32  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAairspadaVRHGI 341
Cdd:COG4152    2 LELKGLTKrfGDktAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEPLDPE--------DRRRI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 342 ALVSEDRkgeGLLLPQSIAANLS-LGQLARVARggvvdgerenALAARQIDA----LRIRARGpAQPVAELSGGNQQKVA 416
Cdd:COG4152   74 GYLPEER---GLYPKMKVGEQLVyLARLKGLSK----------AEAKRRADEwlerLGLGDRA-NKKVEELSKGNQQKVQ 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 417 IGRWLGRDMGVLLFDEPTRGID-VGAKFdIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:COG4152  140 LIAALLHDPELLILDEPFSGLDpVNVEL-LKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
25-230 1.58e-18

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 85.07  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  25 AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphsrahaeALGVRMVMQELNLVPT-- 102
Cdd:PRK11231  14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS--------MLSSRQLARRLALLPQhh 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 -----LTVAENLFLDRLPH-----RFGVIDrrrlAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVL 172
Cdd:PRK11231  86 ltpegITVRELVAYGRSPWlslwgRLSAED----NARVNQAMEQTRINHL-ADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 173 ILDEPTAML-TAREVELLfDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:PRK11231 161 LLDEPTTYLdINHQVELM-RLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA 218
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
201-484 1.61e-18

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: 89.12  E-value: 1.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 201 VALVYISHRLeeLARVAQRVAVLRDGR--LVHVDRID---AQPTERlvalmagreiAEQAVHGTRTPGAPRLRVERLS-- 273
Cdd:COG2274  415 IAFNILSGRF--LAPVAQLIGLLQRFQdaKIALERLDdilDLPPER----------EEGRSKLSLPRLKGDIELENVSfr 482
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 274 ----RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpAAIRS-PADAVRHGIALVSEDr 348
Cdd:COG2274  483 ypgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG----IDLRQiDPASLRRQIGVVLQD- 557
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 349 kgeGLLLPQSIAANLSLG-------QLARVARggvvdgereNALAARQIDAL------RIRARGpaqpvAELSGGNQQKV 415
Cdd:COG2274  558 ---VFLFSGTIRENITLGdpdatdeEIIEAAR---------LAGLHDFIEALpmgydtVVGEGG-----SNLSGGQRQRL 620
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 416 AIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAReGRAIVVVSSDLrELMLICDRIGVMSAGRM 484
Cdd:COG2274  621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLDKGRI 687
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
266-484 1.70e-18

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 87.05  E-value: 1.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 266 RLRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADavRhGI 341
Cdd:COG3839    3 SLELENVSKsyGGveALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG--RDVTDLPPKD--R-NI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 342 ALVsedrkgeglllPQSIA--------ANLSLG-QLARVARGgvvdgERE----NALAARQIDALRirARGPAQpvaeLS 408
Cdd:COG3839   78 AMV-----------FQSYAlyphmtvyENIAFPlKLRKVPKA-----EIDrrvrEAAELLGLEDLL--DRKPKQ----LS 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 409 GGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVV-VSSDLRELMLICDRIGVMSAGRM 484
Cdd:COG3839  136 GGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIyVTHDQVEAMTLADRIAVMNDGRI 212
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
13-228 1.71e-18

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 87.59  E-value: 1.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  13 PTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyAPHSRAHAEALGVR 91
Cdd:PRK09536   2 PMIDVSDLSVEFGDtTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG---DDVEALSARAASRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  92 M--VMQELNLVPTLTVAENLFLDRLPH--RFGVIDrRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAG 167
Cdd:PRK09536  79 VasVPQDTSLSFEFDVRQVVEMGRTPHrsRFDTWT-ETDRAAVERAMERTGVAQF-ADRPVTSLSGGERQRVLLARALAQ 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
277-483 2.37e-18

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 83.69  E-value: 2.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIG-------DPPRPAAIRspadavRHGIALVSEDrk 349
Cdd:cd03255   19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisklSEKELAAFR------RRHIGFVFQS-- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 350 geGLLLP-QSIAANLSLGQLARvargGVVDGEREnALAARQIDALRIRARgPAQPVAELSGGNQQKVAIGRWLGRDMGVL 428
Cdd:cd03255   91 --FNLLPdLTALENVELPLLLA----GVPKKERR-ERAEELLERVGLGDR-LNHYPSELSGGQQQRVAIARALANDPKII 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 429 LFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDlRELMLICDRIGVMSAGR 483
Cdd:cd03255  163 LADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGK 217
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
280-483 3.33e-18

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: 83.11  E-value: 3.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 280 DVSFDVRaGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairSPADAVRHGIALVSEDRKgEGLLLPQ-- 357
Cdd:cd03297   16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG--------TVLFDSRKKINLPPQQRK-IGLVFQQya 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 -----SIAANLSLGqLARVARGgvVDGERENALAAR-QIDALRIRargpaqPVAELSGGNQQKVAIGRWLGRDMGVLLFD 431
Cdd:cd03297   86 lfphlNVRENLAFG-LKRKRNR--EDRISVDELLDLlGLDHLLNR------YPAQLSGGEKQRVALARALAAQPELLLLD 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490656625 432 EPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03297  157 EPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
11-230 4.36e-18

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 83.33  E-value: 4.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  11 DTPTLVVTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHA 85
Cdd:PRK11629   2 NKILLQCDNLCKRYQEgsvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  86 EALGVR---MVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMV 159
Cdd:PRK11629  82 AELRNQklgFIYQFHHLLPDFTALENV---AMPLLIGKKKPAEINSRALEMLAAVGLEHRAnhrPSELSG----GERQRV 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 160 EIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLeELARVAQRVAVLRDGRLVH 230
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLTA 225
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
17-243 4.56e-18

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 85.52  E-value: 4.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  17 VTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYaphSRAHAEALGVRMVMQ 95
Cdd:PRK10851   5 IANIKKSFGRtQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDRKVGFVFQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  96 ELNLVPTLTVAENL-F-LDRLPHRfGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDCR 170
Cdd:PRK10851  82 HYALFRHMTVFDNIaFgLTVLPRR-ERPNAAAIKAKVTQLLEMVQLAHLAdryPAQLSG----GQKQRVALARALAVEPQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 171 VLILDEPTAMLTA---REVELLFDQI-ARLKADGvalVYISHRLEELARVAQRVAVLRDGRLVHV---DRIDAQPTERLV 243
Cdd:PRK10851 157 ILLLDEPFGALDAqvrKELRRWLRQLhEELKFTS---VFVTHDQEEAMEVADRVVVMSQGNIEQAgtpDQVWREPATRFV 233
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
271-483 6.80e-18

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: 82.93  E-value: 6.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 271 RLSRGDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSEDr 348
Cdd:cd03261    7 TKSFGGRTvlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQS- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 349 kgEGLLLPQSIAANLSL-----GQLARvarggvvdgERENALAARQIDALRIRARGPAQPvAELSGGNQQKVAIGRWLGR 423
Cdd:cd03261   86 --GALFDSLTVFENVAFplrehTRLSE---------EEIREIVLEKLEAVGLRGAEDLYP-AELSGGMKKRVALARALAL 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 424 DMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03261  154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGK 214
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
27-229 1.47e-17

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: 82.00  E-value: 1.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeYAPHSR--AHAEALGVRMvMQELNLVPTLT 104
Cdd:cd03267   35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRrkKFLRRIGVVF-GQKTQLWWDLP 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 105 VAENLFLDRLPHRfgvIDRRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAR 184
Cdd:cd03267  112 VIDSFYLLAAIYD---LPPARFKKRLDELSELLDLEEL-LDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 490656625 185 EVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03267  188 AQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
13-235 1.67e-17

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 82.22  E-value: 1.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  13 PTLVVTGIGKTY-----AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAeyaPHSRAHAEA 87
Cdd:COG4525    2 SMLTVRHVSVRYpgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPGADR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  88 lGVrmVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAG 167
Cdd:COG4525   79 -GV--VFQKDALLPWLNVLDNV---AFGLRLRGVPKAERRARAEELLALVGLADFA-RRRIWQLSGGMRQRVGIARALAA 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 168 DCRVLILDEPTAMLTA--REV--ELLFDqIARLKADGVALvyISHRLEELARVAQRVAVL--RDGRLVHVDRID 235
Cdd:COG4525  152 DPRFLLMDEPFGALDAltREQmqELLLD-VWQRTGKGVFL--ITHSVEEALFLATRLVVMspGPGRIVERLELD 222
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
277-484 2.61e-17

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: 80.72  E-value: 2.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPprpaAIRSPADAVRHGIALVSedrkGEGLLLP 356
Cdd:cd03268   15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK----SYQKNIEALRRIGALIE----APGFYPN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLGQLARVARGGVVDgerenalaaRQIDALRIRARGpAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:cd03268   87 LTARENLRLLARLLGIRKKRID---------EVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 490656625 437 IDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03268  157 LDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
26-204 2.77e-17

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 80.30  E-value: 2.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEY-APHSRAHAEALGVRMVMQelnlvPTLT 104
Cdd:PRK13539  15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIdDPDVAEACHYLGHRNAMK-----PALT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 105 VAENL-----FLDRLPHRfgvidrrrlaadARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTA 179
Cdd:PRK13539  90 VAENLefwaaFLGGEELD------------IAAALEAVGLAPLA-HLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
                        170       180
                 ....*....|....*....|....*.
gi 490656625 180 MLTAREVELLFDQI-ARLKADGVALV 204
Cdd:PRK13539 157 ALDAAAVALFAELIrAHLAQGGIVIA 182
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
12-227 3.36e-17

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 83.46  E-value: 3.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  12 TPTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEyapHSRAHAEALGV 90
Cdd:PRK09452  12 SPLVELRGISKSFDGkEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD---ITHVPAENRHV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  91 RMVMQELNLVPTLTVAEN----LFLDRLPH---RFGVIDrrrlaadaraAMARVGLDSL---DPDTLVGslgiGHQQMVE 160
Cdd:PRK09452  89 NTVFQSYALFPHMTVFENvafgLRMQKTPAaeiTPRVME----------ALRMVQLEEFaqrKPHQLSG----GQQQRVA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 161 IARSLAGDCRVLILDEPTAMLTAR---EVELLFDQIAR-LkadGVALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKlrkQMQNELKALQRkL---GITFVFVTHDQEEALTMSDRIVVMRDGR 222
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
266-484 3.90e-17

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: 80.69  E-value: 3.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 266 RLRVERLSRGD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYG-----ADAADGGTVSIGDpprpaairspaDAVR 338
Cdd:cd03260    2 ELRDLNVYYGDkhALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDG-----------KDIY 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 339 HGIALVSEDRKGEGL------LLPQSIAANLSLG-QLARVARGGVVDGERENAL--------AARQIDALRirargpaqp 403
Cdd:cd03260   71 DLDVDVLELRRRVGMvfqkpnPFPGSIYDNVAYGlRLHGIKLKEELDERVEEALrkaalwdeVKDRLHALG--------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 404 vaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREgRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03260  142 ---LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGR 217

                 .
gi 490656625 484 M 484
Cdd:cd03260  218 L 218
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
272-486 9.50e-17

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 82.20  E-value: 9.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 272 LSRGDA--VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHgIALVSEDrk 349
Cdd:PRK09536  11 VEFGDTtvLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG--DDVEALSARAASRR-VASVPQD-- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 350 geglllpQSIAANLSLGQLARVARG---GVVDGERENALAA--RQIDALRIrARGPAQPVAELSGGNQQKVAIGRWLGRD 424
Cdd:PRK09536  86 -------TSLSFEFDVRQVVEMGRTphrSRFDTWTETDRAAveRAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQA 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 425 MGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
264-487 9.71e-17

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 81.68  E-value: 9.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 264 APRLRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADavRh 339
Cdd:COG3842    3 MPALELENVSKryGDvtALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG--RDVTGLPPEK--R- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 340 GIALVSEDrkgeGLLLPQ-SIAANLSLG-QLARVARGgvvdgEREnALAARQIDALRIRARGPAQPvAELSGGNQQKVAI 417
Cdd:COG3842   78 NVGMVFQD----YALFPHlTVAENVAFGlRMRGVPKA-----EIR-ARVAELLELVGLEGLADRYP-HQLSGGQQQRVAL 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 418 GRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:COG3842  147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQV 217
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
276-492 1.30e-16

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 78.94  E-value: 1.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPP----RPAAIRspadAVRHGIALVSEDRKge 351
Cdd:COG2884   16 EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrlKRREIP----YLRRRIGVVFQDFR-- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 352 glLLPQ-SIAANLSLGQlaRVArggvvdGERENALAARQIDALR---IRARGPAQPvAELSGGNQQKVAIGRWLGRDMGV 427
Cdd:COG2884   90 --LLPDrTVYENVALPL--RVT------GKSRKEIRRRVREVLDlvgLSDKAKALP-HELSGGEQQRVAIARALVNRPEL 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 428 LLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAVFERGG 492
Cdd:COG2884  159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
265-484 1.47e-16

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: 78.85  E-value: 1.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADG---GTVSI-GDPPRPaairspaDAVRHG 340
Cdd:cd03234   10 GLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFnGQPRKP-------DQFQKC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 341 IALVSE-DRKGEGLLLPQSI--AANLSLGQLARVA-RGGVVDGERENALAARQIDALRIRArgpaqpvaeLSGGNQQKVA 416
Cdd:cd03234   83 VAYVRQdDILLPGLTVRETLtyTAILRLPRKSSDAiRKKRVEDVLLRDLALTRIGGNLVKG---------ISGGERRRVS 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 417 IGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRaIVVVS-----SDLRELMlicDRIGVMSAGRM 484
Cdd:cd03234  154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNR-IVILTihqprSDLFRLF---DRILLLSSGEI 222
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
26-229 1.50e-16

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: 77.35  E-value: 1.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVrmvmqelnlvptltv 105
Cdd:cd03247   15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISV--------------- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 aenlfLDRLPHRFGvidrrrlaadaraamarvgldsldpDTLVGSLGI----GHQQMVEIARSLAGDCRVLILDEPTAML 181
Cdd:cd03247   80 -----LNQRPYLFD-------------------------TTLRNNLGRrfsgGERQRLALARILLQDAPIVLLDEPTVGL 129
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490656625 182 ---TAREV-ELLFDQiarlkADGVALVYISHRLEELARVaQRVAVLRDGRLV 229
Cdd:cd03247  130 dpiTERQLlSLIFEV-----LKDKTLIWITHHLTGIEHM-DKILFLENGKII 175
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
27-229 1.63e-16

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 82.85  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSrAHAEalgVRMVMQElnlvPTL 103
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplVQYDHHY-LHRQ---VALVGQE----PVL 566
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  104 ---TVAENLF--LDRLPHrfgviDRRRLAADARAAMARVGLDSLDPDTLVGSLG----IGHQQMVEIARSLAGDCRVLIL 174
Cdd:TIGR00958 567 fsgSVRENIAygLTDTPD-----EEIMAAAKAANAHDFIMEFPNGYDTEVGEKGsqlsGGQKQRIAIARALVRKPRVLIL 641
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490656625  175 DEPTAMLTArEVELLFdQIARLKADGVALVyISHRLeELARVAQRVAVLRDGRLV 229
Cdd:TIGR00958 642 DEATSALDA-ECEQLL-QESRSRASRTVLL-IAHRL-STVERADQILVLKKGSVV 692
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
277-487 1.65e-16

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: 78.57  E-value: 1.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpAAIRSPADAVRHGIALVSEDRKGEGLLlp 356
Cdd:cd03265   15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG----HDVVREPREVRRRIGIVFQDLSVDDEL-- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 qSIAANLSLgqLARVArgGVVDGERENalaaRQIDALRIRARGPA--QPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:cd03265   89 -TGWENLYI--HARLY--GVPGAERRE----RIDELLDFVGLLEAadRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490656625 435 RGIDVGAKFDIYALLDAL-AREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:cd03265  160 IGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
cbiO PRK13644
energy-coupling factor transporter ATPase;
27-274 1.71e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 79.65  E-value: 1.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVRMVMQ--ELNLVPTlT 104
Cdd:PRK13644  16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQnpETQFVGR-T 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 105 VAENLfldrlphRFG----VIDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAGDCRVLILDEP 177
Cdd:PRK13644  95 VEEDL-------AFGpenlCLPPIEIRKRVDRALAEIGLEKYrhrSPKTLSG----GQGQCVALAGILTMEPECLIFDEV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 178 TAMLTAREVELLFDQIARLKADGVALVYISHRLEELaRVAQRVAVLRDGRLV---HVDRIDAQPTERLVALMAGR--EIA 252
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVlegEPENVLSDVSLQTLGLTPPSliELA 242
                        250       260
                 ....*....|....*....|....*..
gi 490656625 253 EQ-AVHGTRTP----GAPRLRVERLSR 274
Cdd:PRK13644 243 ENlKMHGVVIPwentSSPSSFAEEICR 269
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
27-229 2.09e-16

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 79.26  E-value: 2.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHA-EALGVrmVMQEL-NLVPTLT 104
Cdd:PRK13632  23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIrKKIGI--IFQNPdNQFIGAT 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 105 VAENLfldrlphRFGV----IDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAGDCRVLILDEP 177
Cdd:PRK13632 101 VEDDI-------AFGLenkkVPPKKMKDIIDDLAKKVGMEDYldkEPQNLSG----GQKQRVAIASVLALNPEIIIFDES 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490656625 178 TAMLTAREVELLFDQIARLKADGV-ALVYISHRLEElARVAQRVAVLRDGRLV 229
Cdd:PRK13632 170 TSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDE-AILADKVIVFSEGKLI 221
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
264-486 2.10e-16

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 78.16  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 264 APRLRVERLSR----GD----AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD-------PPRPA 328
Cdd:COG1136    2 SPLLELRNLTKsygtGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisslsERELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 329 AIRspadavRHGIALVSEDrkgeGLLLPQ-SIAANLSLGQLARvargGVVDGEREnALAARQIDALRIRARGPAQPvAEL 407
Cdd:COG1136   82 RLR------RRHIGFVFQF----FNLLPElTALENVALPLLLA----GVSRKERR-ERARELLERVGLGDRLDHRP-SQL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 408 SGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLReLMLICDRIGVMSAGRMHA 486
Cdd:COG1136  146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPE-LAARADRVIRLRDGRIVS 224
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
30-227 2.19e-16

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 78.88  E-value: 2.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  30 DDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVRMVMQELNLVPTLTVAENL 109
Cdd:PRK11300  22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVRLFREMTVIENL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 110 FLDRLPH-RFGVI-----------DRRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEP 177
Cdd:PRK11300 102 LVAQHQQlKTGLFsgllktpafrrAESEALDRAATWLERVGLLEH-ANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490656625 178 TAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
278-434 2.39e-16

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: 76.15  E-value: 2.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRspaDAVRHGIALVSEDRkgegLLLPQ 357
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER---KSLRKEIGYVFQDP----QLFPR 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625  358 SIAA-NLSLGQLARVARGGVVDGERENALAarQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:pfam00005  74 LTVReNLRLGLLLKGLSKREKDARAEEALE--KLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
274-508 2.43e-16

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 81.93  E-value: 2.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 274 RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAAIRSpadaVRHGIALVSEDrkgeG 352
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIRTVTRAS----LRRNIAVVFQD----A 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 353 LLLPQSIAANLslgqlaRVARGGVVDGE-RENALAARQIDALRIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGV 427
Cdd:PRK13657 419 GLFNRSIEDNI------RVGRPDATDEEmRAAAERAQAHDFIERKPDGYDTVVGErgrqLSGGERQRLAIARALLKDPPI 492
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 428 LLFDEPTRGIDVGAKFDIYALLDALaREGRAIVVVS---SDLRElmliCDRIGVMSAGRmhaVFERGGWTQDALLGAAFA 504
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAhrlSTVRN----ADRILVFDNGR---VVESGSFDELVARGGRFA 564

                 ....
gi 490656625 505 GYAR 508
Cdd:PRK13657 565 ALLR 568
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
28-235 2.74e-16

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 78.58  E-value: 2.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPhsrahaeaLGVRMVMQelnlvPTLTVAE 107
Cdd:COG1134   41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSAL--------LELGAGFH-----PELTGRE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NLFLdrlphrFGVIdrrrlaadaraamarVGLDSLDPDTLVGSL----GIG---HQQ-------MVeiAR-----SLAGD 168
Cdd:COG1134  108 NIYL------NGRL---------------LGLSRKEIDEKFDEIvefaELGdfiDQPvktyssgMR--ARlafavATAVD 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 169 CRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRID 235
Cdd:COG1134  165 PDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
277-487 2.94e-16

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: 78.15  E-value: 2.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADavrHGIALVSEDRkgeGLLLP 356
Cdd:cd03296   17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG--EDATDVPVQE---RNVGFVFQHY---ALFRH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLGQLARVARGGV----VDGERENALAARQIDALRirARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLFDE 432
Cdd:cd03296   89 MTVFDNVAFGLRVKPRSERPpeaeIRAKVHELLKLVQLDWLA--DRYPAQ----LSGGQRQRVALARALAVEPKVLLLDE 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 433 PTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:cd03296  163 PFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQV 218
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
28-228 2.96e-16

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 77.90  E-value: 2.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRAHAEALGVRMVMQELNLVPTLT 104
Cdd:PRK10584  25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplHQMDEEARAKLRAKHVGFVFQSFMLIPTLN 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 105 VAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSlDPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAR 184
Cdd:PRK10584 105 ALENV---ELPALLRGESSRQSRNGAKALLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 490656625 185 EVELLFDQIARLKAD-GVALVYISHRlEELARVAQRVAVLRDGRL 228
Cdd:PRK10584 181 TGDKIADLLFSLNREhGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
13-228 3.50e-16

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 78.15  E-value: 3.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  13 PTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE---YAPHSRAHaeaL 88
Cdd:COG1137    2 MTLEAENLVKSYGKrTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithLPMHKRAR---L 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  89 GVRMVMQELNLVPTLTVAENL--FLDRLPhrfgvidrrrlaadaraamarvgldsLDP-------DTLVGSLGIGH--QQ 157
Cdd:COG1137   79 GIGYLPQEASIFRKLTVEDNIlaVLELRK--------------------------LSKkereerlEELLEEFGITHlrKS 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 158 M-----------VEIARSLAGDCRVLILDEPTA---MLTAREVELLfdqIARLKADGVAlVYIS-HRLEELARVAQRVAV 222
Cdd:COG1137  133 KayslsggerrrVEIARALATNPKFILLDEPFAgvdPIAVADIQKI---IRHLKERGIG-VLITdHNVRETLGICDRAYI 208

                 ....*.
gi 490656625 223 LRDGRL 228
Cdd:COG1137  209 ISEGKV 214
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
275-486 3.95e-16

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: 79.77  E-value: 3.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  275 GDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaaiRSPADAvRHGIALVSEDRK----- 349
Cdd:TIGR02142  10 GDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG-------RTLFDS-RKGIFLPPEKRRigyvf 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  350 GEGLLLPQ-SIAANLSLGqlarVARggvVDGERENALAARQIDALRIrarGP--AQPVAELSGGNQQKVAIGRWLGRDMG 426
Cdd:TIGR02142  82 QEARLFPHlSVRGNLRYG----MKR---ARPSERRISFERVIELLGI---GHllGRLPGRLSGGEKQRVAIGRALLSSPR 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625  427 VLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:TIGR02142 152 LLLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
271-490 4.19e-16

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 79.81  E-value: 4.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 271 RLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPadaVRH-GIALVSEDRk 349
Cdd:COG1118   11 RFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--RDLFTNLP---PRErRVGFVFQHY- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 350 gegLLLPQ-SIAANLSLGqlARVARggvVDGERENALAARQIDALRIR---ARGPAQpvaeLSGGNQQKVAIGRWLGRDM 425
Cdd:COG1118   85 ---ALFPHmTVAENIAFG--LRVRP---PSKAEIRARVEELLELVQLEglaDRYPSQ----LSGGQRQRVALARALAVEP 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 426 GVLLFDEPTRGIDVGAKFDIYALL-DALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM------HAVFER 490
Cdd:COG1118  153 EVLLLDEPFGALDAKVRKELRRWLrRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIeqvgtpDEVYDR 224
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
17-280 4.66e-16

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 79.35  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  17 VTGIGKTY-----AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRahAEALGVR 91
Cdd:COG1135    4 LENLSKTFptkggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSE--RELRAAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  92 ----MVMQELNLVPTLTVAEN----LFLDRLPHR-----------FgvidrrrlaadaraamarVGL-DSLD--PDTLVG 149
Cdd:COG1135   82 rkigMIFQHFNLLSSRTVAENvalpLEIAGVPKAeirkrvaelleL------------------VGLsDKADayPSQLSG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 150 slgiGHQQMVEIARSLAGDCRVLILDEPTAML---TAREV-ELLfDQI-ARLkadGVALVYISHRLEELARVAQRVAVLR 224
Cdd:COG1135  144 ----GQKQRVGIARALANNPKVLLCDEATSALdpeTTRSIlDLL-KDInREL---GLTIVLITHEMDVVRRICDRVAVLE 215
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 225 DGRLV---HVDRIDAQP----TERLVALMAGREIAEQAVHGTRTPGAPRLRVeRLS-RGDAVRD 280
Cdd:COG1135  216 NGRIVeqgPVLDVFANPqselTRRFLPTVLNDELPEELLARLREAAGGGRLV-RLTfVGESADE 278
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
28-229 6.56e-16

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 77.14  E-value: 6.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEA-LGVrmVMQElNLVPTLTVA 106
Cdd:cd03252   17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRqVGV--VLQE-NVLFNRSIR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 107 ENLFL-DRLPHRFGVIDRRRLAADARAAMARvgldSLDPDTLVGSLGI----GHQQMVEIARSLAGDCRVLILDEPTAML 181
Cdd:cd03252   94 DNIALaDPGMSMERVIEAAKLAGAHDFISEL----PEGYDTIVGEQGAglsgGQRQRIAIARALIHNPRILIFDEATSAL 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 490656625 182 TArEVELLFDQIARLKADGVALVYISHRLEELaRVAQRVAVLRDGRLV 229
Cdd:cd03252  170 DY-ESEHAIMRNMHDICAGRTVIIIAHRLSTV-KNADRIIVMEKGRIV 215
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
27-242 7.27e-16

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 77.06  E-value: 7.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEY-APHSRAHAEALGVRMVMQELNLVPTLTV 105
Cdd:PRK09493  15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVnDPKVDERLIRQEAGMVFQQFYLFPHLTA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLFLDrlPHRFGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAMLT 182
Cdd:PRK09493  95 LENVMFG--PLRVRGASKEEAEKQARELLAKVGLAERAhhyPSELSG----GQQQRVAIARALAVKPKLMLFDEPTSALD 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 183 A---REVELLFDQIARlkaDGVALVYISHRLEELARVAQRVAVLRDGRLVH----VDRIDAQPTERL 242
Cdd:PRK09493 169 PelrHEVLKVMQDLAE---EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEdgdpQVLIKNPPSQRL 232
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
27-208 8.77e-16

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: 75.86  E-value: 8.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRAHAEALGVRMVMQelnlvPTL 103
Cdd:TIGR01189  14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplAEQRDEPHENILYLGHLPGLK-----PEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  104 TVAENLfldrlphRFGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTA 183
Cdd:TIGR01189  89 SALENL-------HFWAAIHGGAQRTIEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
                         170       180
                  ....*....|....*....|....*
gi 490656625  184 REVELLFDQIARLKADGVALVYISH 208
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTH 185
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
278-483 1.02e-15

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 77.92  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAaiRSPADAVRHGIalvsedrkgegllLPQ 357
Cdd:PRK13537  23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS--RARHARQRVGV-------------VPQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 --SIAANLSLGQLARVArggvvdgERENALAARQIDAL--------RIRARGPAqPVAELSGGNQQKVAIGRWLGRDMGV 427
Cdd:PRK13537  88 fdNLDPDFTVRENLLVF-------GRYFGLSAAAARALvppllefaKLENKADA-KVGELSGGMKRRLTLARALVNDPDV 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 428 LLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
31-291 1.15e-15

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 78.92  E-value: 1.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  31 DVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL---GVRMVMQELNLVPTLTVAE 107
Cdd:PRK10070  46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkKIAMVFQSFALMPHMTVLD 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NLFLDRlphRFGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAMLTAR 184
Cdd:PRK10070 126 NTAFGM---ELAGINAEERREKALDALRQVGLENYAhsyPDELSG----GMRQRVGLARALAINPDILLMDEAFSALDPL 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 185 EVELLFDQIARLKADGV-ALVYISHRLEELARVAQRVAVLRDGRLVHV---DRIDAQPTERLV----------ALMAGRE 250
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVgtpDEILNNPANDYVrtffrgvdisQVFSAKD 278
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 490656625 251 IAEQAVHGT--RTPG-APRLRVERLSRGDavRDVSFDVRAGEIF 291
Cdd:PRK10070 279 IARRTPNGLirKTPGfGPRSALKLLQDED--REYGYVIERGNKF 320
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
277-483 1.17e-15

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: 74.73  E-value: 1.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRS-PADAVRHGIALVSEDrkgeGLLL 355
Cdd:cd03228   17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD----LRDlDLESLRKNIAYVPQD----PFLF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 PQSIAANLslgqlarvarggvvdgerenalaarqidalrirargpaqpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:cd03228   89 SGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATS 125
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 490656625 436 GIDVGAKFDIYALLDALaREGRAIVVVSSDLrELMLICDRIGVMSAGR 483
Cdd:cd03228  126 ALDPETEALILEALRAL-AKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
15-228 1.23e-15

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 76.93  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG----------AEYAPHSRA 83
Cdd:PRK10619   6 LNVIDLHKRYGEhEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdGQLKVADKN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  84 HAEALGVR--MVMQELNLVPTLTVAENLFldRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGSLGIGHQQMVEI 161
Cdd:PRK10619  86 QLRLLRTRltMVFQHFNLWSHMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSI 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 162 ARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
26-229 1.68e-15

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: 75.72  E-value: 1.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHA-EALGVrmVMQELNLVPTlT 104
Cdd:cd03254   16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLrSMIGV--VLQDTFLFSG-T 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 105 VAENLFLDRLPHRFGVIdrrrlaadaRAAMARVGLDSL------DPDTLVG----SLGIGHQQMVEIARSLAGDCRVLIL 174
Cdd:cd03254   93 IMENIRLGRPNATDEEV---------IEAAKEAGAHDFimklpnGYDTVLGenggNLSQGERQLLAIARAMLRDPKILIL 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 175 DEPTAMLTAREVELLFDQIARLKADGVALVyISHRLEELaRVAQRVAVLRDGRLV 229
Cdd:cd03254  164 DEATSNIDTETEKLIQEALEKLMKGRTSII-IAHRLSTI-KNADKILVLDDGKII 216
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
19-270 1.85e-15

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 77.53  E-value: 1.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  19 GIGKTYAEP-----VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAH--AEALGVR 91
Cdd:PRK11153   6 NISKVFPQGgrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARRQIG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  92 MVMQELNLVPTLTVAENLFldrLPHRFGVIDRRRLAADARAAMARVGL-DSLD--PDTLVGslgiGHQQMVEIARSLAGD 168
Cdd:PRK11153  86 MIFQHFNLLSSRTVFDNVA---LPLELAGTPKAEIKARVTELLELVGLsDKADryPAQLSG----GQKQRVAIARALASN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 169 CRVLILDEPTAML---TAREV-ELLFDQIARLkadGVALVYISHRLEELARVAQRVAVLRDGRLV---HVDRIDAQP--- 238
Cdd:PRK11153 159 PKVLLCDEATSALdpaTTRSIlELLKDINREL---GLTIVLITHEMDVVKRICDRVAVIDAGRLVeqgTVSEVFSHPkhp 235
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 490656625 239 -TERLVALMAGREIAEQ---AVHGTRTPGA-PRLRVE 270
Cdd:PRK11153 236 lTREFIQSTLHLDLPEDylaRLQAEPTTGSgPLLRLE 272
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
25-229 2.70e-15

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: 75.34  E-value: 2.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  25 AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHS-RAHaealgVRMVMQELNLV 100
Cdd:cd03251   14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLASlRRQ-----IGLVSQDVFLF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 101 PTlTVAENLfldrlphRFGVIDRRRLAADARAAMARVG--LDSLDP--DTLVGSLGI----GHQQMVEIARSLAGDCRVL 172
Cdd:cd03251   89 ND-TVAENI-------AYGRPGATREEVEEAARAANAHefIMELPEgyDTVIGERGVklsgGQRQRIAIARALLKDPPIL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 173 ILDEPTAMLTAREVELLFDQIARLKADGVALVyISHRLEELARvAQRVAVLRDGRLV 229
Cdd:cd03251  161 ILDEATSALDTESERLVQAALERLMKNRTTFV-IAHRLSTIEN-ADRIVVLEDGKIV 215
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
12-230 2.84e-15

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 78.61  E-value: 2.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  12 TPTLVVTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA-----PHS 81
Cdd:PRK10535   2 TALLELKDIRRSYPSgeeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtldadALA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  82 RAHAEALGvrMVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLD---SLDPDTLVGslgiGHQQM 158
Cdd:PRK10535  82 QLRREHFG--FIFQRYHLLSHLTAAQNV---EVPAVYAGLERKQRLLRAQELLQRLGLEdrvEYQPSQLSG----GQQQR 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 159 VEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRlEELARVAQRVAVLRDGRLVH 230
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVR 223
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
28-229 3.36e-15

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 75.47  E-value: 3.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG-AEYAPHSRAHAEALGVR----MVMQELNLVPT 102
Cdd:PRK14246  25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkVLYFGKDIFQIDAIKLRkevgMVFQQPNPFPH 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENLFLDRLPHrfGVIDRRRLAADARAAMARVGLDSLDPDTL---VGSLGIGHQQMVEIARSLAGDCRVLILDEPTA 179
Cdd:PRK14246 105 LSIYDNIAYPLKSH--GIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490656625 180 MLTAREVELLFDQIARLKADgVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
262-487 4.00e-15

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: 75.02  E-value: 4.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 262 PGAPRLRVERL--SRGDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAV 337
Cdd:COG1127    1 MSEPMIEVRNLtkSFGDRVvlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 338 RHGI-------AL-----VSED-----RkgEGLLLPQSIAANLSLGQLARVARGGVVDgerenalaarqidalriraRGP 400
Cdd:COG1127   81 RRRIgmlfqggALfdsltVFENvafplR--EHTDLSEAEIRELVLEKLELVGLPGAAD-------------------KMP 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 401 AqpvaELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGID-VGAKfDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGV 478
Cdd:COG1127  140 S----ELSGGMRKRVALARALALDPEILLYDEPTAGLDpITSA-VIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAV 214

                 ....*....
gi 490656625 479 MSAGRMHAV 487
Cdd:COG1127  215 LADGKIIAE 223
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
267-486 4.48e-15

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 75.05  E-value: 4.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSRGDA----VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHgIA 342
Cdd:PRK11231   3 LRTENLTVGYGtkriLNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD--KPISMLSSRQLARR-LA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDrkgegLLLPQSIAAN----------LSL-GQLARVARGGVvdgerENALAARQIDALRIRargpaqPVAELSGGN 411
Cdd:PRK11231  80 LLPQH-----HLTPEGITVRelvaygrspwLSLwGRLSAEDNARV-----NQAMEQTRINHLADR------RLTDLSGGQ 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 412 QQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA 218
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
282-486 5.95e-15

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 74.41  E-value: 5.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 282 SFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD------PP--RPaairspadavrhgIALVSEdrkgEGL 353
Cdd:COG3840   19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltalPPaeRP-------------VSMLFQ----ENN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 LLPQ-SIAANLSLG----------QLARVARggvvdgerenalAARQIDALRIRARGPAQpvaeLSGGNQQKVAIGRWLG 422
Cdd:COG3840   82 LFPHlTVAQNIGLGlrpglkltaeQRAQVEQ------------ALERVGLAGLLDRLPGQ----LSGGQRQRVALARCLV 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 423 RDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:COG3840  146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
29-246 7.48e-15

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: 77.15  E-value: 7.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMR-LAGAEY------APHSRAHAEALgVRMVMQELNLVP 101
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEWvdmtkpGPDGRGRAKRY-IGILHQEYDLYP 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  102 TLTVAENLF----LDrLPHRFGVIdrrrlaaDARAAMARVGLDS------LD--PDTLVGslgiGHQQMVEIARSLAGDC 169
Cdd:TIGR03269 379 HRTVLDNLTeaigLE-LPDELARM-------KAVITLKMVGFDEekaeeiLDkyPDELSE----GERHRVALAQVLIKEP 446
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  170 RVLILDEPTAML---TAREVEllfDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVhvdriDAQPTERLVAL 245
Cdd:TIGR03269 447 RIVILDEPTGTMdpiTKVDVT---HSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIV-----KIGDPEEIVEE 518

                  .
gi 490656625  246 M 246
Cdd:TIGR03269 519 L 519
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
27-489 8.40e-15

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 77.20  E-value: 8.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSR--------AHAEALGVR-----MV 93
Cdd:PRK10261  30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRqvielseqSAAQMRHVRgadmaMI 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 MQE--LNLVPTLTV----AENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGslgiGHQQMVEIARSLAG 167
Cdd:PRK10261 110 FQEpmTSLNPVFTVgeqiAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG----GMRQRVMIAMALSC 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVH---VDRIDAQP----T 239
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVEtgsVEQIFHAPqhpyT 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 240 ERLVAL------MAGREI---------------AEQAVHGTRTPGAPRLRVE--------------RLSRG-DAVRDVSF 283
Cdd:PRK10261 266 RALLAAvpqlgaMKGLDYprrfplislehpakqEPPIEQDTVVDGEPILQVRnlvtrfplrsgllnRVTREvHAVEKVSF 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 284 DVRAGEIFGISGLIGAGRT----ELLRLVygadAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSEDRKGEgllLPQSI 359
Cdd:PRK10261 346 DLWPGETLSLVGESGSGKSttgrALLRLV----ESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYAS---LDPRQ 418
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 360 AANLSLGQLARVArgGVVDGERENALAARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDV 439
Cdd:PRK10261 419 TVGDSIMEPLRVH--GLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 440 GAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRM------HAVFE 489
Cdd:PRK10261 497 SIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIveigprRAVFE 553
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
27-439 8.54e-15

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 77.30  E-value: 8.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAM---------RL--------AGAEY---APHSRAHAE 86
Cdd:PRK11147  17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdlivaRLqqdpprnvEGTVYdfvAEGIEEQAE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  87 ALgvRMVMQELNLVPTLTVAENLflDRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGSLGIGHQQMVEIARSLA 166
Cdd:PRK11147  97 YL--KRYHDISHLVETDPSEKNL--NELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGGWLRKAALGRALV 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 167 GDCRVLILDEPTAMLTAREVELL--FdqiarLKADGVALVYISHRLEELARVAQRVAVLRDGRLVH---------VDRID 235
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDIETIEWLegF-----LKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSypgnydqylLEKEE 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 236 AQPTERLVALMAGREIAEQAV---HG-----TRTPGAPR----LRVERLSR----GDA---------------------- 277
Cdd:PRK11147 248 ALRVEELQNAEFDRKLAQEEVwirQGikarrTRNEGRVRalkaLRRERSERrevmGTAkmqveeasrsgkivfemenvny 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 -------VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIG--------DPPRpaAIRSPADAVrhgia 342
Cdd:PRK11147 328 qidgkqlVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGtklevayfDQHR--AELDPEKTV----- 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 lvsEDRKGEGlllPQSIaanlslgqlarvarggVVDGERENALAARQiDAL--RIRARgpaQPVAELSGGNQQKVAIGRW 420
Cdd:PRK11147 401 ---MDNLAEG---KQEV----------------MVNGRPRHVLGYLQ-DFLfhPKRAM---TPVKALSGGERNRLLLARL 454
                        490
                 ....*....|....*....
gi 490656625 421 LGRDMGVLLFDEPTRGIDV 439
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDV 473
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
277-483 1.06e-14

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: 72.95  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAiRSPADAVRHGIALVSEDRKgeglLLP 356
Cdd:cd03262   15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDD-KKNINELRQKVGMVFQQFN----LFP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 Q-SIAANLSLGQLarvarggVVDGERENALAARQIDALR---IRARGPAQPvAELSGGNQQKVAIGRWLGRDMGVLLFDE 432
Cdd:cd03262   90 HlTVLENITLAPI-------KVKGMSKAEAEERALELLEkvgLADKADAYP-AQLSGGQQQRVAIARALAMNPKVMLFDE 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 433 PTRGID---VGAKFDIyalLDALAREGRAIVVVSSDL---RElmlICDRIGVMSAGR 483
Cdd:cd03262  162 PTSALDpelVGEVLDV---MKDLAEEGMTMVVVTHEMgfaRE---VADRVIFMDDGR 212
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
20-228 1.13e-14

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: 77.36  E-value: 1.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625    20 IGKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGvrMVMQELNL 99
Cdd:TIGR01257  937 IFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLG--MCPQHNIL 1014
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   100 VPTLTVAEN-LFLDRLPHRfgvidrrrlaadaRAAMARVGLDSLDPDTLV--------GSLGIGHQQMVEIARSLAGDCR 170
Cdd:TIGR01257 1015 FHHLTVAEHiLFYAQLKGR-------------SWEEAQLEMEAMLEDTGLhhkrneeaQDLSGGMQRKLSVAIAFVGDAK 1081
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625   171 VLILDEPTAMLTAREVELLFDQIARLKAdGVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
264-491 1.25e-14

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 73.81  E-value: 1.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 264 APRLRVERLSR----GDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairspADAVRH 339
Cdd:PRK11701   4 QPLLSVRGLTKlygpRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM----------RDGQLR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 340 GIALVSEDRK-----GEGLLLPQSIAANLSLGqlarVARGGVVdGERENALAAR----------------QIDALRIRAR 398
Cdd:PRK11701  74 DLYALSEAERrrllrTEWGFVHQHPRDGLRMQ----VSAGGNI-GERLMAVGARhygdiratagdwlervEIDAARIDDL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 399 gPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIG 477
Cdd:PRK11701 149 -PTT----FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLL 223
                        250
                 ....*....|....
gi 490656625 478 VMSAGRmhaVFERG 491
Cdd:PRK11701 224 VMKQGR---VVESG 234
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
279-504 1.28e-14

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 73.42  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 279 RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRS-PADAVRHGIALVSEDRkgegLLLPQ 357
Cdd:cd03253   18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD----IREvTLDSLRRAIGVVPQDT----VLFND 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 SIAANLslgqlaRVARGGVVDGERENALAARQIDALRIRAR-GPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDE 432
Cdd:cd03253   90 TIGYNI------RYGRPDATDEEVIEAAKAAQIHDKIMRFPdGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDE 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 433 PTRGIDVGAKFDIYALLDALAReGRAIVVVSSDLRELMlICDRIGVMSAGRmhaVFERGGWTQDALLGAAFA 504
Cdd:cd03253  164 ATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIV-NADKIIVLKDGR---IVERGTHEELLAKGGLYA 230
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
15-251 1.85e-14

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 73.20  E-value: 1.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYA-EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyAPHSRAHAEAlGVrmV 93
Cdd:PRK11248   2 LQISHLYADYGgKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG---KPVEGPGAER-GV--V 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 MQELNLVPTLTVAENLfldrlphRFGV----IDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDC 169
Cdd:PRK11248  76 FQNEGLLPWRNVQDNV-------AFGLqlagVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANP 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 170 RVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAG 248
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLNFARRFVAGESS 227

                 ...
gi 490656625 249 REI 251
Cdd:PRK11248 228 RSI 230
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
240-499 2.01e-14

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 75.97  E-value: 2.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 240 ERLVALM-AGREIAEQAVHGTRTPGAPRLRVERLS---RGD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADA 313
Cdd:COG1132  312 ERIFELLdEPPEIPDPPGAVPLPPVRGEIEFENVSfsyPGDrpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 314 ADGGTVSIGDPPrpaaIRS-PADAVRHGIALVSEDrkgeGLLLPQSIAANLSLGqlarvaRGGVVDGERENALAARQIDA 392
Cdd:COG1132  392 PTSGRILIDGVD----IRDlTLESLRRQIGVVPQD----TFLFSGTIRENIRYG------RPDATDEEVEEAAKAAQAHE 457
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 393 LrIRA--RGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALaREGRAIVVVSSDL 466
Cdd:COG1132  458 F-IEAlpDGYDTVVGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRL 535
                        250       260       270
                 ....*....|....*....|....*....|...
gi 490656625 467 RELMLiCDRIGVMSAGRmhaVFERGgwTQDALL 499
Cdd:COG1132  536 STIRN-ADRILVLDDGR---IVEQG--THEELL 562
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
271-512 3.75e-14

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: 73.98  E-value: 3.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 271 RLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD------------PPRpaairspadavR 338
Cdd:COG4148    8 RLRRGGFTLDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflPPH-----------R 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 339 HGIALVSEDrkgeGLLLP-QSIAANLSLGQlARVARGgvvdgeRENALAARQIDALRIRA---RGPAQpvaeLSGGNQQK 414
Cdd:COG4148   77 RRIGYVFQE----ARLFPhLSVRGNLLYGR-KRAPRA------ERRISFDEVVELLGIGHlldRRPAT----LSGGERQR 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 415 VAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGR-AIVVVSSDLRELMLICDRIGVMSAGRMHAVfergGW 493
Cdd:COG4148  142 VAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDiPILYVSHSLDEVARLADHVVLLEQGRVVAS----GP 217
                        250
                 ....*....|....*....
gi 490656625 494 TQDALLGAAFAGYARRDAA 512
Cdd:COG4148  218 LAEVLSRPDLLPLAGGEEA 236
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
276-471 4.39e-14

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 70.73  E-value: 4.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAI--RSPADAVrhgialvsedrkgegl 353
Cdd:NF040873   6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVpqRSEVPDS---------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 lLPQSIAANLSLGQLARVARGGVVDGER----ENALAARQIDALRIRargpaqPVAELSGGNQQKVAIGRWLGRDMGVLL 429
Cdd:NF040873  70 -LPLTVRDLVAMGRWARRGLWRRLTRDDraavDDALERVGLADLAGR------QLGELSGGQRQRALLAQGLAQEADLLL 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 490656625 430 FDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELML 471
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR 184
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
276-502 4.64e-14

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 71.77  E-value: 4.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAAIRSPADAVRHGIALVSEDRKgeglL 354
Cdd:PRK11629  23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFnGQPMSKLSSAAKAELRNQKLGFIYQFHH----L 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LP-----QSIAANLSLGQLARvarggvvdgERENALAARQIDALRIRARGPAQPvAELSGGNQQKVAIGRWLGRDMGVLL 429
Cdd:PRK11629  99 LPdftalENVAMPLLIGKKKP---------AEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVL 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 430 FDEPTRGIDVGAKFDIYALLDAL-AREGRAIVVVSSDLRelmlicdrigvmSAGRMHAVFE-RGGWTQD--ALLGAA 502
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ------------LAKRMSRQLEmRDGRLTAelSLMGAE 233
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
10-229 5.06e-14

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 71.88  E-value: 5.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  10 PDTPTLVVTGIGKTYAEPV-LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL 88
Cdd:PRK11701   2 MDQPLLSVRGLTKLYGPRKgCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  89 GVRMVMQ----------ELNLVPTLT----VAENLFLDRLPHrFGVIDRRRLAADARAAMARVGLDSLdPDTLVGslgiG 154
Cdd:PRK11701  82 ERRRLLRtewgfvhqhpRDGLRMQVSaggnIGERLMAVGARH-YGDIRATAGDWLERVEIDAARIDDL-PTTFSG----G 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 155 HQQMVEIARSLAGDCRVLILDEPTAML----TARevelLFDQIARLKAD-GVALVYISHRLeELARV-AQRVAVLRDGRL 228
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLdvsvQAR----LLDLLRGLVRElGLAVVIVTHDL-AVARLlAHRLLVMKQGRV 230

                 .
gi 490656625 229 V 229
Cdd:PRK11701 231 V 231
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
27-228 5.11e-14

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: 71.35  E-value: 5.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYApHSRAHAEalgVRMVMQElnlvPTL 103
Cdd:cd03248   28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpiSQYE-HKYLHSK---VSLVGQE----PVL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 ---TVAENLFLDRLPHRFGVIdrrRLAADARAAMARVGLDSLDPDTLVGSLGI----GHQQMVEIARSLAGDCRVLILDE 176
Cdd:cd03248  100 farSLQDNIAYGLQSCSFECV---KEAAQKAHAHSFISELASGYDTEVGEKGSqlsgGQKQRVAIARALIRNPQVLILDE 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490656625 177 PTAMLTArEVELLFDQIARLKADGVALVYISHRLEELARvAQRVAVLRDGRL 228
Cdd:cd03248  177 ATSALDA-ESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
cbiO PRK13649
energy-coupling factor transporter ATPase;
21-229 5.45e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 72.47  E-value: 5.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  21 GKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYaphsRAHAEALGVRMVMQELNLV 100
Cdd:PRK13649  15 GTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLI----TSTSKNKDIKQIRKKVGLV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 101 ---PTLTVAENLFLDRL---PHRFGViDRRRLAADARAAMARVGLD----SLDPDTLVGslgiGHQQMVEIARSLAGDCR 170
Cdd:PRK13649  91 fqfPESQLFEETVLKDVafgPQNFGV-SQEEAEALAREKLALVGISeslfEKNPFELSG----GQMRRVAIAGILAMEPK 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 171 VLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
27-229 6.08e-14

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 71.49  E-value: 6.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHS-RahaEALGVrmvmqelnlVPT 102
Cdd:cd03253   15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSlR---RAIGV---------VPQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVaenLFLDRLPH--RFGVIDRRRLAADARAAMARVGlDSLDP-----DTLVGSLGI----GHQQMVEIARSLAGDCRV 171
Cdd:cd03253   83 DTV---LFNDTIGYniRYGRPDATDEEVIEAAKAAQIH-DKIMRfpdgyDTIVGERGLklsgGEKQRVAIARAILKNPPI 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 172 LILDEPTAML---TAREVellFDQIARLkADGVALVYISHRLEELARvAQRVAVLRDGRLV 229
Cdd:cd03253  159 LLLDEATSALdthTEREI---QAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
277-483 6.34e-14

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 72.80  E-value: 6.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPP----RPAAIRspadAVRHGIALVSEdrkGEG 352
Cdd:COG1135   20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltalSERELR----AARRKIGMIFQ---HFN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 353 LLLPQSIAAN--LSLgQLARVARggvvdGEREnalaaRQIDAL--------RIRARgPAQpvaeLSGGNQQKVAIGRWLG 422
Cdd:COG1135   93 LLSSRTVAENvaLPL-EIAGVPK-----AEIR-----KRVAELlelvglsdKADAY-PSQ----LSGGQKQRVGIARALA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 423 RDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDL---RElmlICDRIGVMSAGR 483
Cdd:COG1135  157 NNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMdvvRR---ICDRVAVLENGR 218
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
27-236 7.26e-14

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: 73.98  E-value: 7.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHS----RAHaealgVRMVMQELNLVPT 102
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTlaslRRQ-----VALVSQDVVLFND 420
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  103 lTVAENLfldrlphRFGVIDRRRLAADARAAMARVGLDSLDP-----DTLVGSLGI----GHQQMVEIARSLAGDCRVLI 173
Cdd:TIGR02203 421 -TIANNI-------AYGRTEQADRAEIERALAAAYAQDFVDKlplglDTPIGENGVllsgGQRQRLAIARALLKDAPILI 492
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625  174 LDEPTAMLTAREVELLFDQIARLKADGVALVyISHRLEELARvAQRVAVLRDGRLV----HVDRIDA 236
Cdd:TIGR02203 493 LDEATSALDNESERLVQAALERLMQGRTTLV-IAHRLSTIEK-ADRIVVMDDGRIVergtHNELLAR 557
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
265-486 7.68e-14

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 71.34  E-value: 7.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLS--RGDA--VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHg 340
Cdd:PRK13548   1 AMLEARNLSvrLGGRtlLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG--RPLADWSPAELARR- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 341 IAlvsedrkgeglLLPQSiaANLS----------LGQLARVARGGVVDGERENALAARQIDALRIRargpaqPVAELSGG 410
Cdd:PRK13548  78 RA-----------VLPQH--SSLSfpftveevvaMGRAPHGLSRAEDDALVAAALAQVDLAHLAGR------DYPQLSGG 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 411 NQQKVAIGRWL------GRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK13548 139 EQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGR 218

                 ...
gi 490656625 484 MHA 486
Cdd:PRK13548 219 LVA 221
cbiO PRK13637
energy-coupling factor transporter ATPase;
21-229 8.70e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 72.00  E-value: 8.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  21 GKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG-VRMVMQ--EL 97
Cdd:PRK13637  15 GTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKkVGLVFQypEY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  98 NLVPTlTVAENLFLDrlPHRFGVIDRRRLAADARAAMArVGLDSLD-----PDTLVGslgiGHQQMVEIARSLAGDCRVL 172
Cdd:PRK13637  95 QLFEE-TIEKDIAFG--PINLGLSEEEIENRVKRAMNI-VGLDYEDykdksPFELSG----GQKRRVAIAGVVAMEPKIL 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 173 ILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
240-466 1.52e-13

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: 72.78  E-value: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  240 ERLVALMA---GREIAEQAVHGTRTPGAPRLRVERLSRG-----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGA 311
Cdd:TIGR02868 305 ERIVEVLDaagPVAEGSAPAAGAVGLGKPTLELRDLSAGypgapPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  312 DAADGGTVSIGDPPRPAAirsPADAVRHGIALVSEDRKgeglLLPQSIAANLslgqlaRVARGGVVDGERENAL-AARQI 390
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSL---DQDEVRRRVSVCAQDAH----LFDTTVRENL------RLARPDATDEELWAALeRVGLA 451
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  391 DALRIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDAlAREGRAIVVVSSDL 466
Cdd:TIGR02868 452 DWLRALPDGLDTVLGEggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
9-247 1.65e-13

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 70.48  E-value: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   9 TPDTPtLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMrLAGAeyAPHSRAHAEa 87
Cdd:PRK11247   8 NQGTP-LLLNAVSKRYGErTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT--APLAEARED- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  88 lgVRMVMQELNLVPTLTVAENLFLDRLPHrfgvidrrrLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARS 164
Cdd:PRK11247  83 --TRLMFQDARLLPWKKVIDNVGLGLKGQ---------WRDAALQALAAVGLADRAnewPAALSG----GQKQRVALARA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 165 LAGDCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRL---VHVD--RIDAQP 238
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldLTVDlpRPRRRG 227

                 ....*....
gi 490656625 239 TERLVALMA 247
Cdd:PRK11247 228 SARLAELEA 236
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
26-208 1.73e-13

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: 69.44  E-value: 1.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALgvRMVMQELNLVPTLTV 105
Cdd:cd03231   13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL--LYLGHAPGIKTTLSV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENL-FLDRLPHRFGVIDrrrlaadaraAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAR 184
Cdd:cd03231   91 LENLrFWHADHSDEQVEE----------ALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
                        170       180
                 ....*....|....*....|....
gi 490656625 185 EVELLFDQIARLKADGVALVYISH 208
Cdd:cd03231  160 GVARFAEAMAGHCARGGMVVLTTH 183
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
15-232 2.10e-13

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 72.40  E-value: 2.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRlagaeyaphsrahaeaLGVRMV 93
Cdd:COG0488  316 LELEGLSKSYGDkTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK----------------LGETVK 379
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 M----QEL-NLVPTLTVAENL--------------FLDRLphrfgvidrrrlaadaraamarvGLDSLDPDTLVGSLGIG 154
Cdd:COG0488  380 IgyfdQHQeELDPDKTVLDELrdgapggteqevrgYLGRF-----------------------LFSGDDAFKPVGVLSGG 436
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 155 HQQMVEIARSLAGDCRVLILDEPT-----AMLTAREvELL--FdqiarlkaDGvALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:COG0488  437 EKARLALAKLLLSPPNVLLLDEPTnhldiETLEALE-EALddF--------PG-TVLLVSHDRYFLDRVATRILEFEDGG 506

                 ....*
gi 490656625 228 LVHVD 232
Cdd:COG0488  507 VREYP 511
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
28-229 2.20e-13

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: 69.09  E-value: 2.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGL--VAPTTGAMRLAG---AEYAPHSRAhaeALGVRMVMQELNLVPT 102
Cdd:cd03217   15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGediTDLPPEERA---RLGIFLAFQYPPEIPG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAEnlFLdrlphRFgvidrrrlaadaraamarVGldsldpdtlVGSLGiGHQQMVEIARSLAGDCRVLILDEPTAMLT 182
Cdd:cd03217   92 VKNAD--FL-----RY------------------VN---------EGFSG-GEKKRNEILQLLLLEPDLAILDEPDSGLD 136
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 490656625 183 AREVELLFDQIARLKADGVALVYISHRLEELARV-AQRVAVLRDGRLV 229
Cdd:cd03217  137 IDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIV 184
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
277-484 2.39e-13

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: 69.67  E-value: 2.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPpRPAAIRspaDAVRHGIALVSedrkGEGLLLP 356
Cdd:cd03267   36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRR---KKFLRRIGVVF----GQKTQLW 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLGQLARVARggvVDGERENALAARQIDALRIrARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:cd03267  108 WDLPVIDSFYLLAAIYD---LPPARFKKRLDELSELLDL-EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490656625 437 IDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03267  184 LDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
266-486 2.46e-13

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: 69.06  E-value: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 266 RLRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAirSPADAVrhgialVS 345
Cdd:cd03298    2 RLDKIRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA--PPADRP------VS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 346 EDRKGEGLLLPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRARGpaqpvaELSGGNQQKVAIGRWLGRDM 425
Cdd:cd03298   74 MLFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPG------ELSGGERQRVALARVLVRDK 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 426 GVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:cd03298  148 PVLLLDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
267-487 2.51e-13

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: 69.67  E-value: 2.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSR--GD-AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI------GDPPRpaairspadav 337
Cdd:cd03299    1 LKVENLSKdwKEfKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLngkditNLPPE----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 338 RHGIALVSEDRKgeglLLPQ-SIAANLSLGqlARVARGGVVDGEREnalaARQIDA-LRIRA---RGPAQpvaeLSGGNQ 412
Cdd:cd03299   70 KRDISYVPQNYA----LFPHmTVYKNIAYG--LKKRKVDKKEIERK----VLEIAEmLGIDHllnRKPET----LSGGEQ 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 413 QKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVV-VSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:cd03299  136 QRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQV 211
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
28-210 2.69e-13

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 69.76  E-value: 2.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRlagaeyaphsraHAEALGVRMVMQELNLVPTLTVAE 107
Cdd:PRK09544  19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------------RNGKLRIGYVPQKLYLDTTLPLTV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NLFLdRLphRFGVIDRRRLAADARAAMARVgldsldPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVE 187
Cdd:PRK09544  87 NRFL-RL--RPGTKKEDILPALKRVQAGHL------IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
                        170       180
                 ....*....|....*....|....
gi 490656625 188 LLFDQIARLKAD-GVALVYISHRL 210
Cdd:PRK09544 158 ALYDLIDQLRRElDCAVLMVSHDL 181
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
28-231 2.82e-13

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 69.56  E-value: 2.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVapttgamrlagaEYAPHSRAHAEAL----------------GVR 91
Cdd:PRK14247  18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLI------------ELYPEARVSGEVYldgqdifkmdvielrrRVQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  92 MVMQELNLVPTLTVAEN----LFLDRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTlvGSLGIGHQQMVEIARSLAG 167
Cdd:PRK14247  86 MVFQIPNPIPNLSIFENvalgLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPA--GKLSGGQQQRLCIARALAF 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 168 DCRVLILDEPTAML----TAReVELLFdqiARLKADgVALVYISHRLEELARVAQRVAVLRDGRLVHV 231
Cdd:PRK14247 164 QPEVLLADEPTANLdpenTAK-IESLF---LELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
cbiO PRK13641
energy-coupling factor transporter ATPase;
29-229 3.64e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 69.86  E-value: 3.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHaealGVRMVMQELNLV---PTLTV 105
Cdd:PRK13641  23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNK----NLKKLRKKVSLVfqfPEAQL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLFLDRL---PHRFGVIDrRRLAADARAAMARVGLD----SLDPDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPT 178
Cdd:PRK13641  99 FENTVLKDVefgPKNFGFSE-DEAKEKALKWLKKVGLSedliSKSPFELSG----GQMRRVAIAGVMAYEPEILCLDEPA 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490656625 179 AMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
29-232 3.67e-13

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 69.42  E-value: 3.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  29 LDDVSLALYPGEALALTGENGAGKSTLSKIV--AGLVAP---TTGAMRLAGAE-YAPHSRAHAEALGVRMVMQELNLVPt 102
Cdd:PRK14239  21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNiYSPRTDTVDLRKEIGMVFQQPNPFP- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENLFLD-RLPhrfGVIDRRRLAADARAAMARVGL-----DSLDpDTLVGSLGiGHQQMVEIARSLAGDCRVLILDE 176
Cdd:PRK14239 100 MSIYENVVYGlRLK---GIKDKQVLDEAVEKSLKGASIwdevkDRLH-DSALGLSG-GQQQRVCIARVLATSPKIILLDE 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 177 PTAML---TAREVEllfDQIARLKADgVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:PRK14239 175 PTSALdpiSAGKIE---ETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYN 229
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
12-214 3.83e-13

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 68.97  E-value: 3.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  12 TPTLVVTGIG-KTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSrahAEALgv 90
Cdd:PRK10247   5 SPLLQLQNVGyLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK---PEIY-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  91 RMVMQELNLVPTL---TVAENL---------------FLDRLpHRFGVidrrrlaadaraamarvgldsldPDTL----V 148
Cdd:PRK10247  80 RQQVSYCAQTPTLfgdTVYDNLifpwqirnqqpdpaiFLDDL-ERFAL-----------------------PDTIltknI 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 149 GSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELA 214
Cdd:PRK10247 136 AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEIN 202
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
15-227 4.39e-13

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: 66.70  E-value: 4.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGamrlagaeyaphsrahaealgvrmv 93
Cdd:cd03221    1 IELENLSKTYGGkLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG------------------------- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 mqELNLVPTLTVAenlFLDRLphrfgvidrrrlaadaraamarvgldsldpdtlvgSLGighQQM-VEIARSLAGDCRVL 172
Cdd:cd03221   56 --IVTWGSTVKIG---YFEQL-----------------------------------SGG---EKMrLALAKLLLENPNLL 92
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 173 ILDEPTAMLTAREVELLFDQIARLKAdgvALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:cd03221   93 LLDEPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIELEDGK 144
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
27-229 4.84e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 69.35  E-value: 4.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHS-----RAHAEalgvrMVMQELN--L 99
Cdd:PRK13633  24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlwdiRNKAG-----MVFQNPDnqI 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 100 VPTLT---VA---ENLFLDRLPHRFGVIDRRRLaadaraamarVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDCR 170
Cdd:PRK13633  99 VATIVeedVAfgpENLGIPPEEIRERVDESLKK----------VGMYEYRrhaPHLLSG----GQKQRVAIAGILAMRPE 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 171 VLILDEPTAMLTA---REVellFDQIARL-KADGVALVYISHRLEELARvAQRVAVLRDGRLV 229
Cdd:PRK13633 165 CIIFDEPTAMLDPsgrREV---VNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
12-226 4.94e-13

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: 72.35  E-value: 4.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625    12 TPTLVVTGIGKTY---AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHsrahaeal 88
Cdd:TIGR01257 1935 TDILRLNELTKVYsgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN-------- 2006
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625    89 gVRMVMQELNLVPTLTVAENLFLDR----LPHRFGVIDRRRLAADARAAMARVGLdSLDPDTLVGSLGIGHQQMVEIARS 164
Cdd:TIGR01257 2007 -ISDVHQNMGYCPQFDAIDDLLTGRehlyLYARLRGVPAEEIEKVANWSIQSLGL-SLYADRLAGTYSGGNKRKLSTAIA 2084
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625   165 LAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDG 226
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
281-484 5.13e-13

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 69.01  E-value: 5.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 281 VSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIrspadAVRHGIALVSEDRKGEGL------L 354
Cdd:PRK11264  22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTAR-----SLSQQKGLIRQLRQHVGFvfqnfnL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LPQSIAanlslgqLARVARGGV-VDGE-RENALA-ARQIDA-LRIRARGPAQPvAELSGGNQQKVAIGRWLGRDMGVLLF 430
Cdd:PRK11264  97 FPHRTV-------LENIIEGPViVKGEpKEEATArARELLAkVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILF 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490656625 431 DEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
277-474 5.72e-13

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 69.14  E-value: 5.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRspadavRHGIALV--SEDRKGEGLL 354
Cdd:PRK15056  22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ------KNLVAYVpqSEEVDWSFPV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LPQSIAANLSLGQLARVARGGVVDGERENALAARqIDALRIRARgpaqPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:PRK15056  96 LVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALAR-VDMVEFRHR----QIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 490656625 435 RGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICD 474
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
28-230 6.10e-13

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: 68.33  E-value: 6.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPhsrahaeaLGVRMVMQelnlvPTLTVAE 107
Cdd:cd03220   37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL--------LGLGGGFN-----PELTGRE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NLFLDrlphrfGVIdrrrlaadaraamarVGLDSLDPDTLVGSL----GIG---HQQMVE-----IAR-----SLAGDCR 170
Cdd:cd03220  104 NIYLN------GRL---------------LGLSRKEIDEKIDEIiefsELGdfiDLPVKTyssgmKARlafaiATALEPD 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 171 VLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:cd03220  163 ILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
21-229 6.99e-13

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 68.66  E-value: 6.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  21 GKTYAEPVlddvSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAP-HSRAHAEAlgVRMVMQELNL 99
Cdd:PRK10575  23 GRTLLHPL----SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARK--VAYLPQQLPA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 100 VPTLTVAENLFLDRLP-H----RFGVIDrrrlAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLIL 174
Cdd:PRK10575  97 AEGMTVRELVAIGRYPwHgalgRFGAAD----REKVEEAISLVGLKPL-AHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 175 DEPTAML-TAREVELLfDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK10575 172 DEPTSALdIAHQVDVL-ALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
28-208 7.94e-13

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


Pssm-ID: 130234 [Multi-domain]  Cd Length: 190  Bit Score: 67.06  E-value: 7.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYApHSRAHAEAL--GVRMVMQELNlvptltv 105
Cdd:TIGR01166   7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLD-YSRKGLLERrqRVGLVFQDPD------- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  106 aENLFLDRL-------PHRFGVIDRRRLAADARAAMArVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPT 178
Cdd:TIGR01166  79 -DQLFAADVdqdvafgPLNLGLSEAEVERRVREALTA-VGASGLR-ERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
                         170       180       190
                  ....*....|....*....|....*....|
gi 490656625  179 AMLTAREVELLFDQIARLKADGVALVYISH 208
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTH 185
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
271-485 8.77e-13

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: 67.60  E-value: 8.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 271 RLSRGDAVRDVSFDVRAGeIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairspADAVRHGIALvsedRKG 350
Cdd:cd03264    9 RYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG----------QDVLKQPQKL----RRR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 351 EGLLlPQ--SIAANLS-LGQLARVARGGVVDGERENALAARQIDALRIRARGpAQPVAELSGGNQQKVAIGRWLGRDMGV 427
Cdd:cd03264   74 IGYL-PQefGVYPNFTvREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSI 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 428 LLFDEPTRGIDVGAKFDIYALLDALAREgrAIVVVSSDLRE-LMLICDRIGVMSAGRMH 485
Cdd:cd03264  152 LIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEdVESLCNQVAVLNKGKLV 208
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
277-465 1.03e-12

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: 67.43  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSEDRKgegLLLP 356
Cdd:cd03292   16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQDFR---LLPD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANlslgqlarVARGGVVDGERENALAARQIDALR---IRARGPAQPvAELSGGNQQKVAIGRWLGRDMGVLLFDEP 433
Cdd:cd03292   93 RNVYEN--------VAFALEVTGVPPREIRKRVPAALElvgLSHKHRALP-AELSGGEQQRVAIARAIVNSPTILIADEP 163
                        170       180       190
                 ....*....|....*....|....*....|..
gi 490656625 434 TRGIDVGAKFDIYALLDALAREGRAIVVVSSD 465
Cdd:cd03292  164 TGNLDPDTTWEIMNLLKKINKAGTTVVVATHA 195
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
19-244 1.24e-12

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 69.29  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  19 GIGKTYAEPVLD-DVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGA---EYAPHSRahaealGVRMVM 94
Cdd:PRK11000   8 NVTKAYGDVVISkDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAER------GVGMVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  95 QELNLVPTLTVAENLfldrlphRFGV----IDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAG 167
Cdd:PRK11000  82 QSYALYPHLSVAENM-------SFGLklagAKKEEINQRVNQVAEVLQLAHLldrKPKALSG----GQRQRVAIGRTLVA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDR---IDAQPTERLV 243
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKpleLYHYPANRFV 230

                 .
gi 490656625 244 A 244
Cdd:PRK11000 231 A 231
cbiO PRK13646
energy-coupling factor transporter ATPase;
21-229 1.41e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 68.27  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  21 GKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYapHSRAHAEALgvRMVMQELNLV 100
Cdd:PRK13646  15 GTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITI--THKTKDKYI--RPVRKRIGMV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 101 PTLTVAEnLFLDRL-------PHRFGvIDRRRLAADARAAMARVGLD----SLDPDTLVGslgiGHQQMVEIARSLAGDC 169
Cdd:PRK13646  91 FQFPESQ-LFEDTVereiifgPKNFK-MNLDEVKNYAHRLLMDLGFSrdvmSQSPFQMSG----GQMRKIAIVSILAMNP 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 170 RVLILDEPTAML---TAREVELLFDQIArlKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13646 165 DIIVLDEPTAGLdpqSKRQVMRLLKSLQ--TDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
29-230 1.55e-12

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 68.58  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeYAPHSR--AHAEALGVrmVM-QELNLVPTLTV 105
Cdd:COG4586   38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG--YVPFKRrkEFARRIGV--VFgQRSQLWWDLPA 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLFLDRLPHRfgvIDRRRLAADAraamarvgldsldpDTLVGSLGIGH------------QQM-VEIARSLAGDCRVL 172
Cdd:COG4586  114 IDSFRLLKAIYR---IPDAEYKKRL--------------DELVELLDLGElldtpvrqlslgQRMrCELAAALLHRPKIL 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 173 ILDEPT------AMLTAREvellFdqIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:COG4586  177 FLDEPTigldvvSKEAIRE----F--LKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRIIY 235
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
280-463 1.59e-12

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 67.43  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 280 DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpAAIRSPADAVRhgialvsEDRKGEGL------ 353
Cdd:PRK09493  19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG----LKVNDPKVDER-------LIRQEAGMvfqqfy 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 LLPQSIA-ANLSLGQLaRVARGGVVDGERenaLAARQIDALRIRARGPAQPvAELSGGNQQKVAIGRWLGRDMGVLLFDE 432
Cdd:PRK09493  88 LFPHLTAlENVMFGPL-RVRGASKEEAEK---QARELLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKLMLFDE 162
                        170       180       190
                 ....*....|....*....|....*....|.
gi 490656625 433 PTRGIDVGAKFDIYALLDALAREGRAIVVVS 463
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVT 193
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
19-465 1.77e-12

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 69.76  E-value: 1.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  19 GIGKTY--AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLagaeyaphsrahAEALGVRMVMQE 96
Cdd:PRK11819  11 RVSKVVppKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP------------APGIKVGYLPQE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  97 LNLVPTLTVAENLF---------LDRLPH---RFGVIDRRRLAADARAAMARVGLDSLD-------------------PD 145
Cdd:PRK11819  79 PQLDPEKTVRENVEegvaevkaaLDRFNEiyaAYAEPDADFDALAAEQGELQEIIDAADawdldsqleiamdalrcppWD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 146 TLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAdgvALVYISHRLEELARVAQRVAVLRD 225
Cdd:PRK11819 159 AKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG---TVVAVTHDRYFLDNVAGWILELDR 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 226 GRLV------------HVDRI---DAQPTERLVALMA----------GR------------EIAEQAVHGTRT------P 262
Cdd:PRK11819 236 GRGIpwegnysswleqKAKRLaqeEKQEAARQKALKRelewvrqspkARqakskarlaryeELLSEEYQKRNEtneifiP 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 263 GAPRL-----RVERLSR--GDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGdpprpaairsp 333
Cdd:PRK11819 316 PGPRLgdkviEAENLSKsfGDRLliDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG----------- 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 334 aDAVRhgIALVSEDRKgeglllpqSIAANLSLGQLarvarggVVDGERENALAARQIDAlriRA-------RGPAQ--PV 404
Cdd:PRK11819 385 -ETVK--LAYVDQSRD--------ALDPNKTVWEE-------ISGGLDIIKVGNREIPS---RAyvgrfnfKGGDQqkKV 443
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 405 AELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAkfdIYALLDALAREGRAIVVVSSD 465
Cdd:PRK11819 444 GVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET---LRALEEALLEFPGCAVVISHD 501
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
29-238 1.86e-12

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 68.45  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL--GVRMVMQ----ELN---- 98
Cdd:PRK11308  31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqKIQIVFQnpygSLNprkk 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  99 ---------LVPT-LTVAENL---------------FLDRLPHRFGvidrrrlaadaraamarvGldsldpdtlvgslgi 153
Cdd:PRK11308 111 vgqileeplLINTsLSAAERRekalammakvglrpeHYDRYPHMFS------------------G--------------- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 154 GHQQMVEIARSLAGDCRVLILDEPTAML----TAREVELLFDqiarLKAD-GVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALdvsvQAQVLNLMMD----LQQElGLSYVFISHDLSVVEHIADEVMVMYLGRC 233
                        250
                 ....*....|...
gi 490656625 229 VHV---DRIDAQP 238
Cdd:PRK11308 234 VEKgtkEQIFNNP 246
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
277-513 1.91e-12

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 67.21  E-value: 1.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHGIALVSEDRKgegLLLP 356
Cdd:PRK11614  20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG--KDITDWQTAKIMREAVAIVPEGRR---VFSR 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLGqlarvarGGVVDGERENALAARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:PRK11614  95 MTVEENLAMG-------GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 437 IDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGrmHAVFERGGwtqDALLgaafAGYARRDAAL 513
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENG--HVVLEDTG---DALL----ANEAVRSAYL 235
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
29-229 1.98e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 67.74  E-value: 1.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRA-HAEAL--GVRMVMQ--ELNLVPTl 103
Cdd:PRK13634  23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkKLKPLrkKVGIVFQfpEHQLFEE- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLFLDrlPHRFGVIDrrrlAADARAAMARVGLDSLDPDTLVGS---LGIGHQQMVEIARSLAGDCRVLILDEPTAM 180
Cdd:PRK13634 102 TVEKDICFG--PMNFGVSE----EDAKQKAREMIELVGLPEELLARSpfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490656625 181 LTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
17-230 2.08e-12

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 67.35  E-value: 2.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  17 VTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVaptTG-----------------AMRLAGAeyA 78
Cdd:PRK09984   7 VEKLAKTFNQhQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI---TGdksagshiellgrtvqrEGRLARD--I 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  79 PHSRAHAEAlgvrmVMQELNLVPTLTVAENLFLDRL---PHRFGVID--RRRLAADARAAMARVGLDSLdPDTLVGSLGI 153
Cdd:PRK09984  82 RKSRANTGY-----IFQQFNLVNRLSVLENVLIGALgstPFWRTCFSwfTREQKQRALQALTRVGMVHF-AHQRVSTLSG 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 154 GHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFY 233
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
278-483 2.11e-12

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: 66.80  E-value: 2.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD---PPRPAAIRSpadavRHGIALvsedrkgegll 354
Cdd:cd03218   16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqdiTKLPMHKRA-----RLGIGY----------- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LPQ--SIAANLSLGQ--LARVARGGVVDGER----ENALAARQIDALRirargpAQPVAELSGGNQQKVAIGRWLGRDMG 426
Cdd:cd03218   80 LPQeaSIFRKLTVEEniLAVLEIRGLSKKEReeklEELLEEFHITHLR------KSKASSLSGGERRRVEIARALATNPK 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 427 VLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03218  154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGK 210
cbiO PRK13643
energy-coupling factor transporter ATPase;
277-489 2.13e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 67.84  E-value: 2.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPA-DAVRHGIALVSEdrKGEGLLL 355
Cdd:PRK13643  21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEiKPVRKKVGVVFQ--FPESQLF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 PQSIAANLSLGqlarvARGGVVDGERENALAARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:PRK13643  99 EETVLKDVAFG-----PQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 436 GIDVGAKFDIYALLDALAREGRAIVVVS------SDLRELMLICDRIGVMSAGRMHAVFE 489
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVThlmddvADYADYVYLLEKGHIISCGTPSDVFQ 233
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
28-236 2.14e-12

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 66.83  E-value: 2.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA--PHSRAHAEALGVrmVMQELNLVPTLTV 105
Cdd:PRK11614  20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREAVAI--VPEGRRVFSRMTV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENL-----------FLDRLPHRFGVIDRRRLAADARAamarvgldsldpdtlvGSLGIGHQQMVEIARSLAGDCRVLIL 174
Cdd:PRK11614  98 EENLamggffaerdqFQERIKWVYELFPRLHERRIQRA----------------GTMSGGEQQMLAIGRALMSQPRLLLL 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 175 DEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDA 236
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDA 223
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
4-210 2.16e-12

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: 69.31  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625    4 TDPDSTPDTPTLVVTGIGKTY--AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeYAPHS 81
Cdd:TIGR02868 324 AAGAVGLGKPTLELRDLSAGYpgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG--VPVSS 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   82 RAHAE-ALGVRMVMQELNLVPTlTVAENLfldrlphRFGVIDRRRLAADARAAMARVG--LDSLDP--DTLVGSLGI--- 153
Cdd:TIGR02868 402 LDQDEvRRRVSVCAQDAHLFDT-TVRENL-------RLARPDATDEELWAALERVGLAdwLRALPDglDTVLGEGGArls 473
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625  154 -GHQQMVEIARSLAGDCRVLILDEPTAMLTAR-EVELLFDQIARLkaDGVALVYISHRL 210
Cdd:TIGR02868 474 gGERQRLALARALLADAPILLLDEPTEHLDAEtADELLEDLLAAL--SGRTVVLITHHL 530
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
280-476 2.29e-12

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 67.06  E-value: 2.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 280 DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSigdppRPAAIRspadavrhgIALVsedrkgeglllPQSI 359
Cdd:PRK09544  22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----RNGKLR---------IGYV-----------PQKL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 360 AAN----LSLGQLARVaRGGVVDGERENALAARQIDALRirargpAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:PRK09544  77 YLDttlpLTVNRFLRL-RPGTKKEDILPALKRVQAGHLI------DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 490656625 436 GIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRI 476
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
277-484 2.46e-12

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: 66.94  E-value: 2.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRS-PADAVRHGIALVSEDRkgeGLLL 355
Cdd:cd03295   16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGED----IREqDPVELRRKIGYVIQQI---GLFP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 PQSIAANLSL-GQLARVARGGVVDGEREnALAARQIDALRIRARGPAqpvaELSGGNQQKVAIGRWLGRDMGVLLFDEPt 434
Cdd:cd03295   89 HMTVEENIALvPKLLKWPKEKIRERADE-LLALVGLDPAEFADRYPH----ELSGGQQQRVGVARALAADPPLLLMDEP- 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 435 rgidVGAkfdiyalLDALARE-------------GRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03295  163 ----FGA-------LDPITRDqlqeefkrlqqelGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
21-244 2.50e-12

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 67.43  E-value: 2.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  21 GKTyaepVLDDVSLAlYPGEAL-ALTGENGAGKSTLSKIVAGLVAPTTGA-----MRLAGAEYAPHSRAHAEALGVRMVM 94
Cdd:PRK14271  33 GKT----VLDQVSMG-FPARAVtSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVLEFRRRVGMLF 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  95 QELNLVPtLTVAENLFLDRLPHRfgVIDRRRLAADARAAMARVGLDSLDPDTLVGS---LGIGHQQMVEIARSLAGDCRV 171
Cdd:PRK14271 108 QRPNPFP-MSIMDNVLAGVRAHK--LVPRKEFRGVAQARLTEVGLWDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEV 184
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 172 LILDEPTAMLTAREVELLfDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVhvdriDAQPTERLVA 244
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLV-----EEGPTEQLFS 251
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
273-487 2.54e-12

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 68.52  E-value: 2.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 273 SRGDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD------PPRpaairspadavRHGIALV 344
Cdd:PRK11000  12 AYGDVVisKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndvPPA-----------ERGVGMV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 345 SEDRKgeglLLPQ-SIAANLSLG-QLARVARGgVVDGERENALAARQIDALRIRargpaQPVAeLSGGNQQKVAIGRWLG 422
Cdd:PRK11000  81 FQSYA----LYPHlSVAENMSFGlKLAGAKKE-EINQRVNQVAEVLQLAHLLDR-----KPKA-LSGGQRQRVAIGRTLV 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 423 RDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQV 215
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
26-209 2.97e-12

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 65.74  E-value: 2.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGvrMVMQELNLVPTLTV 105
Cdd:PRK13540  14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLC--FVGHRSGINPYLTL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLFLDrlphrfgvIDRRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTARE 185
Cdd:PRK13540  92 RENCLYD--------IHFSPGAVGITELCRLFSLEHL-IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
                        170       180
                 ....*....|....*....|....
gi 490656625 186 VELLFDQIARLKADGVALVYISHR 209
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSHQ 186
cbiO PRK13643
energy-coupling factor transporter ATPase;
24-229 4.80e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 66.68  E-value: 4.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  24 YAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRaHAEALGVRMVMQELNLVPTL 103
Cdd:PRK13643  17 FASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSK-QKEIKPVRKKVGVVFQFPES 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLFLDRL---PHRFGvIDRRRLAADARAAMARVGLDSLDPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAM 180
Cdd:PRK13643  96 QLFEETVLKDVafgPQNFG-IPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490656625 181 LTAR---EVELLFDQIARlkaDGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13643 175 LDPKariEMMQLFESIHQ---SGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
265-483 5.51e-12

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 67.55  E-value: 5.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLSRG----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIG--DPPRPAAIRSPADAVR 338
Cdd:PRK11607  18 PLLEIRNLTKSfdgqHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvDLSHVPPYQRPINMMF 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 339 HGIALVSEdrkgegLLLPQSIAANLSLGQLARvargGVVDGERENALAArqIDALRIRARGPAQpvaeLSGGNQQKVAIG 418
Cdd:PRK11607  98 QSYALFPH------MTVEQNIAFGLKQDKLPK----AEIASRVNEMLGL--VHMQEFAKRKPHQ----LSGGQRQRVALA 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 419 RWLGRDMGVLLFDEPTRGIDVGAKFDI-YALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
276-438 5.69e-12

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 65.80  E-value: 5.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD-------PPRPAAIRspadAVRHGIALVSEDR 348
Cdd:COG4161   16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqKPSEKAIR----LLRQKVGMVFQQY 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 349 KgeglLLPQ-SIAANLS------LGQLARVARggvvdgERENALAARqidaLRIRARGPAQPVAeLSGGNQQKVAIGRWL 421
Cdd:COG4161   92 N----LWPHlTVMENLIeapckvLGLSKEQAR------EKAMKLLAR----LRLTDKADRFPLH-LSGGQQQRVAIARAL 156
                        170
                 ....*....|....*..
gi 490656625 422 GRDMGVLLFDEPTRGID 438
Cdd:COG4161  157 MMEPQVLLFDEPTAALD 173
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
279-486 8.30e-12

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: 65.15  E-value: 8.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 279 RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI--------GDPPRpAAIRSpadavRH-GI-------- 341
Cdd:COG4181   29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLagqdlfalDEDAR-ARLRA-----RHvGFvfqsfqll 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 342 ----ALvsedrkgEGLLLPQSIAANLSLGQLARVARGGVVDGERENALaarqidalrirargPAQpvaeLSGGNQQKVAI 417
Cdd:COG4181  103 ptltAL-------ENVMLPLELAGRRDARARARALLERVGLGHRLDHY--------------PAQ----LSGGEQQRVAL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 418 GRWLGRDMGVLLFDEPTRGID--VGAKfdIYALLDALARE-GRAIVVVSSDLrELMLICDRIGVMSAGRMHA 486
Cdd:COG4181  158 ARAFATEPAILFADEPTGNLDaaTGEQ--IIDLLFELNRErGTTLVLVTHDP-ALAARCDRVLRLRAGRLVE 226
cbiO PRK13640
energy-coupling factor transporter ATPase;
26-229 8.44e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 65.98  E-value: 8.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAP--------TTGAMRLaGAEYAPHSRahaEALGVrmVMQEL 97
Cdd:PRK13640  20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskiTVDGITL-TAKTVWDIR---EKVGI--VFQNP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  98 -NLVPTLTVAENLfldrlphRFGV----IDRRRLAADARAAMARVG-LDSLD--PDTLVGslgiGHQQMVEIARSLAGDC 169
Cdd:PRK13640  94 dNQFVGATVGDDV-------AFGLenraVPRPEMIKIVRDVLADVGmLDYIDsePANLSG----GQKQRVAIAGILAVEP 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 170 RVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEElARVAQRVAVLRDGRLV 229
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDE-ANMADQVLVLDDGKLL 222
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
27-229 9.46e-12

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 64.87  E-value: 9.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGA---EYAPHS-RAHaealgVRMVMQELNLVPT 102
Cdd:cd03249   17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirDLNLRWlRSQ-----IGLVSQEPVLFDG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 lTVAENL-----------------------FLDRLPHRFgvidrrrlaadaraamarvgldsldpDTLVGSLGI----GH 155
Cdd:cd03249   92 -TIAENIrygkpdatdeeveeaakkanihdFIMSLPDGY--------------------------DTLVGERGSqlsgGQ 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 156 QQMVEIARSLAGDCRVLILDEPTAMLTA---REVELLFDQIARlkadGVALVYISHRLEELaRVAQRVAVLRDGRLV 229
Cdd:cd03249  145 KQRIAIARALLRNPKILLLDEATSALDAeseKLVQEALDRAMK----GRTTIVIAHRLSTI-RNADLIAVLQNGQVV 216
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
278-484 9.65e-12

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 65.48  E-value: 9.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSED-------RKG 350
Cdd:PRK10419  28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDsisavnpRKT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 351 EGLLLPQSIAANLSLGQLARVARggvvdgeRENALAARQIDAlRIRARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLF 430
Cdd:PRK10419 108 VREIIREPLRHLLSLDKAERLAR-------ASEMLRAVDLDD-SVLDKRPPQ----LSGGQLQRVCLARALAVEPKLLIL 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 431 DEPTRGIDVGAKFDIYALLDAL-AREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
278-484 1.04e-11

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: 64.11  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLV--YGADAADGGTVSIGDPPRPAairspaDAVRHGIALVSEDRkgegLLL 355
Cdd:cd03213   25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK------RSFRKIIGYVPQDD----ILH 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 PQsiaanlslgqlarvarggvvdgerenaLAARQidALRIRA--RGpaqpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEP 433
Cdd:cd03213   95 PT---------------------------LTVRE--TLMFAAklRG-------LSGGERKRVSIALELVSNPSLLFLDEP 138
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 434 TRGIDVGAKFDIYALLDALAREGRAIVVV----SSDLRELmliCDRIGVMSAGRM 484
Cdd:cd03213  139 TSGLDSSSALQVMSLLRRLADTGRTIICSihqpSSEIFEL---FDKLLLLSQGRV 190
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
265-483 1.12e-11

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: 64.38  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLS-------RGD----AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD---------- 323
Cdd:COG4778    3 TLLEVENLSktftlhlQGGkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwvdlaqa 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 324 PPRP-AAIRspadavRHGIALVSEdrkgegLL--LPQsIAAnlslgqLARVARGGVVDG-ERENAL--AARQIDALRIRA 397
Cdd:COG4778   83 SPREiLALR------RRTIGYVSQ------FLrvIPR-VSA------LDVVAEPLLERGvDREEARarARELLARLNLPE 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 398 RGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIG 477
Cdd:COG4778  144 RLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVV 223

                 ....*.
gi 490656625 478 VMSAGR 483
Cdd:COG4778  224 DVTPFS 229
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
14-229 1.27e-11

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 64.77  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  14 TLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEY-APHSRAHAEAL--- 88
Cdd:PRK11264   3 AIEVKNLVKKFhGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLirq 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  89 ---GVRMVMQELNLVPTLTVAENLFldRLPHRFGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSL 165
Cdd:PRK11264  83 lrqHVGFVFQNFNLFPHRTVLENII--EGPVIVKGEPKEEATARARELLAKVGLAGKE-TSYPRRLSGGQQQRVAIARAL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 166 AGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
267-485 1.28e-11

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 64.13  E-value: 1.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSRG-----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGI 341
Cdd:PRK10908   2 IRFEHVSKAylggrQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 342 ALVSEDRKgegLLLPQSIAANLSLGQLARVARGgvvDGERENALAArqIDALRIRARGPAQPVaELSGGNQQKVAIGRWL 421
Cdd:PRK10908  82 GMIFQDHH---LLMDRTVYDNVAIPLIIAGASG---DDIRRRVSAA--LDKVGLLDKAKNFPI-QLSGGEQQRVGIARAV 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 422 GRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMH 485
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
276-501 1.39e-11

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: 64.43  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPAdAVRHGIALVSEdrkgEGLLL 355
Cdd:cd03252   16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG--HDLALADPA-WLRRQVGVVLQ----ENVLF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 PQSIAANLSLGQLArvarggvVDGER--ENALAARQIDALRIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLL 429
Cdd:cd03252   89 NRSIRDNIALADPG-------MSMERviEAAKLAGAHDFISELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILI 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 430 FDEPTRGIDVGAKFDIYALLDALArEGRAIVVVSSDLRELMlICDRIGVMSAGRmhaVFERGgwTQDALLGA 501
Cdd:cd03252  162 FDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVK-NADRIIVMEKGR---IVEQG--SHDELLAE 226
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
43-234 1.41e-11

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 66.05  E-value: 1.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  43 ALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG-----AE----YAPHSRahaealGVRMVMQELNLVPTLTVAENLfldr 113
Cdd:PRK11144  28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdAEkgicLPPEKR------RIGYVFQDARLFPHYKVRGNL---- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 114 lphRFGVidrrrLAADARAAMARVGLDSLDP--DTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTA-REVELLf 190
Cdd:PRK11144  98 ---RYGM-----AKSMVAQFDKIVALLGIEPllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLpRKRELL- 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 490656625 191 DQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVDRI 234
Cdd:PRK11144 169 PYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
21-229 1.44e-11

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 66.79  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  21 GKTYAEPVlddvSLALYPGEALALTGENGAGKSTLSKIVAGLvAPTTGAMRLAGAEYA----PHSRAHAEALGvrmvmQE 96
Cdd:PRK11174 362 GKTLAGPL----NFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELReldpESWRKHLSWVG-----QN 431
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  97 lnlvPTL---TVAENL-----------------------FLDRLPHrfgvidrrrlaadaraamarvGLDSLDPDTLVGs 150
Cdd:PRK11174 432 ----PQLphgTLRDNVllgnpdasdeqlqqalenawvseFLPLLPQ---------------------GLDTPIGDQAAG- 485
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 151 LGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVyISHRLEELARVAQrVAVLRDGRLV 229
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLM-VTHQLEDLAQWDQ-IWVMQDGQIV 562
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
267-483 1.68e-11

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 65.52  E-value: 1.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVE-RLSRGD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADG---GTVS-----IGDPPRPAAIRSPAD 335
Cdd:PRK09473  18 LRVTfSTPDGDvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATfngreILNLPEKELNKLRAE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 336 AvrhgIALVSEDrkgeglllPQ-SIAANLSLG-QLARV--ARGGVVDGERENAlAARQIDALRI---RARGPAQPvAELS 408
Cdd:PRK09473  98 Q----ISMIFQD--------PMtSLNPYMRVGeQLMEVlmLHKGMSKAEAFEE-SVRMLDAVKMpeaRKRMKMYP-HEFS 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 409 GGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
29-229 1.78e-11

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 63.74  E-value: 1.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL--GVRMVMQELNLVPTLTVA 106
Cdd:PRK10908  18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLrrQIGMIFQDHHLLMDRTVY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 107 ENLfldRLPHRFGVIDRRRLAADARAAMARVGLdsLD-----PDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAML 181
Cdd:PRK10908  98 DNV---AIPLIIAGASGDDIRRRVSAALDKVGL--LDkaknfPIQLSG----GEQQRVGIARAVVNKPAVLLADEPTGNL 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490656625 182 T---AREVELLFDQIARLkadGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK10908 169 DdalSEGILRLFEEFNRV---GVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
29-262 2.06e-11

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 64.37  E-value: 2.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALgVRMVMQEL-NLVPTLTVAE 107
Cdd:PRK13647  21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK-VGLVFQDPdDQVFSSTVWD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NLFLDrlPHRFGvIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVE 187
Cdd:PRK13647 100 DVAFG--PVNMG-LDKDEVERRVEEALKAVRMWDFR-DKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 188 LLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVhvdridaqpTERLVALMAGREIAEQAvhGTRTP 262
Cdd:PRK13647 176 TLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL---------AEGDKSLLTDEDIVEQA--GLRLP 239
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
277-484 2.18e-11

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 65.83  E-value: 2.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYgadaadggtvSIGDPPRPAAIRSPADAVRHGIALVSEDRKGEGLLLP 356
Cdd:PRK10070  43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLN----------RLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVF 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLGQLARVARG----GVVDGER-ENALAARQIDALRIRARGPAQpvaELSGGNQQKVAIGRWLGRDMGVLLFD 431
Cdd:PRK10070 113 QSFALMPHMTVLDNTAFGmelaGINAEERrEKALDALRQVGLENYAHSYPD---ELSGGMRQRVGLARALAINPDILLMD 189
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490656625 432 EPTRGIDVGAKFDIY-ALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK10070 190 EAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
240-508 2.19e-11

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


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 66.38  E-value: 2.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 240 ERLVALMA-GREIAEQavhgtrtPGAPRLRVERLS-RGDAV-----------RDVSFDVRAGEIFGISGLIGAGRTELLR 306
Cdd:COG5265  330 ERMFDLLDqPPEVADA-------PDAPPLVVGGGEvRFENVsfgydperpilKGVSFEVPAGKTVAIVGPSGAGKSTLAR 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 307 LVYGADAADGGTVSIGDPPrpaaIRS-PADAVRHGIALVSEDRkgegLLLPQSIAANLSLGqlarvaRGGVVDGERENAL 385
Cdd:COG5265  403 LLFRFYDVTSGRILIDGQD----IRDvTQASLRAAIGIVPQDT----VLFNDTIAYNIAYG------RPDASEEEVEAAA 468
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 386 AARQIDALrIRA--RGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAReGRAI 459
Cdd:COG5265  469 RAAQIHDF-IESlpDGYDTRVGErglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTT 546
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 490656625 460 VVVSSDLRELMlICDRIGVMSAGRmhaVFERGgwTQDALLgaAFAG-YAR 508
Cdd:COG5265  547 LVIAHRLSTIV-DADEILVLEAGR---IVERG--THAELL--AQGGlYAQ 588
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
279-483 2.39e-11

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 63.86  E-value: 2.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 279 RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD---PPRPAAIRspadAVRHGIALVsedrkgeglll 355
Cdd:COG1126   18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedlTDSKKDIN----KLRRKVGMV----------- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 PQS--------IAANLSLGQlaRVARGgvVDGERENALAARQIDALRIRARGPAQPvAELSGGNQQKVAIGRWLGRDMGV 427
Cdd:COG1126   83 FQQfnlfphltVLENVTLAP--IKVKK--MSKAEAEERAMELLERVGLADKADAYP-AQLSGGQQQRVAIARALAMEPKV 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 428 LLFDEPTRGID---VGakfDIYALLDALAREGRAIVVVSSDL---RElmlICDRIGVMSAGR 483
Cdd:COG1126  158 MLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEMgfaRE---VADRVVFMDGGR 213
cbiO PRK13637
energy-coupling factor transporter ATPase;
277-483 3.09e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 64.30  E-value: 3.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairspADAVRHGIALvSEDRKGEGL--- 353
Cdd:PRK13637  22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG----------VDITDKKVKL-SDIRKKVGLvfq 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 -----LLPQSIAANLSLGQLARvargGVVDGEREN----ALAARQIDALRIRARGPAqpvaELSGGNQQKVAIGRWLGRD 424
Cdd:PRK13637  91 ypeyqLFEETIEKDIAFGPINL----GLSEEEIENrvkrAMNIVGLDYEDYKDKSPF----ELSGGQKRRVAIAGVVAME 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 425 MGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGK 222
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
17-177 3.85e-11

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 63.18  E-value: 3.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  17 VTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAphSRAHAEALGVrm 92
Cdd:COG4604    4 IKNVSKRYGGkVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvATTP--SRELAKRLAI-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  93 VMQELNLVPTLTVAENLFLDRLPH---RFGVIDRRRLAADaraamarvgLD--SLDP------DTLVGslgiGHQQMVEI 161
Cdd:COG4604   80 LRQENHINSRLTVRELVAFGRFPYskgRLTAEDREIIDEA---------IAylDLEDladrylDELSG----GQRQRAFI 146
                        170
                 ....*....|....*.
gi 490656625 162 ARSLAGDCRVLILDEP 177
Cdd:COG4604  147 AMVLAQDTDYVLLDEP 162
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
277-491 4.29e-11

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 63.71  E-value: 4.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAiRSPADAVRHGIALVSEDRKGEglLLP 356
Cdd:PRK13636  21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYS-RKGLMKLRESVGMVFQDPDNQ--LFS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLGQLARVARGGVVDGERENALAARQIDALRirargpAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:PRK13636  98 ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLK------DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 437 IDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRmhAVFERG 491
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGR--VILQGN 225
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
277-482 4.39e-11

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 63.18  E-value: 4.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPP--RPAAIRspadavrhgiALVSEDrkgEGLL 354
Cdd:PRK11248  16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPveGPGAER----------GVVFQN---EGLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LPQSIAANLSLG-QLARVARGgvvdgERENAlaARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEP 433
Cdd:PRK11248  83 PWRNVQDNVAFGlQLAGVEKM-----QRLEI--AHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490656625 434 TRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAG 482
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPG 205
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
21-302 4.56e-11

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 65.53  E-value: 4.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  21 GKTYAepvLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphSRAHAEALGVRMV-M-QEL- 97
Cdd:NF033858  12 GKTVA---LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAVCPRIAyMpQGLg 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  98 -NLVPTLTVAENL-FLDRLphrFGvIDRRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILD 175
Cdd:NF033858  87 kNLYPTLSVFENLdFFGRL---FG-QDAAERRRRIDELLRATGLAPF-ADRPAGKLSGGMKQKLGLCCALIHDPDLLILD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 176 EPTamlTAreVELL-----FDQIARLKADG------VALVYIshrlEELARVAQRVAvLRDGRLvhvdrIDAQPTERL-- 242
Cdd:NF033858 162 EPT---TG--VDPLsrrqfWELIDRIRAERpgmsvlVATAYM----EEAERFDWLVA-MDAGRV-----LATGTPAELla 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 243 -----------VALM-AGREIAEQAVH----GTRTPGAPRLRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRT 302
Cdd:NF033858 227 rtgadtleaafIALLpEEKRRGHQPVVipprPADDDDEPAIEARGLTMrfGDftAVDHVSFRIRRGEIFGFLGSNGCGKS 306
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
277-484 7.32e-11

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 63.67  E-value: 7.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSEdrkGEGLLLP 356
Cdd:PRK11153  20 ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQ---HFNLLSS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLG-QLARVARGGVvdGERENALAAR-QIDALRirARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:PRK11153  97 RTVFDNVALPlELAGTPKAEI--KARVTELLELvGLSDKA--DRYPAQ----LSGGQKQRVAIARALASNPKVLLCDEAT 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490656625 435 RGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK11153 169 SALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
28-231 7.72e-11

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 62.55  E-value: 7.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLV-----APTTGAMRLAGAE-YAPHSRAHAEALGVRMVMQELNLVP 101
Cdd:PRK14267  19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNiYSPDVDPIEVRREVGMVFQYPNPFP 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 102 TLTVAEN----LFLDRLPHRFGVIDRRRLAADARAAMARVGLDSLD--PDTLVGslgiGHQQMVEIARSLAGDCRVLILD 175
Cdd:PRK14267  99 HLTIYDNvaigVKLNGLVKSKKELDERVEWALKKAALWDEVKDRLNdyPSNLSG----GQRQRLVIARALAMKPKILLMD 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 176 EPTAML----TAREVELLFDqiarLKADgVALVYISHRLEELARVAQRVAVLRDGRLVHV 231
Cdd:PRK14267 175 EPTANIdpvgTAKIEELLFE----LKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEV 229
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
14-229 8.40e-11

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 62.22  E-value: 8.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  14 TLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA---PHSRAHAealG 89
Cdd:PRK10895   3 TLTAKNLAKAYkGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllpLHARARR---G 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  90 VRMVMQELNLVPTLTVAENLfldrlphrFGVIDRRRLAADARAAMARVGL-----DSLDPDTLVGSLGIGHQQMVEIARS 164
Cdd:PRK10895  80 IGYLPQEASIFRRLSVYDNL--------MAVLQIRDDLSAEQREDRANELmeefhIEHLRDSMGQSLSGGERRRVEIARA 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 165 LAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
cbiO PRK13645
energy-coupling factor transporter ATPase;
277-484 8.80e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 62.72  E-value: 8.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADA--VRHGIALVSEdrKGEGLL 354
Cdd:PRK13645  26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVkrLRKEIGLVFQ--FPEYQL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LPQSIAANLSLGQLARVArggvvDGERENALAARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:PRK13645 104 FQETIEKDIAFGPVNLGE-----NKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490656625 435 RGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
277-489 9.53e-11

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 62.19  E-value: 9.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRSPaDAVRhgiALVSEDrkgEGLLLP 356
Cdd:COG4525   22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP----VTGP-GADR---GVVFQK---DALLPW 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLG-QLARVARGgvvdgEREnALAARQIDALRIRARGpAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPtr 435
Cdd:COG4525   91 LNVLDNVAFGlRLRGVPKA-----ERR-ARAEELLALVGLADFA-RRRIWQLSGGMRQRVGIARALAADPRFLLMDEP-- 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 436 gidVGAkfdiyalLDALARE-------------GRAIVVVSSDLRELMLICDRIGVMSA--GRMHAVFE 489
Cdd:COG4525  162 ---FGA-------LDALTREqmqellldvwqrtGKGVFLITHSVEEALFLATRLVVMSPgpGRIVERLE 220
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
28-229 1.05e-10

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: 61.52  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLV---APTTGAMRLAGAEYAPH----SRAHaealgvrmVMQELNLV 100
Cdd:cd03234   22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPDqfqkCVAY--------VRQDDILL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 101 PTLTVAENLF---LDRLPHRFGviDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEP 177
Cdd:cd03234   94 PGLTVRETLTytaILRLPRKSS--DAIRKKRVEDVLLRDLALTRIG-GNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 178 TAML---TAREVELLFDQIARlkADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03234  171 TSGLdsfTALNLVSTLSQLAR--RNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
278-486 1.06e-10

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 61.83  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHGIALVSEDrkgEGLLLPQ 357
Cdd:PRK10895  19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD--EDISLLPLHARARRGIGYLPQE---ASIFRRL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 SIAANLSLGQLARVARGGVVDGERENALAAR-QIDALRiRARGPAqpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:PRK10895  94 SVYDNLMAVLQIRDDLSAEQREDRANELMEEfHIEHLR-DSMGQS-----LSGGERRRVEIARALAANPKFILLDEPFAG 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490656625 437 IDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
15-230 1.07e-10

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 62.41  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE------PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE---YAPHSRAha 85
Cdd:COG1101    2 LELKNLSKTFNPgtvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYKRA-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  86 ealgvRM---VMQE--LNLVPTLTVAENLFL-----DRLPHRFGVIDRRRLAADARAAMARVGL-DSLdpDTLVGSLGIG 154
Cdd:COG1101   80 -----KYigrVFQDpmMGTAPSMTIEENLALayrrgKRRGLRRGLTKKRRELFRELLATLGLGLeNRL--DTKVGLLSGG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 155 HQQ-----MVEIARSlagdcRVLILDEPTAML---TAREVELLFDQIARlkADGVALVYISHRLEELARVAQRVAVLRDG 226
Cdd:COG1101  153 QRQalsllMATLTKP-----KLLLLDEHTAALdpkTAALVLELTEKIVE--ENNLTTLMVTHNMEQALDYGNRLIMMHEG 225

                 ....
gi 490656625 227 RLVH 230
Cdd:COG1101  226 RIIL 229
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
277-501 1.45e-10

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


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 61.48  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLV---YGADAadgGTVSI-GDPPRPAAIRSpadaVRHGIALVSEDRkgeg 352
Cdd:cd03251   17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfYDVDS---GRILIdGHDVRDYTLAS----LRRQIGLVSQDV---- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 353 LLLPQSIAANLSLGQLaRVARGGVVDGEReNALAARQIDAL------RIRARGpaqpvAELSGGNQQKVAIGRWLGRDMG 426
Cdd:cd03251   86 FLFNDTVAENIAYGRP-GATREEVEEAAR-AANAHEFIMELpegydtVIGERG-----VKLSGGQRQRIAIARALLKDPP 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 427 VLLFDEPTRGIDVGAKFDIYALLDALArEGRAIVVVSSDLRELMLIcDRIGVMSAGRmhaVFERGgwTQDALLGA 501
Cdd:cd03251  159 ILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIENA-DRIVVLEDGK---IVERG--THEELLAQ 226
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
14-229 1.48e-10

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: 60.64  E-value: 1.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  14 TLVVTGIGKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAP--TTGAMRLAGA-EYAPHSRAHaealgV 90
Cdd:cd03213   10 TVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRpLDKRSFRKI-----I 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  91 RMVMQELNLVPTLTVAENL-FLDRLPhrfgvidrrrlaadaraamarvgldsldpdtlvgSLGIGHQQMVEIARSLAGDC 169
Cdd:cd03213   85 GYVPQDDILHPTLTVRETLmFAAKLR----------------------------------GLSGGERKRVSIALELVSNP 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 170 RVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRL-EELARVAQRVAVLRDGRLV 229
Cdd:cd03213  131 SLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
29-229 1.86e-10

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 61.39  E-value: 1.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVaPTTGAMRLAG---AEYAPHSRAHAEAlgvrMVMQELNLVPTLTV 105
Cdd:COG4138   12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGrplSDWSAAELARHRA----YLSQQQSPPFAMPV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLFLdrlpHRFGVIDRRRLAADARAAMARVGLDSLDPdTLVGSLGIGHQQMVEIAR-------SLAGDCRVLILDEPT 178
Cdd:COG4138   87 FQYLAL----HQPAGASSEAVEQLLAQLAEALGLEDKLS-RPLTQLSGGEWQRVRLAAvllqvwpTINPEGQLLLLDEPM 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490656625 179 AMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG4138  162 NSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
31-244 2.20e-10

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 61.34  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  31 DVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAM-----RLAGAEYAPHSRAhaealgVRMVMQE--LNLVPTL 103
Cdd:PRK15112  31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhPLHFGDYSYRSQR------IRMIFQDpsTSLNPRQ 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAEnlFLDrLPHRFGV-IDRRRLAADARAAMARVGLDSLDPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLT 182
Cdd:PRK15112 105 RISQ--ILD-FPLRLNTdLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 183 AREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVH---VDRIDAQP----TERLVA 244
Cdd:PRK15112 182 MSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVErgsTADVLASPlhelTKRLIA 251
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
262-482 3.09e-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: 63.11  E-value: 3.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   262 PGAPRLRVERLSRGdavrdvsfdVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIgdpprpaairspadAVRHGI 341
Cdd:TIGR01257 1948 SGTSSPAVDRLCVG---------VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATV--------------AGKSIL 2004
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   342 ALVSEDRKGEGLLlPQSIAAN-LSLGQ--LARVARGGVVDGERENALAARQIDALRIRARGPaQPVAELSGGNQQKVAIG 418
Cdd:TIGR01257 2005 TNISDVHQNMGYC-PQFDAIDdLLTGRehLYLYARLRGVPAEEIEKVANWSIQSLGLSLYAD-RLAGTYSGGNKRKLSTA 2082
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625   419 RWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAG 482
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
28-242 3.29e-10

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 60.82  E-value: 3.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSK-------IVAGlvAPTTGAMRLAGAE-YAPHS-----RAHaealgVRMVM 94
Cdd:COG1117   26 ALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPG--ARVEGEILLDGEDiYDPDVdvvelRRR-----VGMVF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  95 QELNLVPTlTVAEN-LFLDRLphrFGVIDRRRLAADARAAMARVGL-----DSLDpdTLVGSLGIGHQQMVEIARSLAGD 168
Cdd:COG1117   99 QKPNPFPK-SIYDNvAYGLRL---HGIKSKSELDEIVEESLRKAALwdevkDRLK--KSALGLSGGQQQRLCIARALAVE 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 169 CRVLILDEPTAML----TAReVELLfdqIARLKADgVALVYISHRLEELARVAQRVAVLRDGRLVHVDridaqPTERL 242
Cdd:COG1117  173 PEVLLMDEPTSALdpisTAK-IEEL---ILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFG-----PTEQI 240
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
28-229 3.41e-10

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 61.46  E-value: 3.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAP----TTGAMRLAGAE---YAPHSRAHAEALGVRMVMQELN-- 98
Cdd:COG4170   22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDllkLSPRERRKIIGREIAMIFQEPSsc 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  99 LVPTLTVAENL------------FLDR----------LPHRFGVIDRRRLaadaraamarvgLDSLdPDTLvgSLGIGhq 156
Cdd:COG4170  102 LDPSAKIGDQLieaipswtfkgkWWQRfkwrkkraieLLHRVGIKDHKDI------------MNSY-PHEL--TEGEC-- 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 157 QMVEIARSLAGDCRVLILDEPT-AMLTAREVellfdQIARL-----KADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG4170  165 QKVMIAMAIANQPRLLIADEPTnAMESTTQA-----QIFRLlarlnQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
277-438 3.56e-10

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 60.41  E-value: 3.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD-------PPRPAAIRspadAVRHGIALVSEDRK 349
Cdd:PRK11124  17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfskTPSDKAIR----ELRRNVGMVFQQYN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 350 geglLLPQ-SIAANLsLGQLARVARggvVDGERENALAARQIDALRIRARGPAQPVaELSGGNQQKVAIGRWLGRDMGVL 428
Cdd:PRK11124  93 ----LWPHlTVQQNL-IEAPCRVLG---LSKDQALARAEKLLERLRLKPYADRFPL-HLSGGQQQRVAIARALMMEPQVL 163
                        170
                 ....*....|
gi 490656625 429 LFDEPTRGID 438
Cdd:PRK11124 164 LFDEPTAALD 173
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
270-466 4.16e-10

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 60.37  E-value: 4.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 270 ERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpAAIRSPADavRHGIALVSeDRK 349
Cdd:PRK10619  13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNG----QTINLVRD--KDGQLKVA-DKN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 350 GEGLLLPQ-----------SIAANLSLGQLARVARGGVVDGE-RENALaaRQIDALRIRARGPAQPVAELSGGNQQKVAI 417
Cdd:PRK10619  86 QLRLLRTRltmvfqhfnlwSHMTVLENVMEAPIQVLGLSKQEaRERAV--KYLAKVGIDERAQGKYPVHLSGGQQQRVSI 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490656625 418 GRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDL 466
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
279-483 4.51e-10

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 60.46  E-value: 4.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 279 RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGdpprpaaiRSPADAVRHGIALVSEDRKgeglLLP-Q 357
Cdd:PRK11247  29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG--------TAPLAEAREDTRLMFQDAR----LLPwK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 SIAANLSLGqlarvARGGVvdgeRENALAArqIDALRIRARGPAQPVAeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRGI 437
Cdd:PRK11247  97 KVIDNVGLG-----LKGQW----RDAALQA--LAAVGLADRANEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 490656625 438 DVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK11247 165 DALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
26-196 4.67e-10

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 59.42  E-value: 4.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAP---TTGAMRLAGAE---YAPHSRahaealGVRMVMQELNL 99
Cdd:COG4136   14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRltaLPAEQR------RIGILFQDDLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 100 VPTLTVAENLFLDrLPHRFGvidRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAGDCRVLILDE 176
Cdd:COG4136   88 FPHLSVGENLAFA-LPPTIG---RAQRRARVEQALEEAGLAGFadrDPATLSG----GQRARVALLRALLAEPRALLLDE 159
                        170       180
                 ....*....|....*....|....
gi 490656625 177 P----TAMLTAREVELLFDQIARL 196
Cdd:COG4136  160 PfsklDAALRAQFREFVFEQIRQR 183
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
279-499 4.76e-10

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: 59.86  E-value: 4.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 279 RDVSFDVRAGEIFGISGLIGAGRTELLRLV---YGADAadgGTVSI-GDPPRPAAIRSpadaVRHGIALVSEdrkgEGLL 354
Cdd:cd03249   20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfYDPTS---GEILLdGVDIRDLNLRW----LRSQIGLVSQ----EPVL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LPQSIAANLSLGqlarvaRGGVVDGERENALAARQIDAL----------RIRARGpaqpvAELSGGNQQKVAIGRWLGRD 424
Cdd:cd03249   89 FDGTIAENIRYG------KPDATDEEVEEAAKKANIHDFimslpdgydtLVGERG-----SQLSGGQKQRIAIARALLRN 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 425 MGVLLFDEPTRGIDVGAKFDIYALLDAlAREGRAIVVVS---SDLRElmliCDRIGVMSAGRmhaVFERGgwTQDALL 499
Cdd:cd03249  158 PKILLLDEATSALDAESEKLVQEALDR-AMKGRTTIVIAhrlSTIRN----ADLIAVLQNGQ---VVEQG--THDELM 225
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
26-229 4.96e-10

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 61.96  E-value: 4.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGA---EYAPHS-RAHaealgVRMVMQELNLVP 101
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrDYTLASlRNQ-----VALVSQNVHLFN 430
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 102 TlTVAENL------------------------FLDRLPHrfgvidrrrlaadaraamarvGLDsldpdTLVGSLGI---- 153
Cdd:PRK11176 431 D-TIANNIayarteqysreqieeaarmayamdFINKMDN---------------------GLD-----TVIGENGVllsg 483
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 154 GHQQMVEIARSLAGDCRVLILDEPTAML---TAREVELLFDQiarLKADGVALVyISHRLEELARvAQRVAVLRDGRLV 229
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALdteSERAIQAALDE---LQKNRTSLV-IAHRLSTIEK-ADEILVVEDGEIV 557
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
277-500 5.22e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 61.67  E-value: 5.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHGIALVSEDRKgegLLLP 356
Cdd:PRK10982  13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG--KEIDFKSSKEALENGISMVHQELN---LVLQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLGQLARvaRGGVVDGERENALAARQIDALRIRArGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:PRK10982  88 RSVMDNMWLGRYPT--KGMFVDQDKMYRDTKAIFDELDIDI-DPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 437 IDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAVFERGGWTQDALLG 500
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIA 228
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
277-483 5.56e-10

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 61.12  E-value: 5.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD------PPRpaaiRSPADAVRHGIALvsedrkg 350
Cdd:PRK09452  29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdithvPAE----NRHVNTVFQSYAL------- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 351 egllLPQ-SIAANLSLG-QLARVArggvvdgerENALAARQIDALRI------RARGPAQpvaeLSGGNQQKVAIGRWLG 422
Cdd:PRK09452  98 ----FPHmTVFENVAFGlRMQKTP---------AAEITPRVMEALRMvqleefAQRKPHQ----LSGGQQQRVAIARAVV 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 423 RDMGVLLFDEPTRGIDvgakfdiYAL-------LDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK09452 161 NKPKVLLLDESLSALD-------YKLrkqmqneLKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 222
cbiO PRK13650
energy-coupling factor transporter ATPase;
26-228 5.86e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 60.13  E-value: 5.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHS----RAHaealgVRMVMQEL-NLV 100
Cdd:PRK13650  20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwdiRHK-----IGMVFQNPdNQF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 101 PTLTVAENLfldrlphRFGV----IDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAGDCRVLI 173
Cdd:PRK13650  95 VGATVEDDV-------AFGLenkgIPHEEMKERVNEALELVGMQDFkerEPARLSG----GQKQRVAIAGAVAMRPKIII 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 174 LDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELArVAQRVAVLRDGRL 228
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
15-244 6.14e-10

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 60.89  E-value: 6.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEalgVRMV 93
Cdd:PRK11432   7 VVLKNITKRFGSnTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD---ICMV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  94 MQELNLVPTLTVAENLfldrlphRFGV----IDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDC 169
Cdd:PRK11432  84 FQSYALFPHMSLGENV-------GYGLkmlgVPKEERKQRVKEALELVDLAGFE-DRYVDQISGGQQQRVALARALILKP 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 170 RVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDA---QPTERLVA 244
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQElyrQPASRFMA 234
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
267-484 6.20e-10

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: 60.45  E-value: 6.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVE-RLSRGD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYG---ADAADGGTVSIG-------DPPRPAAIRSp 333
Cdd:COG0444    7 LKVYfPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDgedllklSEKELRKIRG- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 334 adavrHGIALVSEDrkgeglllPQSiaanlSL-------GQLARVAR-GGVVDGERENALAARQIDALRIRArgPAQpVA 405
Cdd:COG0444   86 -----REIQMIFQD--------PMT-----SLnpvmtvgDQIAEPLRiHGGLSKAEARERAIELLERVGLPD--PER-RL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 406 -----ELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDL---RElmlICDRI 476
Cdd:COG0444  145 dryphELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLgvvAE---IADRV 221

                 ....*...
gi 490656625 477 GVMSAGRM 484
Cdd:COG0444  222 AVMYAGRI 229
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
277-483 6.57e-10

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 58.48  E-value: 6.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRSPADAVRHGIALVSEdrkgEGLLLP 356
Cdd:cd03247   17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP----VSDLEKALSSLISVLNQ----RPYLFD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLslgqlarvarggvvdGERenalaarqidalrirargpaqpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:cd03247   89 TTLRNNL---------------GRR-------------------------FSGGERQRLALARILLQDAPIVLLDEPTVG 128
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490656625 437 IDVGAKFDIYALLDALAREgRAIVVVSSDLR--ELMlicDRIGVMSAGR 483
Cdd:cd03247  129 LDPITERQLLSLIFEVLKD-KTLIWITHHLTgiEHM---DKILFLENGK 173
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
28-229 6.84e-10

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 60.00  E-value: 6.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaEYAPHSRAHAEALGVRMVMQELNLVPTLTVAE 107
Cdd:PRK10253  22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG-EHIQHYASKEVARRIGLLAQNATTPGDITVQE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NLFLDRLPH-----RFGVIDrrrlAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAML- 181
Cdd:PRK10253 101 LVARGRYPHqplftRWRKED----EEAVTKAMQATGITHL-ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLd 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490656625 182 TAREVEL--LFDQIARLKadGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK10253 176 ISHQIDLleLLSELNREK--GYTLAAVLHDLNQACRYASHLIALREGKIV 223
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
10-229 8.35e-10

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: 61.37  E-value: 8.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  10 PDTPTLVVTG-------IGKTY--AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEY 77
Cdd:COG5265  346 PDAPPLVVGGgevrfenVSFGYdpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDV 425
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  78 APHS-RAhaeALGVrmVMQElnlvpTL----TVAENL-----------------------FLDRLPHRFgvidrrrlaad 129
Cdd:COG5265  426 TQASlRA---AIGI--VPQD-----TVlfndTIAYNIaygrpdaseeeveaaaraaqihdFIESLPDGY----------- 484
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 130 araamarvgldsldpDTLVGSLGI----GHQQMVEIARSLAGDCRVLILDEPTAML-TAREVELLfDQIARLKADGVALV 204
Cdd:COG5265  485 ---------------DTRVGERGLklsgGEKQRVAIARTLLKNPPILIFDEATSALdSRTERAIQ-AALREVARGRTTLV 548
                        250       260
                 ....*....|....*....|....*
gi 490656625 205 yISHRLEELARvAQRVAVLRDGRLV 229
Cdd:COG5265  549 -IAHRLSTIVD-ADEILVLEAGRIV 571
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
280-487 8.84e-10

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 60.48  E-value: 8.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 280 DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairspADAVRhgiaLVSEDRK------GEGL 353
Cdd:PRK10851  20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG----------TDVSR----LHARDRKvgfvfqHYAL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 LLPQSIAANLSLGqLARVARGgvvdgERENALAARQ--------IDALRIRARGPAQpvaeLSGGNQQKVAIGRWLGRDM 425
Cdd:PRK10851  86 FRHMTVFDNIAFG-LTVLPRR-----ERPNAAAIKAkvtqllemVQLAHLADRYPAQ----LSGGQKQRVALARALAVEP 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 426 GVLLFDEPTRGIDVGAKFDIYALLDALAREGR-AIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQA 218
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
29-226 1.33e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 58.99  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHS----RAHaealgVRMVMQ--ELNLVPT 102
Cdd:PRK13648  25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfeklRKH-----IGIVFQnpDNQFVGS 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LT---VAENLFLDRLPHRfgvidrrRLAADARAAMARVG-LDSLD--PDTLVGslgiGHQQMVEIARSLAGDCRVLILDE 176
Cdd:PRK13648 100 IVkydVAFGLENHAVPYD-------EMHRRVSEALKQVDmLERADyePNALSG----GQKQRVAIAGVLALNPSVIILDE 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490656625 177 PTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEElARVAQRVAVLRDG 226
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSE-AMEADHVIVMNKG 218
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
278-482 1.41e-09

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 58.25  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPP--RPAAIRS---------PADAVRHGIALvse 346
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQitEPGPDRMvvfqnysllPWLTVRENIAL--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  347 drkgeglllpqsiAANLSLGQLARVARGGVVDgerenalaaRQIDALRIRARGPAQPvAELSGGNQQKVAIGRWLGRDMG 426
Cdd:TIGR01184  78 -------------AVDRVLPDLSKSERRAIVE---------EHIALVGLTEAADKRP-GQLSGGMKQRVAIARALSIRPK 134
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625  427 VLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVV-VSSDLRELMLICDRIGVMSAG 482
Cdd:TIGR01184 135 VLLLDEPFGALDALTRGNLQEELMQIWEEHRVTVLmVTHDVDEALLLSDRVVMLTNG 191
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
277-484 1.58e-09

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


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 57.81  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIgDPPRPAAIrsPADAVRHGIALVSEDRkgegLLLP 356
Cdd:cd03369   23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDISTI--PLEDLRSSLTIIPQDP----TLFS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLslgqlarvarggvvdgERENALAARQI-DALRIRARGpaqpvAELSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:cd03369   96 GTIRSNL----------------DPFDEYSDEEIyGALRVSEGG-----LNLSQGQRQLLCLARALLKRPRVLVLDEATA 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490656625 436 GIDVGAKfdiyALLDALARE---GRAIVVVSSDLRELmLICDRIGVMSAGRM 484
Cdd:cd03369  155 SIDYATD----ALIQKTIREeftNSTILTIAHRLRTI-IDYDKILVMDAGEV 201
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
404-479 1.77e-09

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: 58.53  E-value: 1.77e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 404 VAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVM 479
Cdd:cd03236  137 IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
278-484 1.78e-09

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: 56.84  E-value: 1.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpAAIRSPA-DAVRHGIALVSEDRKgeglLLP 356
Cdd:cd03246   18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG----ADISQWDpNELGDHVGYLPQDDE----LFS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLslgqlarvarggvvdgerenalaarqidalrirargpaqpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:cd03246   90 GSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSH 126
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 490656625 437 IDVGAKFDIYALLDALAREGRAIVVVSSDlRELMLICDRIGVMSAGRM 484
Cdd:cd03246  127 LDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
30-229 2.51e-09

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 58.95  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  30 DDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTG---------------AMR-------------LAG------- 74
Cdd:PRK15079  38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGevawlgkdllgmkddEWRavrsdiqmifqdpLASlnprmti 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  75 ----AE----YAPHSRAHAEALGVRMVMQELNLVPTLtvaenlfLDRLPHRFGvidrrrlaadaraamarvgldsldpdt 146
Cdd:PRK15079 118 geiiAEplrtYHPKLSRQEVKDRVKAMMLKVGLLPNL-------INRYPHEFS--------------------------- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 147 lvgslgiGHQ-QMVEIARSLAGDCRVLILDEPTAML----TAREVELLFDQIARLkadGVALVYISHRLEELARVAQRVA 221
Cdd:PRK15079 164 -------GGQcQRIGIARALILEPKLIICDEPVSALdvsiQAQVVNLLQQLQREM---GLSLIFIAHDLAVVKHISDRVL 233

                 ....*...
gi 490656625 222 VLRDGRLV 229
Cdd:PRK15079 234 VMYLGHAV 241
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
22-244 2.72e-09

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 58.66  E-value: 2.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  22 KTYAEPV--LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAP----TTGAMRLAGAE---YAPHSRAHAEALGVRM 92
Cdd:PRK15093  14 KTSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDllrLSPRERRKLVGHNVSM 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  93 VMQELN--LVPTLTVAENL--------FLDRLPHRFGvidrrRLAADARAAMARVGLDslDPDTLVGS----LGIGHQQM 158
Cdd:PRK15093  94 IFQEPQscLDPSERVGRQLmqnipgwtYKGRWWQRFG-----WRKRRAIELLHRVGIK--DHKDAMRSfpyeLTEGECQK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 159 VEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLVHvdriDAQ 237
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVE----TAP 242

                 ....*..
gi 490656625 238 PTERLVA 244
Cdd:PRK15093 243 SKELVTT 249
hmuV PRK13547
heme ABC transporter ATP-binding protein;
28-229 2.75e-09

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 58.30  E-value: 2.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLV--------APTTGAMRLAGaeyAPHSRAHAEALG-VRMVM-QEL 97
Cdd:PRK13547  16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNG---EPLAAIDAPRLArLRAVLpQAA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  98 NLVPTLTVAENLFLDRLPHrfgvIDRRRLAADARAAMARVGLDSLDPDTLVG----SLGIGHQQMVEIARSLA------- 166
Cdd:PRK13547  93 QPAFAFSAREIVLLGRYPH----ARRAGALTHRDGEIAWQALALAGATALVGrdvtTLSGGELARVQFARVLAqlwpphd 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 167 --GDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13547 169 aaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
277-486 3.09e-09

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 57.40  E-value: 3.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVsigdpprpaairspadaVRHGialvsedrkgeglllp 356
Cdd:COG1134   41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV-----------------EVNG---------------- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 qSIAANLSLGqlarvarGGvVDGE---RENA--------LAARQIDAlRIRArgpaqpVAELSGgnqqkvaIGRWlgrdm 425
Cdd:COG1134   88 -RVSALLELG-------AG-FHPEltgRENIylngrllgLSRKEIDE-KFDE------IVEFAE-------LGDF----- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 426 gvllFDEPTR------------GIDVGAKFDIY------------------ALLDALAREGRAIVVVSSDLRELMLICDR 475
Cdd:COG1134  140 ----IDQPVKtyssgmrarlafAVATAVDPDILlvdevlavgdaafqkkclARIRELRESGRTVIFVSHSMGAVRRLCDR 215
                        250
                 ....*....|.
gi 490656625 476 IGVMSAGRMHA 486
Cdd:COG1134  216 AIWLEKGRLVM 226
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
171-438 3.10e-09

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 59.26  E-value: 3.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 171 VLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGRE 250
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQLAHSE 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 251 ---------IAEQAVHGTRTPGAPR--LRVERLSRGDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVygadaadgg 317
Cdd:PRK10938 236 qlegvqlpePDEPSARHALPANEPRivLNNGVVSYNDRPilHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI--------- 306
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 318 tvsIGDPP------------RPAAIRSPADAVRHgIALVSEdrkgeglllpqsiaanlSLGQLARV---ARGGVVDG--- 379
Cdd:PRK10938 307 ---TGDHPqgysndltlfgrRRGSGETIWDIKKH-IGYVSS-----------------SLHLDYRVstsVRNVILSGffd 365
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 380 ---------ERENALAARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGID 438
Cdd:PRK10938 366 sigiyqavsDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
28-229 3.27e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 57.89  E-value: 3.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaEYAPHSRAHAEALGVRMVMQEL-NLVPTLTVA 106
Cdd:PRK13652  19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG-EPITKENIREVRKFVGLVFQNPdDQIFSPTVE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 107 ENLFLDrlPHRFGvIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREV 186
Cdd:PRK13652  98 QDIAFG--PINLG-LDEETVAHRVSSALHMLGLEELR-DRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 490656625 187 ELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13652 174 KELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
3-229 3.79e-09

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 59.07  E-value: 3.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   3 STDPDSTPDTPTLVVTGIGKTY---AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAP 79
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYpdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD 406
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  80 HSRAhaeALGVRM--VMQELNLVPTlTVAENLFL-------DRLphrfgvidrrrlaadaRAAMARVGLDSL--DPDTLV 148
Cdd:PRK11160 407 YSEA---ALRQAIsvVSQRVHLFSA-TLRDNLLLaapnasdEAL----------------IEVLQQVGLEKLleDDKGLN 466
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 149 GSLGIGHQQM-------VEIARSLAGDCRVLILDEPTAML---TAREV-ELLFDQiarlkADGVALVYISHRLEELARVa 217
Cdd:PRK11160 467 AWLGEGGRQLsggeqrrLGIARALLHDAPLLLLDEPTEGLdaeTERQIlELLAEH-----AQNKTVLMITHRLTGLEQF- 540
                        250
                 ....*....|..
gi 490656625 218 QRVAVLRDGRLV 229
Cdd:PRK11160 541 DRICVMDNGQII 552
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
277-485 4.03e-09

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: 59.64  E-value: 4.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpAAIRSPADAVRHGIALVSEdrkgEGLLLP 356
Cdd:TIGR01257  945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG----KDIETNLDAVRQSLGMCPQ----HNILFH 1016
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   357 QSIAAN--LSLGQLarvaRGGVVDGERENALAARQIDALRIRARGPAQpvaELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:TIGR01257 1017 HLTVAEhiLFYAQL----KGRSWEEAQLEMEAMLEDTGLHHKRNEEAQ---DLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 490656625   435 RGIDVGAKFDIYALLDALaREGRAIVVVSSDLRELMLICDRIGVMSAGRMH 485
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLY 1139
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
277-483 4.12e-09

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 58.32  E-value: 4.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADavrHGIALVSEDRKgeglLLP 356
Cdd:PRK11650  19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG--RVVNELEPAD---RDIAMVFQNYA----LYP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 Q-SIAANLSLG-QLARVARGGVvdgERENALAAR--QIDALRirARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLFDE 432
Cdd:PRK11650  90 HmSVRENMAYGlKIRGMPKAEI---EERVAEAARilELEPLL--DRKPRE----LSGGQRQRVAMGRAIVREPAVFLFDE 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490656625 433 PTRGIDvgAKFDIYALLD--ALAREGRAI-VVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK11650 161 PLSNLD--AKLRVQMRLEiqRLHRRLKTTsLYVTHDQVEAMTLADRVVVMNGGV 212
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
277-484 5.51e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 57.31  E-value: 5.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaaIRSPADAVRH-----GIALVSEDRKGE 351
Cdd:PRK13632  24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG------ITISKENLKEirkkiGIIFQNPDNQFI 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 352 GLLLPQSIAANLSLGQLARVARGGVVDGerenalAARQIDALRIRARGPAqpvaELSGGNQQKVAIGRWLGRDMGVLLFD 431
Cdd:PRK13632  98 GATVEDDIAFGLENKKVPPKKMKDIIDD------LAKKVGMEDYLDKEPQ----NLSGGQKQRVAIASVLALNPEIIIFD 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490656625 432 EPTRGIDVGAKFDIYALLDALAREG-RAIVVVSSDLRELMLiCDRIGVMSAGRM 484
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAIL-ADKVIVFSEGKL 220
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
282-485 6.22e-09

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 56.51  E-value: 6.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 282 SFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD------PP--RPAAIrspadavrhgiaLVSEDRkgegl 353
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtttPPsrRPVSM------------LFQENN----- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 LLPQ-SIAANLSLGqlarVARGGVVDGERENALA--ARQIDALRIRARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLF 430
Cdd:PRK10771  82 LFSHlTVAQNIGLG----LNPGLKLNAAQREKLHaiARQMGIEDLLARLPGQ----LSGGQRQRVALARCLVREQPILLL 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 431 DEPTRGIDVGAKFDIYALLDALAREGR-AIVVVSSDLRELMLICDRIGVMSAGRMH 485
Cdd:PRK10771 154 DEPFSALDPALRQEMLTLVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIA 209
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
10-233 6.92e-09

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


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 55.88  E-value: 6.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  10 PDTPTLVVTGIGKTYA---EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphsrahae 86
Cdd:cd03369    2 PEHGEIEVENLSVRYApdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS-------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  87 ALGVRMVMQELNLV---PTL---TVAENLflDRLphrfgvidrrrlaadaraamarvglDSLDPDTLVGSLGI------- 153
Cdd:cd03369   74 TIPLEDLRSSLTIIpqdPTLfsgTIRSNL--DPF-------------------------DEYSDEEIYGALRVsegglnl 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 154 --GHQQMVEIARSLAGDCRVLILDEPTAMLTArEVELLFDQIARLKADGVALVYISHRLEELARVAqRVAVLRDGRLVHV 231
Cdd:cd03369  127 sqGQRQLLCLARALLKRPRVLVLDEATASIDY-ATDALIQKTIREEFTNSTILTIAHRLRTIIDYD-KILVMDAGEVKEY 204

                 ..
gi 490656625 232 DR 233
Cdd:cd03369  205 DH 206
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
405-462 7.53e-09

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 56.73  E-value: 7.53e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 405 AELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGID---VGakfDIYALLDALAREGRAIVVV 462
Cdd:COG4598  153 AHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDpelVG---EVLKVMRDLAEEGRTMLVV 210
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
27-229 9.03e-09

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 58.05  E-value: 9.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAH-AEALGVrmVMQELNLVpTLTV 105
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlRRNIAV--VFQDAGLF-NRSI 425
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLFLDRLphrfGVIDRRRLAADARAAMARVGLDSLDP-DTLVG----SLGIGHQQMVEIARSLAGDCRVLILDEPTAM 180
Cdd:PRK13657 426 EDNIRVGRP----DATDEEMRAAAERAQAHDFIERKPDGyDTVVGergrQLSGGERQRLAIARALLKDPPILILDEATSA 501
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490656625 181 L---TAREVELLFDQIARlkadGVALVYISHRLEELaRVAQRVAVLRDGRLV 229
Cdd:PRK13657 502 LdveTEAKVKAALDELMK----GRTTFIIAHRLSTV-RNADRILVFDNGRVV 548
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
15-255 9.08e-09

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 56.55  E-value: 9.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYA-EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaEYAPHSRAHAEAL--GVR 91
Cdd:PRK13638   2 LATSDLWFRYQdEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-KPLDYSKRGLLALrqQVA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  92 MVMQELNL--------------VPTLTVAENLFLDRLPHRFGVIDRRRLAADAraamarvgldsldpdtlVGSLGIGHQQ 157
Cdd:PRK13638  81 TVFQDPEQqifytdidsdiafsLRNLGVPEAEITRRVDEALTLVDAQHFRHQP-----------------IQCLSHGQKK 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 158 MVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVhvdrIDAQ 237
Cdd:PRK13638 144 RVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQIL----THGA 219
                        250
                 ....*....|....*...
gi 490656625 238 PTErlvaLMAGREIAEQA 255
Cdd:PRK13638 220 PGE----VFACTEAMEQA 233
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
278-484 9.50e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 56.21  E-value: 9.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELL----RLVYGADA---ADGGTVSIG-DPPRPAAIRspadaVRHGIALV-SEDR 348
Cdd:PRK14246  26 LKDITIKIPNNSIFGIMGPSGSGKSTLLkvlnRLIEIYDSkikVDGKVLYFGkDIFQIDAIK-----LRKEVGMVfQQPN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 349 KGEGLLLPQSIAANLSLGQLA--RVARGGVVDGERENALAARQIDALRirargpaQPVAELSGGNQQKVAIGRWLGRDMG 426
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKekREIKKIVEECLRKVGLWKEVYDRLN-------SPASQLSGGQQQRLTIARALALKPK 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 427 VLLFDEPTRGIDVGAKFDIYALLDALAREgRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
32-229 9.82e-09

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 56.09  E-value: 9.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  32 VSLALYPGEALALTGENGAGKSTLSKIVAGLVaPTTGAMRLAG---AEYAPHSRAHAEAlgvrMVMQELNLVPTLTVAEN 108
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGqplEAWSAAELARHRA----YLSQQQTPPFAMPVFQY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 109 LFLDRLPHRfgviDRRRLAADARAAMARVGLDSLDPdTLVGSLGIGHQQMVEIA-------RSLAGDCRVLILDEPTAML 181
Cdd:PRK03695  90 LTLHQPDKT----RTEAVASALNEVAEALGLDDKLG-RSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSL 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 490656625 182 TAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
cbiO PRK13644
energy-coupling factor transporter ATPase;
277-484 1.06e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 56.53  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-----GDPPRPAAIRSPAdavrhGIALVSEDRKGE 351
Cdd:PRK13644  17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidtGDFSKLQGIRKLV-----GIVFQNPETQFV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 352 GLLLPQSIA---ANLSLGQLARVARggvVDgereNALAarQIDALRIRARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVL 428
Cdd:PRK13644  92 GRTVEEDLAfgpENLCLPPIEIRKR---VD----RALA--EIGLEKYRHRSPKT----LSGGQGQCVALAGILTMEPECL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 429 LFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMlICDRIGVMSAGRM 484
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKI 213
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
25-204 1.26e-08

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 55.24  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  25 AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyapHSRAHAEALGVRMVMQEL-NLVPTL 103
Cdd:PRK13543  23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG-----KTATRGDRSRFMAYLGHLpGLKADL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLfldrlpHRFGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTA 183
Cdd:PRK13543  98 STLENL------HFLCGLHGRRAKQMPGSALAIVGLAGYE-DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
                        170       180
                 ....*....|....*....|..
gi 490656625 184 REVELLFDQI-ARLKADGVALV 204
Cdd:PRK13543 171 EGITLVNRMIsAHLRGGGAALV 192
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
277-486 1.85e-08

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: 54.85  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSigdpprpaairspadavRHGialvsedrkgeglllp 356
Cdd:cd03220   37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT-----------------VRG---------------- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 qSIAANLSLGqlarvarGGvVDGE---RENA--------LAARQIDALRIRARGPA-------QPVAELSGGNQQKVAIG 418
Cdd:cd03220   84 -RVSSLLGLG-------GG-FNPEltgRENIylngrllgLSRKEIDEKIDEIIEFSelgdfidLPVKTYSSGMKARLAFA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 419 RWLGRDMGVLLFDEptrGIDVG-AKFDI--YALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:cd03220  155 IATALEPDILLIDE---VLAVGdAAFQEkcQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
21-227 1.85e-08

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: 54.78  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  21 GKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE-YAPhsrahaealgvrmvmQELNL 99
Cdd:cd03250   13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIaYVS---------------QEPWI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 100 VPTlTVAEN-LFLDRLPHRF--GVIDRRrlaadaraamarvgldSLDPD---------TLVGSLGI----GHQQMVEIAR 163
Cdd:cd03250   78 QNG-TIRENiLFGKPFDEERyeKVIKAC----------------ALEPDleilpdgdlTEIGEKGInlsgGQKQRISLAR 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 164 SLAGDCRVLILDEPTAMLTAREVELLFDQ-IARLKADGVALVYISHRLEELARvAQRVAVLRDGR 227
Cdd:cd03250  141 AVYSDADIYLLDDPLSAVDAHVGRHIFENcILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
402-479 1.98e-08

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: 56.72  E-value: 1.98e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 402 QPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVM 479
Cdd:COG1245  208 RDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHIL 285
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
265-482 3.55e-08

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 54.40  E-value: 3.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLS----RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLV-----YGADAADGGTVSIGDpprpAAIRSP-A 334
Cdd:PRK14239   4 PILQVSDLSvyynKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNG----HNIYSPrT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 335 DAVrhgialvsEDRKGEGLLL------PQSIAANLSLG-QLARVARGGVVDGERENALAARQI-----DALRIRARGpaq 402
Cdd:PRK14239  80 DTV--------DLRKEIGMVFqqpnpfPMSIYENVVYGlRLKGIKDKQVLDEAVEKSLKGASIwdevkDRLHDSALG--- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 403 pvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALaREGRAIVVVSSDLRELMLICDRIGVMSAG 482
Cdd:PRK14239 149 ----LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDG 223
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
267-492 3.86e-08

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 54.63  E-value: 3.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSR----GDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGadaadggtVSIGDPPRPAAIRSPADAVRHGIA 342
Cdd:PRK09984   5 IRVEKLAKtfnqHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSG--------LITGDKSAGSHIELLGRTVQREGR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDRKGE---GLLLPQ-------SIAANLSLGQLA-----RVARGGVVDGERENALAARQIDALrirARGPAQPVAEL 407
Cdd:PRK09984  77 LARDIRKSRantGYIFQQfnlvnrlSVLENVLIGALGstpfwRTCFSWFTREQKQRALQALTRVGM---VHFAHQRVSTL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 408 SGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDV-GAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRmha 486
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPeSARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH--- 230

                 ....*.
gi 490656625 487 VFERGG 492
Cdd:PRK09984 231 VFYDGS 236
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
277-484 3.96e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 55.24  E-value: 3.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD---PPRPAAIRSPADAVRHGIALVSEDRKGEGL 353
Cdd:PRK13631  41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyiGDKKNNHELITNPYSKKIKNFKELRRRVSM 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 --------LLPQSIAANLSLGQlarVARGgvVDGERENALAARQIDALRIRA----RGPAqpvaELSGGNQQKVAIGRWL 421
Cdd:PRK13631 121 vfqfpeyqLFKDTIEKDIMFGP---VALG--VKKSEAKKLAKFYLNKMGLDDsyleRSPF----GLSGGQKRRVAIAGIL 191
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 422 GRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
264-466 4.55e-08

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: 53.52  E-value: 4.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  264 APRLRVERLSRgDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADavrhGIAL 343
Cdd:TIGR01189   3 ARNLACSRGER-MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE----NILY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  344 VSEDRKGEGLLlpqSIAANLSLGQlarvARGGVVDGERENALAARQIDALRIRargpaqPVAELSGGNQQKVAIGRWLGR 423
Cdd:TIGR01189  78 LGHLPGLKPEL---SALENLHFWA----AIHGGAQRTIEDALAAVGLTGFEDL------PAAQLSAGQQRRLALARLWLS 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 490656625  424 DMGVLLFDEPTRGIDVGAKFDIYALLDA-LAREGRAIVVVSSDL 466
Cdd:TIGR01189 145 RRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTHQDL 188
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
30-224 5.55e-08

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 53.27  E-value: 5.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  30 DDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL-------GVRmvmqelnlvPT 102
Cdd:PRK13538  18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylghqpGIK---------TE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENL-FLDRLphrFGVIDrrrlAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAML 181
Cdd:PRK13538  89 LTALENLrFYQRL---HGPGD----DEALWEALAQVGLAGFE-DVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 490656625 182 TAREVELLFDQIARLKADGVALVYISHRleELARVAQRVAVLR 224
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVILTTHQ--DLPVASDKVRKLR 201
cbiO PRK13646
energy-coupling factor transporter ATPase;
406-484 6.17e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 54.02  E-value: 6.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 406 ELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALA-REGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK13646 145 QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
26-229 6.66e-08

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 55.11  E-value: 6.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyAPHSRAHAEAL--GVRMVMQElNLVPTL 103
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG---RPLSSLSHSVLrqGVAMVQQD-PVVLAD 429
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLFLDRLPHRFGVIDrrrlaadaraAMARVGLDSLD---PD---TLVG----SLGIGHQQMVEIARSLAGDCRVLI 173
Cdd:PRK10790 430 TFLANVTLGRDISEEQVWQ----------ALETVQLAELArslPDglyTPLGeqgnNLSVGQKQLLALARVLVQTPQILI 499
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 174 LDEPTAMLTArEVELLFDQIARLKADGVALVYISHRLEELARvAQRVAVLRDGRLV 229
Cdd:PRK10790 500 LDEATANIDS-GTEQAIQQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAV 553
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
402-479 6.92e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 55.20  E-value: 6.92e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 402 QPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALArEGRAIVVVSSDLRELMLICDRIGVM 479
Cdd:PRK13409 208 RDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHDLAVLDYLADNVHIA 284
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
29-229 7.10e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 54.08  E-value: 7.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMrLAGAEYAPHSRAHAEAL--GVRMVMQEL-NLVPTLTV 105
Cdd:PRK13636  22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSRKGLMKLreSVGMVFQDPdNQLFSASV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLfldrlphRFGVIDRR----RLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAML 181
Cdd:PRK13636 101 YQDV-------SFGAVNLKlpedEVRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490656625 182 TAREV-ELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13636 173 DPMGVsEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
265-483 7.13e-08

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 53.49  E-value: 7.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLS---RG-DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD---PPRPAAIRSpadav 337
Cdd:COG1137    2 MTLEAENLVksyGKrTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGediTHLPMHKRA----- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 338 RHGIAlvsedrkgeglLLPQ--SIAANLSLGQ-LARVARGGVVDGERENALAARQIDALRI--RARGPAQpvaELSGGNQ 412
Cdd:COG1137   77 RLGIG-----------YLPQeaSIFRKLTVEDnILAVLELRKLSKKEREERLEELLEEFGIthLRKSKAY---SLSGGER 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 413 QKVAIGRWLGRDMGVLLFDEPTRGID---VGakfDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:COG1137  143 RRVEIARALATNPKFILLDEPFAGVDpiaVA---DIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGK 213
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
14-229 7.38e-08

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 53.55  E-value: 7.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  14 TLVVTGIGKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAP----TTGAMRLAGAEYAPhsrAHAEALG 89
Cdd:PRK10418   4 QIELRNIALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAP---CALRGRK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  90 VRMVMQE----LNLVPTLT--VAENLFldrlphrfgVIDRRRLAADARAAMARVGLDslDPDTLVGS----LGIGHQQMV 159
Cdd:PRK10418  81 IATIMQNprsaFNPLHTMHthARETCL---------ALGKPADDATLTAALEAVGLE--NAARVLKLypfeMSGGMLQRM 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 160 EIARSLAGDCRVLILDEPT----AMLTAREVELLfDQIARLKADGVALVyiSHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTtdldVVAQARILDLL-ESIVQKRALGMLLV--THDMGVVARLADDVAVMSHGRIV 220
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
26-229 8.36e-08

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: 52.88  E-value: 8.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHS-RAHaealgVRMVMQElnlvP 101
Cdd:cd03244   17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiSKIGLHDlRSR-----ISIIPQD----P 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 102 TL---TVAENL-FLDRLP--------HRFGVIDRRRLAADaraamarvGLDSldPDTLVGS-LGIGHQQMVEIARSLAGD 168
Cdd:cd03244   88 VLfsgTIRSNLdPFGEYSdeelwqalERVGLKEFVESLPG--------GLDT--VVEEGGEnLSVGQRQLLCLARALLRK 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 169 CRVLILDEPTA---MLTAREVEllfdQIARLKADGVALVYISHRLEELARvAQRVAVLRDGRLV 229
Cdd:cd03244  158 SKILVLDEATAsvdPETDALIQ----KTIREAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
277-502 9.01e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 53.59  E-value: 9.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAAIRSpadaVRHGIALVSEDRKGEglLL 355
Cdd:PRK13647  20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVmGREVNAENEKW----VRSKVGLVFQDPDDQ--VF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 PQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRargpaqPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:PRK13647  94 SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDK------PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMA 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 436 GIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAVFERGGWTQDALLGAA 502
Cdd:PRK13647 168 YLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQA 234
cbiO PRK13645
energy-coupling factor transporter ATPase;
12-229 9.26e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 53.86  E-value: 9.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  12 TPTLVVTGIGKTYAEPV------LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHA 85
Cdd:PRK13645   4 SKDIILDNVSYTYAKKTpfefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  86 EalgVRMVMQELNLVPTLTVAEnLFLDRLPH--RFGVIDRRRLAADA-RAAMARVGLDSLDPDTLVGS---LGIGHQQMV 159
Cdd:PRK13645  84 E---VKRLRKEIGLVFQFPEYQ-LFQETIEKdiAFGPVNLGENKQEAyKKVPELLKLVQLPEDYVKRSpfeLSGGQKRRV 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 160 EIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
15-68 1.08e-07

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 54.51  E-value: 1.08e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490656625  15 LVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTG 68
Cdd:PRK15064 320 LEVENLTKGFdNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
6-73 1.21e-07

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 54.41  E-value: 1.21e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625   6 PDSTPDtPTLVVTGIGKTYAEP-VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLA 73
Cdd:PRK10636 305 PESLPN-PLLKMEKVSAGYGDRiILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA 372
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
354-474 1.28e-07

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 53.12  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 LLPQSIAANLSLGQLARVARGGV-VDGERENALAARQI-DALRIRARGPAqpvAELSGGNQQKVAIGRWLGRDMGVLLFD 431
Cdd:PRK14258  99 LFPMSVYDNVAYGVKIVGWRPKLeIDDIVESALKDADLwDEIKHKIHKSA---LDLSGGQQQRLCIARALAVKPKVLLMD 175
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490656625 432 EPTRGIDVGAKFDIYALLDALA-REGRAIVVVSSDLRELMLICD 474
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSD 219
cbiO PRK13649
energy-coupling factor transporter ATPase;
275-484 1.42e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 52.82  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 275 GDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaaIRSPADAVRHGIALVsedRKGEGLL 354
Cdd:PRK13649  20 GRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDD------TLITSTSKNKDIKQI---RKKVGLV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 L--PQSIAANLSLgqLARVARG----GVVDGEREnALAARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVL 428
Cdd:PRK13649  91 FqfPESQLFEETV--LKDVAFGpqnfGVSQEEAE-ALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKIL 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 429 LFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
272-439 1.92e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 53.80  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 272 LSRGDA--VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIG----------DPPRPAAiRSPADAVRH 339
Cdd:PRK11147  11 LSFSDAplLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlqqDPPRNVE-GTVYDFVAE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 340 GIALVSEDRKGEGLLLPQsIAANLS---LGQLARVArgGVVDGERENALAARQIDALRIRARGPAQPVAELSGGNQQKVA 416
Cdd:PRK11147  90 GIEEQAEYLKRYHDISHL-VETDPSeknLNELAKLQ--EQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGGWLRKAA 166
                        170       180
                 ....*....|....*....|...
gi 490656625 417 IGRWLGRDMGVLLFDEPTRGIDV 439
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDI 189
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
406-466 2.04e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 52.78  E-value: 2.04e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 406 ELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGID-VGAKfDIYALLDALAREGRAIVVVSSDL 466
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVK-EILEIFDNLNKQGKTIILVTHDL 225
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
28-229 2.10e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 52.93  E-value: 2.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG---------------VRM 92
Cdd:PRK13631  41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkelrrrVSM 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  93 VMQ--ELNLVPTlTVAENLFLDrlPHRFGViDRRRLAADARAAMARVGLDS--LD--PDTLVGslgiGHQQMVEIARSLA 166
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMFG--PVALGV-KKSEAKKLAKFYLNKMGLDDsyLErsPFGLSG----GQKRRVAIAGILA 192
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 167 GDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
278-484 2.12e-07

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: 51.70  E-value: 2.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAairSPADAVRHGIALVSEdrkgEGLLLPQ 357
Cdd:cd03248   30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ---YEHKYLHSKVSLVGQ----EPVLFAR 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 SIAANLSLGqLARVARGGVVdgerENALAARQIDALRIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEP 433
Cdd:cd03248  103 SLQDNIAYG-LQSCSFECVK----EAAQKAHAHSFISELASGYDTEVGEkgsqLSGGQKQRVAIARALIRNPQVLILDEA 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490656625 434 TRGIDVGAKFDIY-ALLDALARegRAIVVVSSDLrELMLICDRIGVMSAGRM 484
Cdd:cd03248  178 TSALDAESEQQVQqALYDWPER--RTVLVIAHRL-STVERADQILVLDGGRI 226
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
28-242 2.13e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 52.78  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMrlagaEYA-PHSRAHAEALGVRMVMQELNLVPT---- 102
Cdd:PRK13651  22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI-----EWIfKDEKNKKKTKEKEKVLEKLVIQKTrfkk 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 --------------LTVAE-NLFLDRL-------PHRFGViDRRRLAADARAAMARVGLDS--LD--PDTLVGslgiGHQ 156
Cdd:PRK13651  97 ikkikeirrrvgvvFQFAEyQLFEQTIekdiifgPVSMGV-SKEEAKKRAAKYIELVGLDEsyLQrsPFELSG----GQK 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 157 QMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHvdriDA 236
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIK----DG 247

                 ....*.
gi 490656625 237 QPTERL 242
Cdd:PRK13651 248 DTYDIL 253
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
390-499 2.19e-07

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 52.32  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 390 IDALRIRArgpaQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLREL 469
Cdd:PRK13638 124 VDAQHFRH----QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLI 199
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 490656625 470 MLICDRIGVMSAGRMHA------VF------ERGGWTQDALL 499
Cdd:PRK13638 200 YEISDAVYVLRQGQILThgapgeVFacteamEQAGLTQPWLV 241
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
29-181 2.76e-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: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLvapttgamRLAGAEYAPHSRAHAEALGVRM-------VMQELNLVP 101
Cdd:TIGR00955  41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFR--------SPKGVKGSGSVLLNGMPIDAKEmraisayVQQDDLFIP 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  102 TLTVAENLFLD---RLPHRfgvIDRRRLAADARAAMARVGLDSLdPDTLVG------SLGIGHQQMVEIARSLAGDCRVL 172
Cdd:TIGR00955 113 TLTVREHLMFQahlRMPRR---VTKKEKRERVDEVLQALGLRKC-ANTRIGvpgrvkGLSGGERKRLAFASELLTDPPLL 188

                  ....*....
gi 490656625  173 ILDEPTAML 181
Cdd:TIGR00955 189 FCDEPTSGL 197
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
281-486 2.91e-07

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 51.86  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 281 VSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGgTVSIGDppRPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIA 360
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSG-SIQFAG--QPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 361 anLSLGQLARVARGGVVDGERENALaarQIDALRIRargpaqPVAELSGGNQQKV-------AIGRWLGRDMGVLLFDEP 433
Cdd:PRK03695  92 --LHQPDKTRTEAVASALNEVAEAL---GLDDKLGR------SVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490656625 434 TRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA 213
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
29-68 3.01e-07

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 51.74  E-value: 3.01e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 490656625  29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTG 68
Cdd:PRK13546  40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG 79
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
290-486 3.43e-07

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 52.18  E-value: 3.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 290 IFGISGligAGRTELLRLVYGADAADGGTVSIGDpprpaaiRSPADAVRhGIALVSEDRK-----GEGLLLPQ-SIAANL 363
Cdd:PRK11144  29 IFGRSG---AGKTSLINAISGLTRPQKGRIVLNG-------RVLFDAEK-GICLPPEKRRigyvfQDARLFPHyKVRGNL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 364 SLGqLARVARggvvdgerenALAARQIDALRIRA---RGPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVG 440
Cdd:PRK11144  98 RYG-MAKSMV----------AQFDKIVALLGIEPlldRYPGS----LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 490656625 441 AKFDIYALLDALAREGR-AIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:PRK11144 163 RKRELLPYLERLAREINiPILYVSHSLDEILRLADRVVVLEQGKVKA 209
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
262-484 5.67e-07

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: 51.99  E-value: 5.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 262 PGAPRLRVERLS---RGD-----AVRDVSFDVRAGEIFGISGLIGAGRT----ELLRLVYGADAADGGTVS------IGD 323
Cdd:COG4172    2 MSMPLLSVEDLSvafGQGggtveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILfdgqdlLGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 324 PPRpaAIRspadAVR-HGIALVSEDrkgeglllPQSiAAN--LSLG-QLARVARggVVDGERENALAARQIDAL-RIRAR 398
Cdd:COG4172   82 SER--ELR----RIRgNRIAMIFQE--------PMT-SLNplHTIGkQIAEVLR--LHRGLSGAAARARALELLeRVGIP 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 399 GPAQPVA----ELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDL---RElm 470
Cdd:COG4172  145 DPERRLDayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLgvvRR-- 222
                        250
                 ....*....|....
gi 490656625 471 lICDRIGVMSAGRM 484
Cdd:COG4172  223 -FADRVAVMRQGEI 235
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
273-474 6.76e-07

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 50.92  E-value: 6.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 273 SRGDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALvsedrkg 350
Cdd:PRK11831  16 TRGNRCifDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSM------- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 351 egllLPQSIAANLSLGQLARVARGgVVDGERENALAARQIDALRIRA---RGPAQPV-AELSGGNQQKVAIGRWLGRDMG 426
Cdd:PRK11831  89 ----LFQSGALFTDMNVFDNVAYP-LREHTQLPAPLLHSTVMMKLEAvglRGAAKLMpSELSGGMARRAALARAIALEPD 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490656625 427 VLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICD 474
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIAD 212
PLN03211 PLN03211
ABC transporter G-25; Provisional
28-233 7.09e-07

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 51.80  E-value: 7.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVApttgAMRLAGAEYAPHSRAHAEALG-VRMVMQELNLVPTLTVA 106
Cdd:PLN03211  83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQ----GNNFTGTILANNRKPTKQILKrTGFVTQDDILYPHLTVR 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 107 ENLF---LDRLPHRfgvIDRRRLAADARAAMARVGLDSLDpDTLVGSLGI-----GHQQMVEIARSLAGDCRVLILDEPT 178
Cdd:PLN03211 159 ETLVfcsLLRLPKS---LTKQEKILVAESVISELGLTKCE-NTIIGNSFIrgisgGERKRVSIAHEMLINPSLLILDEPT 234
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 179 AMLTAREVELLFDQIARLKADGVALVYISHrlEELARVAQ---RVAVLRDGRLVHVDR 233
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMH--QPSSRVYQmfdSVLVLSEGRCLFFGK 290
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
32-84 9.85e-07

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: 51.34  E-value: 9.85e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490656625  32 VSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAH 84
Cdd:COG4615  351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREA 403
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
28-229 1.02e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 50.46  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL-GVRMVMQELN---LVPtl 103
Cdd:PRK13639  17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRkTVGIVFQNPDdqlFAP-- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAMLTA 183
Cdd:PRK13639  95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSG----GQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 490656625 184 REVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13639 171 MGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKII 216
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
277-491 1.06e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 50.40  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADaVRHGIALVSE--DRKGEGLL 354
Cdd:PRK13635  22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG--MVLSEETVWD-VRRQVGMVFQnpDNQFVGAT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LPQSIAANLSLGQlarVARGGVVdgERENAlAARQIDALRIRARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:PRK13635  99 VQDDVAFGLENIG---VPREEMV--ERVDQ-ALRQVGMEDFLNREPHR----LSGGQKQRVAIAGVLALQPDIIILDEAT 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 435 RGIDVGAKFDIYALLDALAREGRAIVV-VSSDLRElMLICDRIGVMSAGRMHA------VFERG 491
Cdd:PRK13635 169 SMLDPRGRREVLETVRQLKEQKGITVLsITHDLDE-AAQADRVIVMNKGEILEegtpeeIFKSG 231
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
277-486 1.08e-06

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 50.17  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVR-------------AGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRpAAIRSPADAvRHGIAL 343
Cdd:PRK10575  13 ALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL-ESWSSKAFA-RKVAYL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 344 VSEDRKGEGLLLPQSIAanlsLGQL---ARVARGGVVDGER-ENALAARQIDALRIRArgpaqpVAELSGGNQQKVAIGR 419
Cdd:PRK10575  91 PQQLPAAEGMTVRELVA----IGRYpwhGALGRFGAADREKvEEAISLVGLKPLAHRL------VDSLSGGERQRAWIAM 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 420 WLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
404-476 1.30e-06

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: 47.83  E-value: 1.30e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 404 VAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAkfdIYALLDALAREGRAIVVVSSDlRELM-LICDRI 476
Cdd:cd03221   68 FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES---IEALEEALKEYPGTVILVSHD-RYFLdQVATKI 137
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
32-523 1.37e-06

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 51.41  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   32 VSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVRMVMQELNLVPTLTVAEnlfL 111
Cdd:COG3321   861 VPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALA---A 937
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  112 DRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFD 191
Cdd:COG3321   938 AAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAA 1017
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  192 QIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGREIAEQAVHGTRTPGAPRLRVER 271
Cdd:COG3321  1018 AAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALAL 1097
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  272 LSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSEDRKGE 351
Cdd:COG3321  1098 ALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLAL 1177
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  352 GLLLPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFD 431
Cdd:COG3321  1178 ALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLA 1257
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  432 EPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAVFERGGWTQDALLGAAFAGYARRDA 511
Cdd:COG3321  1258 ALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAV 1337
                         490
                  ....*....|..
gi 490656625  512 ALHPPGGARSAA 523
Cdd:COG3321  1338 AAALALAAAAAA 1349
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
17-217 1.48e-06

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: 50.70  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   17 VTGIGKTYAEPVL-DDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGA---EYAPHSRAHaealgvrm 92
Cdd:TIGR03719 325 AENLTKAFGDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvklAYVDQSRDA-------- 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   93 vmqelnLVPTLTVAENLF--LDrlphrfgVIDRRRLAADARAAMARVGLDSLDPDTLVGSLGIGHQQMVEIARSLAGDCR 170
Cdd:TIGR03719 397 ------LDPNKTVWEEISggLD-------IIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGN 463
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 490656625  171 VLILDEPTAML---TAREVELlfdqiARLKADGVALVyISHRLEELARVA 217
Cdd:TIGR03719 464 VLLLDEPTNDLdveTLRALEE-----ALLNFAGCAVV-ISHDRWFLDRIA 507
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
26-226 1.52e-06

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 50.96  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRL-AGAEYA-------------------PHSRAHA 85
Cdd:COG4178  376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLflpqrpylplgtlreallyPATAEAF 455
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  86 EALGVRMVMQELNlvptltvaenlfLDRLPHRfgvidrrrlaadaraamarvgLDSLDPDTLVgsLGIGHQQMVEIARSL 165
Cdd:COG4178  456 SDAELREALEAVG------------LGHLAER---------------------LDEEADWDQV--LSLGEQQRLAFARLL 500
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 166 AGDCRVLILDEPTAMLTAREVELLFDQI-ARLKadGVALVYISHRlEELARVAQRVAVLRDG 226
Cdd:COG4178  501 LHKPDWLFLDEATSALDEENEAALYQLLrEELP--GTTVISVGHR-STLAAFHDRVLELTGD 559
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
277-461 1.87e-06

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 50.40  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLV---YgaDAADGGTVSIGDPPRPAAIRSpadaVRHGIALVSEDRKgegl 353
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLtrfY--DIDEGEILLDGHDLRDYTLAS----LRNQVALVSQNVH---- 427
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 LLPQSIAANLSLGQLARVARGGVVdgerENALAARQIDALRIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLL 429
Cdd:PRK11176 428 LFNDTIANNIAYARTEQYSREQIE----EAARMAYAMDFINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILI 503
                        170       180       190
                 ....*....|....*....|....*....|..
gi 490656625 430 FDEPTRGIDVGAKFDIYALLDALAREGRAIVV 461
Cdd:PRK11176 504 LDEATSALDTESERAIQAALDELQKNRTSLVI 535
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
27-223 2.10e-06

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: 47.92  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGamrlagaeyaphsrahaealgvRMVMqelnlvptLTVA 106
Cdd:cd03223   15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG----------------------RIGM--------PEGE 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 107 ENLFLDRLPHrfgvidrrrlaadaraamarvgldsLDPDTLVGS--------LGIGHQQMVEIARSLAGDCRVLILDEPT 178
Cdd:cd03223   65 DLLFLPQRPY-------------------------LPLGTLREQliypwddvLSGGEQQRLAFARLLLHKPKFVFLDEAT 119
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 490656625 179 AMLTArEVELLFDQIarLKADGVALVYISHRlEELARVAQRVAVL 223
Cdd:cd03223  120 SALDE-ESEDRLYQL--LKELGITVISVGHR-PSLWKFHDRVLDL 160
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
15-241 2.40e-06

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: 49.08  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  15 LVVTGIGKTYAE---PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVApTTGAMRLAGAEYAPHS-RAHAEALGV 90
Cdd:cd03289    3 MTVKDLTAKYTEggnAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPlQKWRKAFGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  91 rmVMQEL---------NLVP--------TLTVAENLFLDRLPHRFGvidrrrlaadaraamarvglDSLDPDTLVGS--L 151
Cdd:cd03289   82 --IPQKVfifsgtfrkNLDPygkwsdeeIWKVAEEVGLKSVIEQFP--------------------GQLDFVLVDGGcvL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 152 GIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADgVALVYISHRLEELARvAQRVAVLRDGRLVHV 231
Cdd:cd03289  140 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFAD-CTVILSEHRIEAMLE-CQRFLVIEENKVRQY 217
                        250
                 ....*....|
gi 490656625 232 DRIDAQPTER 241
Cdd:cd03289  218 DSIQKLLNEK 227
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
10-241 2.85e-06

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: 50.29  E-value: 2.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625    10 PDTPTLVVTGIGKTYAE---PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLvAPTTGAMRLAGAEYAPHS-RAHA 85
Cdd:TIGR01271 1213 PSGGQMDVQGLTAKYTEagrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTlQTWR 1291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625    86 EALGVrmVMQELnLVPTLTVAENLflDrlPHrfgvidRRRLAADARAAMARVGLDSLD---PDTLV-----GS--LGIGH 155
Cdd:TIGR01271 1292 KAFGV--IPQKV-FIFSGTFRKNL--D--PY------EQWSDEEIWKVAEEVGLKSVIeqfPDKLDfvlvdGGyvLSNGH 1358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   156 QQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADgVALVYISHRLEELARvAQRVAVLRDGRLVHVDRID 235
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN-CTVILSEHRVEALLE-CQQFLVIEGSSVKQYDSIQ 1436

                   ....*.
gi 490656625   236 AQPTER 241
Cdd:TIGR01271 1437 KLLNET 1442
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
276-465 3.00e-06

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 50.11  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGT-------VSIGDPPRPAAIRspadavRHGIALVSEDR 348
Cdd:PRK10535  22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdVATLDADALAQLR------REHFGFIFQRY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 349 KgeglLLPQSIAA-NLSL----GQLARVARGgvvdgERENALAARqidaLRIRARGPAQPvAELSGGNQQKVAIGRWLGR 423
Cdd:PRK10535  96 H----LLSHLTAAqNVEVpavyAGLERKQRL-----LRAQELLQR----LGLEDRVEYQP-SQLSGGQQQRVSIARALMN 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 490656625 424 DMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSD 465
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
PLN03232 PLN03232
ABC transporter C family member; Provisional
27-232 3.12e-06

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 50.36  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphsrahaeALGVRMVMQELNLVP----- 101
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--------KFGLTDLRRVLSIIPqspvl 1321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  102 -TLTVAENL--F-------LDRLPHRFGVIDRRRLAADaraamarvgldSLDPDTLVG--SLGIGHQQMVEIARSLAGDC 169
Cdd:PLN03232 1322 fSGTVRFNIdpFsehndadLWEALERAHIKDVIDRNPF-----------GLDAEVSEGgeNFSVGQRQLLSLARALLRRS 1390
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625  170 RVLILDEPTAMLTAReVELLFDQIARLKADGVALVYISHRLEELARvAQRVAVLRDGRLVHVD 232
Cdd:PLN03232 1391 KILVLDEATASVDVR-TDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYD 1451
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
27-229 3.58e-06

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


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 47.64  E-value: 3.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPT---TGAMRLAGAEYAP-HSRAHAEALgvrMVMQELNLVPT 102
Cdd:cd03233   21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEfAEKYPGEII---YVSEEDVHFPT 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENLfldrlphRFGVidrrrlaadaraamarvgldSLDPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAML- 181
Cdd:cd03233   98 LTVRETL-------DFAL--------------------RCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLd 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490656625 182 --TAREvellFDQIARLKAD---GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03233  151 ssTALE----ILKCIRTMADvlkTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
276-486 3.91e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 48.65  E-value: 3.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAAIRspadavrhgialvsEDRKGEGLL 354
Cdd:PRK13652  18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIR--------------EVRKFVGLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALR------IRARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVL 428
Cdd:PRK13652  84 FQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHmlgleeLRDRVPHH----LSGGEKKRVAIAGVIAMEPQVL 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 429 LFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELML-ICDRIGVMSAGRMHA 486
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPeMADYIYVMDKGRIVA 218
cbiO PRK13642
energy-coupling factor transporter ATPase;
29-240 4.63e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 48.55  E-value: 4.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyaphSRAHAEAL-----GVRMVMQEL-NLVPT 102
Cdd:PRK13642  23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG------ELLTAENVwnlrrKIGMVFQNPdNQFVG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAMLT 182
Cdd:PRK13642  97 ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSG----GQKQRVAVAGIIALRPEIIILDESTSMLD 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 183 AREVELLFDQIARLKAD-GVALVYISHRLEELARvAQRVAVLRDGRLVHvdriDAQPTE 240
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIK----EAAPSE 226
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
29-204 5.61e-06

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: 47.24  E-value: 5.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAG--LVAPTTGAMRLAGAEyaphsRAHAEALGVRMVMQELNLVPTLTVA 106
Cdd:cd03232   23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRP-----LDKNFQRSTGYVEQQDVHSPNLTVR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 107 ENLfldrlphRFgvidrrrlaadaraamarvgldsldpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREV 186
Cdd:cd03232   98 EAL-------RF--------------------------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
                        170
                 ....*....|....*...
gi 490656625 187 ELLFDQIARLKADGVALV 204
Cdd:cd03232  145 YNIVRFLKKLADSGQAIL 162
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
277-502 5.74e-06

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 48.42  E-value: 5.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSED-------RK 349
Cdd:PRK11308  30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpygslnpRK 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 350 GEGLLLPQSIAANLSLGQLARvarggvvdgeRENALAARQIDALRIR--ARGPAQpvaeLSGGNQQKVAIGRWLGRDMGV 427
Cdd:PRK11308 110 KVGQILEEPLLINTSLSAAER----------REKALAMMAKVGLRPEhyDRYPHM----FSGGQRQRIAIARALMLDPDV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 428 LLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRM------HAVFE--RGGWTQdAL 498
Cdd:PRK11308 176 VVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCvekgtkEQIFNnpRHPYTQ-AL 254

                 ....
gi 490656625 499 LGAA 502
Cdd:PRK11308 255 LSAT 258
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
277-484 6.18e-06

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 48.67  E-value: 6.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAirsPADAVRHGIALVSE------DRKG 350
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY---SEAALRQAISVVSQrvhlfsATLR 431
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 351 EGLLLPQSIAANLSLGQ-LARVARGGVVDGEreNALAA------RQidalrirargpaqpvaeLSGGNQQKVAIGRWLGR 423
Cdd:PRK11160 432 DNLLLAAPNASDEALIEvLQQVGLEKLLEDD--KGLNAwlgeggRQ-----------------LSGGEQRRLGIARALLH 492
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 424 DMGVLLFDEPTRGIDVGAKFDIYALLDALAReGRAIVVVSSDLREL--MlicDRIGVMSAGRM 484
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRLTGLeqF---DRICVMDNGQI 551
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
28-220 6.30e-06

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 47.17  E-value: 6.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGvrmvmQELNLVPTLTVAE 107
Cdd:PRK13541  15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG-----HNLGLKLEMTVFE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NL-----------FLDRLPHRFGVIDRRrlaadaraamarvgldsldpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDE 176
Cdd:PRK13541  90 NLkfwseiynsaeTLYAAIHYFKLHDLL--------------------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 490656625 177 PTAMLTAREVELLFDQIArLKADGVALVYISHRLEELARVAQRV 220
Cdd:PRK13541 150 VETNLSKENRDLLNNLIV-MKANSGGIVLLSSHLESSIKSAQIL 192
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
402-478 7.27e-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: 48.63  E-value: 7.27e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 402 QPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGV 478
Cdd:COG1245  451 KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLMV 528
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
407-483 8.14e-06

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 48.50  E-value: 8.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  407 LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVV----SSDLRELMlicDRIGVMSAG 482
Cdd:TIGR00955 167 LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFELF---DKIILMAEG 243

                  .
gi 490656625  483 R 483
Cdd:TIGR00955 244 R 244
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
277-484 8.98e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 47.38  E-value: 8.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPAdAVRHGIALVSEDRKGEglLLP 356
Cdd:PRK13639  17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLL-EVRKTVGIVFQNPDDQ--LFA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLGQLARvarggvvdGERENALAARQIDAL-RIRARG-PAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:PRK13639  94 PTVEEDVAFGPLNL--------GLSKEEVEKRVKEALkAVGMEGfENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490656625 435 RGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
358-484 9.15e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 47.21  E-value: 9.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 SIAANLSLG-QLARVARGGVVDGER-ENALAARQI-DALRIRARGPAqpvAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:PRK14247  98 SIFENVALGlKLNRLVKSKKELQERvRWALEKAQLwDEVKDRLDAPA---GKLSGGQQQRLCIARALAFQPEVLLADEPT 174
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 490656625 435 RGIDVGAKFDIYALLDALAREgRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQI 223
cbiO PRK13641
energy-coupling factor transporter ATPase;
280-495 1.01e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 47.52  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 280 DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPA-DAVRHGIALVSEdrKGEGLLLPQS 358
Cdd:PRK13641  25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlKKLRKKVSLVFQ--FPEAQLFENT 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 359 IAANLSLGQLarvaRGGVVDGERENAlaarqidALR-IRARGPAQPVA-----ELSGGNQQKVAIGRWLGRDMGVLLFDE 432
Cdd:PRK13641 103 VLKDVEFGPK----NFGFSEDEAKEK-------ALKwLKKVGLSEDLIskspfELSGGQMRRVAIAGVMAYEPEILCLDE 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 433 PTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM--HA----VFERGGWTQ 495
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLikHAspkeIFSDKEWLK 240
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
277-483 1.11e-05

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: 46.72  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTE----LLRLVYgadaADGGTVSIGDPPrpaaIRS-PADAVRHGIALVSEDrkge 351
Cdd:cd03244   19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVE----LSSGSILIDGVD----ISKiGLHDLRSRISIIPQD---- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 352 GLLLPQSIAANL-SLGQLArvarggvvDGERENALAARQIDA----------LRIRARGpaqpvAELSGGNQQKVAIGRW 420
Cdd:cd03244   87 PVLFSGTIRSNLdPFGEYS--------DEELWQALERVGLKEfveslpggldTVVEEGG-----ENLSVGQRQLLCLARA 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 421 LGRDMGVLLFDEPTRGIDVgakfDIYALLDALARE---GRAIVVVSSDLRELMlICDRIGVMSAGR 483
Cdd:cd03244  154 LLRKSKILVLDEATASVDP----ETDALIQKTIREafkDCTVLTIAHRLDTII-DSDRILVLDKGR 214
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
277-498 1.31e-05

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 47.39  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVS-IGDPPRPAAiRSPADAVRHGIALVSEDrkgeglll 355
Cdd:PRK15079  36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLGMK-DDEWRAVRSDIQMIFQD-------- 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 P-QSIAANLSLGQL---------ARVARGGVVDGEREN----ALAARQIDalriraRGPAqpvaELSGGNQQKVAIGRWL 421
Cdd:PRK15079 107 PlASLNPRMTIGEIiaeplrtyhPKLSRQEVKDRVKAMmlkvGLLPNLIN------RYPH----EFSGGQCQRIGIARAL 176
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 422 GRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGrmHAVfERGgwTQDAL 498
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLG--HAV-ELG--TYDEV 249
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
14-109 1.33e-05

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 47.53  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  14 TLVVTGIGKTYA--EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGA---EYAPHSRahaeal 88
Cdd:PRK11650   3 GLKLQAVRKSYDgkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnELEPADR------ 76
                         90       100
                 ....*....|....*....|.
gi 490656625  89 GVRMVMQELNLVPTLTVAENL 109
Cdd:PRK11650  77 DIAMVFQNYALYPHMSVRENM 97
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
24-74 1.38e-05

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: 46.77  E-value: 1.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490656625  24 YAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG 74
Cdd:cd03291   48 VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG 98
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
137-321 1.52e-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: 47.70  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  137 VGLDSLDPDTLVGSLGIGHQQMVEIARSL-AGDCRVL-ILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRlEELA 214
Cdd:TIGR00630 475 VGLDYLSLSRAAGTLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTI 553
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  215 RVAQRV------AVLRDGRLVH---VDRIDAQPTERLVALMAGREiaEQAVHGTRTPGAPRLRVERLSRGDAVRDVSFDV 285
Cdd:TIGR00630 554 RAADYVidigpgAGEHGGEVVAsgtPEEILANPDSLTGQYLSGRK--KIEVPAERRPGNGKFLTLKGARENNLKNITVSI 631
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 490656625  286 RAGEIFGISGLIGAGRTELL---------RLVYGADAADGGTVSI 321
Cdd:TIGR00630 632 PLGLFTCITGVSGSGKSTLIndtlypalaNRLNGAKTVPGRYTSI 676
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
28-232 1.59e-05

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: 48.02  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625    28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphsrahaeALGVRMVMQELNLVPTLTVae 107
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA--------KIGLHDLRFKITIIPQDPV-- 1370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   108 nLF-------LD--------------RLPHRFGVIDRRRlaadaraamarvglDSLDPDTLVG--SLGIGHQQMVEIARS 164
Cdd:TIGR00957 1371 -LFsgslrmnLDpfsqysdeevwwalELAHLKTFVSALP--------------DKLDHECAEGgeNLSVGQRQLVCLARA 1435
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625   165 LAGDCRVLILDEPTAMLTArEVELLFDQIARLKADGVALVYISHRLEELARVAqRVAVLRDGRLVHVD 232
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDL-ETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
261-468 1.81e-05

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 46.52  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 261 TPGAPRLRVERLSRG----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRL-------VYGADAADGGTVSigdpprpaa 329
Cdd:PRK10253   2 TESVARLRGEQLTLGygkyTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTlsrlmtpAHGHVWLDGEHIQ--------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 330 iRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGGVVDGEREN-ALAARQIDALrirargPAQPVAELS 408
Cdd:PRK10253  73 -HYASKEVARRIGLLAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTkAMQATGITHL------ADQSVDTLS 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 409 GGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRE 468
Cdd:PRK10253 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQ 206
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
154-258 1.97e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 46.65  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 154 GHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDR 233
Cdd:NF000106 148 GMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
                         90       100
                 ....*....|....*....|....*
gi 490656625 234 IDAQPTErlvalMAGREIAEQAVHG 258
Cdd:NF000106 228 VDELKTK-----VGGRTLQIRPAHA 247
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
12-210 2.28e-05

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 46.03  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  12 TPTLVVTGIGKTY--AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyAPHSRAHAEALg 89
Cdd:PRK15056   4 QAGIVVNDVTVTWrnGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG---QPTRQALQKNL- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  90 VRMVMQ--ELNLVPTLTVAENLFLDRLPHrFGVIDRRRLAADARAAMARVGLDSLD-PDTLVGSLGIGHQQMVEIARSLA 166
Cdd:PRK15056  80 VAYVPQseEVDWSFPVLVEDVVMMGRYGH-MGWLRRAKKRDRQIVTAALARVDMVEfRHRQIGELSGGQKKRVFLARAIA 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 490656625 167 GDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRL 210
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNL 202
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
145-240 2.30e-05

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 47.33  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  145 DTLVGS----LGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVAL-VYISHRLEELaRVAQR 219
Cdd:PTZ00265  570 ETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLSTI-RYANT 648
                          90       100
                  ....*....|....*....|....
gi 490656625  220 VAVLRD---GRLVHVDRIDAQPTE 240
Cdd:PTZ00265  649 IFVLSNrerGSTVDVDIIGEDPTK 672
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
13-224 2.47e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 46.18  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  13 PTLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLvAPTTGAMRLAG-AEYAPHS----RAHAE 86
Cdd:PRK14258   6 PAIKVNNLSFYYdTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGrVEFFNQNiyerRVNLN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  87 AL--GVRMVMQELNLVPtLTVAENLfldrlphRFGV----------IDRRRLAADARAAMARVGLDSLDPDTLvgSLGIG 154
Cdd:PRK14258  85 RLrrQVSMVHPKPNLFP-MSVYDNV-------AYGVkivgwrpkleIDDIVESALKDADLWDEIKHKIHKSAL--DLSGG 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 155 HQQMVEIARSLAGDCRVLILDEPTAML---TAREVELLFdQIARLKADgVALVYISHRLEELARVAQRVAVLR 224
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLdpiASMKVESLI-QSLRLRSE-LTMVIVSHNLHQVSRLSDFTAFFK 225
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
27-230 2.48e-05

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 47.01  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyAPHSRAHAEALGVRMVMqeLNLVPTL--- 103
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD---IPLTKLQLDSWRSRLAV--VSQTPFLfsd 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLFLDRlPhrfgviDRRRLAADARAAMARVGLDSLD-P---DTLVGSLGI----GHQQMVEIARSLAGDCRVLILD 175
Cdd:PRK10789 404 TVANNIALGR-P------DATQQEIEHVARLASVHDDILRlPqgyDTEVGERGVmlsgGQKQRISIARALLLNAEILILD 476
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 176 EPTAMLTAR-EVELLfdQIARLKADGVALVYISHRLEELARvAQRVAVLRDGRLVH 230
Cdd:PRK10789 477 DALSAVDGRtEHQIL--HNLRQWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQ 529
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
22-222 2.56e-05

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 45.86  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  22 KTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE--YAPhsrahaealgvrmvmQELNL 99
Cdd:cd03237    8 KTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTvsYKP---------------QYIKA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 100 VPTLTVAENLfldrlphrFGVIDRRRLAAD-ARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPT 178
Cdd:cd03237   73 DYEGTVRDLL--------SSITKDFYTHPYfKTEIAKPLQIEQI-LDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 490656625 179 AMLTAREVELLFDQIAR--LKADGVALVyISHRLEELARVAQRVAV 222
Cdd:cd03237  144 AYLDVEQRLMASKVIRRfaENNEKTAFV-VEHDIIMIDYLADRLIV 188
ycf16 CHL00131
sulfate ABC transporter protein; Validated
27-61 2.68e-05

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 45.79  E-value: 2.68e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAG 61
Cdd:CHL00131  21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
cbiO PRK13642
energy-coupling factor transporter ATPase;
267-484 2.88e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 45.85  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIgDPPRPAAIRSPADAVRHGIALVSE 346
Cdd:PRK13642  12 FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI-DGELLTAENVWNLRRKIGMVFQNP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 347 DRKGEGLLLPQSIAANLSLGQLARVARGGVVDgerENALAARQIDalrIRARGPAQpvaeLSGGNQQKVAIGRWLGRDMG 426
Cdd:PRK13642  91 DNQFVGATVEDDVAFGMENQGIPREEMIKRVD---EALLAVNMLD---FKTREPAR----LSGGQKQRVAVAGIIALRPE 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 427 VLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVV-VSSDLRElMLICDRIGVMSAGRM 484
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLsITHDLDE-AASSDRILVMKAGEI 218
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
267-474 3.57e-05

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 45.54  E-value: 3.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLS--RGD--AVRDVSFDVRAGEIFGISGLIGAGRTELLR-------LVYGADAAdgGTVSIGDPPRPAAIRSPAd 335
Cdd:PRK14243  11 LRTENLNvyYGSflAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRVE--GKVTFHGKNLYAPDVDPV- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 336 AVRHGIALVSEDRKGegllLPQSIAANLSLGqlARV-ARGGVVDGERENALaaRQI-------DALRirargpaQPVAEL 407
Cdd:PRK14243  88 EVRRRIGMVFQKPNP----FPKSIYDNIAYG--ARInGYKGDMDELVERSL--RQAalwdevkDKLK-------QSGLSL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 408 SGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALaREGRAIVVVSSDLRELMLICD 474
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSD 218
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
258-484 3.75e-05

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 45.41  E-value: 3.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 258 GTRTPGAPRLRVERLS--RGD--AVRDVSFDVRAGEIFGISGLIGAGRTELLR-------LVYGADAAdgGTVSIGDppr 326
Cdd:COG1117    3 APASTLEPKIEVRNLNvyYGDkqALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARVE--GEILLDG--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 327 pAAIRSP-ADAVRHgialvsedRKGEGLL------LPQSIAANLSLG-QLARVARGGVVDGERENALaaRQI-------D 391
Cdd:COG1117   78 -EDIYDPdVDVVEL--------RRRVGMVfqkpnpFPKSIYDNVAYGlRLHGIKSKSELDEIVEESL--RKAalwdevkD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 392 ALRirargpaQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREgRAIVVVSSDLRELML 471
Cdd:COG1117  147 RLK-------KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAAR 218
                        250
                 ....*....|...
gi 490656625 472 ICDRIGVMSAGRM 484
Cdd:COG1117  219 VSDYTAFFYLGEL 231
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
281-513 3.79e-05

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 46.38  E-value: 3.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 281 VSFDVRAGEIFGISGLIGAGRTELLRLVYGAdAADGGTVSI-GDPPRpaaiRSPADAVRHGIALVSEdrkgEGLLLPQSI 359
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKInGIELR----ELDPESWRKHLSWVGQ----NPQLPHGTL 439
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 360 AANLSLGQLArvarggVVDGERENALAARQI-DALRIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:PRK11174 440 RDNVLLGNPD------ASDEQLQQALENAWVsEFLPLLPQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPT 513
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 435 RGIDVGAKfdiYALLDAL--AREGRAIVVVSSDLRELMLiCDRIGVMSAGRmhaVFERGGWTQDALLGAAFAG-YARRDA 511
Cdd:PRK11174 514 ASLDAHSE---QLVMQALnaASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQ---IVQQGDYAELSQAGGLFATlLAHRQE 586

                 ..
gi 490656625 512 AL 513
Cdd:PRK11174 587 EI 588
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
2-181 3.96e-05

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: 46.32  E-value: 3.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   2 DSTDPDSTPDTPTLVV-TGIGKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAM----RLAgae 76
Cdd:COG1245  328 EVHAPRREKEEETLVEyPDLTKSYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlKIS--- 404
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  77 YAPhsrahaealgvrmvmQELNLVPTLTVAENLFlDRLPHRFG-------VIDrrrlaadaraamaRVGLDSLdPDTLVG 149
Cdd:COG1245  405 YKP---------------QYISPDYDGTVEEFLR-SANTDDFGssyykteIIK-------------PLGLEKL-LDKNVK 454
                        170       180       190
                 ....*....|....*....|....*....|..
gi 490656625 150 SLGIGHQQMVEIARSLAGDCRVLILDEPTAML 181
Cdd:COG1245  455 DLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
24-74 4.01e-05

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 46.44  E-value: 4.01e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 490656625    24 YAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG 74
Cdd:TIGR01271  437 YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG 487
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
30-178 4.14e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 46.27  E-value: 4.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  30 DDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAhaealgVRM---VM-QELNLVPTLTV 105
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIA------TRRrvgYMsQAFSLYGELTV 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLFLD-RLPH---------------RFGVIDRrrlaadaraamarvgLDSLdPDTLvgSLGIgHQQMveiarSLAGDC 169
Cdd:NF033858 357 RQNLELHaRLFHlpaaeiaarvaemleRFDLADV---------------ADAL-PDSL--PLGI-RQRL-----SLAVAV 412
                        170
                 ....*....|...
gi 490656625 170 ----RVLILDEPT 178
Cdd:NF033858 413 ihkpELLILDEPT 425
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
267-463 4.36e-05

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: 45.95  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  267 LRVERLSRG----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADA--ADGGTV-----------------SIGD 323
Cdd:TIGR03269   1 IEVKNLTKKfdgkEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpsKVGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  324 P---------PRPAAIRSPADAVRHGI------------ALVSEDRkgeglLLPQSIAANLSLGQLARVARGGVVDGERE 382
Cdd:TIGR03269  81 PcpvcggtlePEEVDFWNLSDKLRRRIrkriaimlqrtfALYGDDT-----VLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  383 NALAARQIDALRirargpaqpvaELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGID-VGAKFDIYALLDALAREGRAIVV 461
Cdd:TIGR03269 156 VQLSHRITHIAR-----------DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKLVHNALEEAVKASGISMVL 224

                  ..
gi 490656625  462 VS 463
Cdd:TIGR03269 225 TS 226
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
257-486 4.92e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 45.50  E-value: 4.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 257 HGTRTPGAPRLRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAG--RTELLRLVYGADAADggtvsigDPPRPAAIRSPA 334
Cdd:NF000106   8 NGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGR-------RPWRF*TWCANR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 335 DAVRHGIALVSEDRKGEglllPQSIAANLSLGQLARVarggvVDGERENALAarQIDALRIR---ARGPAQPVAELSGGN 411
Cdd:NF000106  81 RALRRTIG*HRPVR*GR----RESFSGRENLYMIGR*-----LDLSRKDARA--RADELLERfslTEAAGRAAAKYSGGM 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 412 QQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:NF000106 150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
27-229 6.67e-05

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 44.76  E-value: 6.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVRMVM--QELNLVPTLT 104
Cdd:PRK11831  21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMlfQSGALFTDMN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 105 VAENLFL-----DRLPhrfgvidRRRLAADARAAMARVGLD---SLDPDTLVGslgiGHQQMVEIARSLAGDCRVLILDE 176
Cdd:PRK11831 101 VFDNVAYplrehTQLP-------APLLHSTVMMKLEAVGLRgaaKLMPSELSG----GMARRAALARAIALEPDLIMFDE 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490656625 177 PTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK11831 170 PFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIV 223
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
406-482 6.82e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 45.01  E-value: 6.82e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 406 ELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAG 482
Cdd:PRK13634 145 ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKG 222
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
6-88 9.02e-05

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 44.96  E-value: 9.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   6 PDSTPDTPTLVVTGIGKTYAEP--VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRA 83
Cdd:PRK10522 314 PQAFPDWQTLELRNVTFAYQDNgfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE 393

                 ....*
gi 490656625  84 HAEAL 88
Cdd:PRK10522 394 DYRKL 398
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
265-484 9.81e-05

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: 43.41  E-value: 9.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADG---GTVSIGD-PPRPAAIRSPADavrhg 340
Cdd:cd03233   10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGiPYKEFAEKYPGE----- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 341 IALVSEDrkgeglllpQSIAANLSLGQLARVArggvvdgerenalaarqidalrIRARGpAQPVAELSGGNQQKVAIGRW 420
Cdd:cd03233   85 IIYVSEE---------DVHFPTLTVRETLDFA----------------------LRCKG-NEFVRGISGGERKRVSIAEA 132
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 421 LGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVS----SDlrELMLICDRIGVMSAGRM 484
Cdd:cd03233  133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSlyqaSD--EIYDLFDKVLVLYEGRQ 198
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
284-439 1.05e-04

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: 43.94  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 284 DVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVsigdpprpaairspadavrhGIALVSEDRKgeglllPQSIAANL 363
Cdd:cd03237   21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--------------------EIELDTVSYK------PQYIKADY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 364 SL---GQLARVARGGVVDGERENALA-ARQIDALRirargpAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDV 439
Cdd:cd03237   75 EGtvrDLLSSITKDFYTHPYFKTEIAkPLQIEQIL------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
279-483 1.25e-04

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: 43.23  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 279 RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairspadavrhGIALVSEdrkgEGLLLPQS 358
Cdd:cd03250   22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG----------------SIAYVSQ----EPWIQNGT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 359 IAANLSLGQlarvarggVVDGER-ENALAARQIDA-LRIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDE 432
Cdd:cd03250   82 IRENILFGK--------PFDEERyEKVIKACALEPdLEILPDGDLTEIGEkginLSGGQKQRISLARAVYSDADIYLLDD 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490656625 433 PTRGID--VGAK-FDiYALLDALaREGRAIVVVSSDLrELMLICDRIGVMSAGR 483
Cdd:cd03250  154 PLSAVDahVGRHiFE-NCILGLL-LNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
17-72 1.30e-04

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 44.72  E-value: 1.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625  17 VTGIGKTYAEPVL-DDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRL 72
Cdd:PRK11819 327 AENLSKSFGDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
29-229 1.38e-04

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 43.96  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLV----APTTGAMRLAGAEY---APHSRAHAEALGVRMVMQE--LNL 99
Cdd:PRK11022  23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLqriSEKERRNLVGAEVAMIFQDpmTSL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 100 VPTLTVAENLFLDRLPHRFGviDRRRLAADARAAMARVGLDslDP----DTLVGSLGIGHQQMVEIARSLAGDCRVLILD 175
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVHQGG--NKKTRRQRAIDLLNQVGIP--DPasrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 176 EPTAML----TAREVELLFDQIARlkaDGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK11022 179 EPTTALdvtiQAQIIELLLELQQK---ENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
402-478 1.46e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 44.41  E-value: 1.46e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 402 QPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGV 478
Cdd:PRK13409 449 KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLMV 526
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
265-466 1.47e-04

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 42.94  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLS--RGDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAAIRSPADAVRH 339
Cdd:PRK13539   1 MMLEGEDLAcvRGGRVlfSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdGGDIDDPDVAEACHYLGH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 340 GIALvsedrKGEglllpQSIAANLSLgqLARVARGGvvDGERENALAARQIDALRIRargpaqPVAELSGGNQQKVAIGR 419
Cdd:PRK13539  81 RNAM-----KPA-----LTVAENLEF--WAAFLGGE--ELDIAAALEAVGLAPLAHL------PFGYLSAGQKRRVALAR 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 490656625 420 WLGRDMGVLLFDEPTRGIDVGAKFDIYALLDA-LAREGRAIVVVSSDL 466
Cdd:PRK13539 141 LLVSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIVIAATHIPL 188
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
277-491 1.61e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 43.59  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRH-GIALVSEDRKGEGLLL 355
Cdd:PRK13648  24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN--QAITDDNFEKLRKHiGIVFQNPDNQFVGSIV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 PQSIAANLslgqlarvaRGGVVDGERENALAARQIDALRIRARGPAQPVAeLSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:PRK13648 102 KYDVAFGL---------ENHAVPYDEMHRRVSEALKQVDMLERADYEPNA-LSGGQKQRVAIAGVLALNPSVIILDEATS 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 436 GIDVGAKFDIYALLDALAREGR-AIVVVSSDLRELMLiCDRIGVMSAGRmhaVFERG 491
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGT---VYKEG 224
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
150-241 1.62e-04

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 43.62  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 150 SLGIGHQQMVEIARSLAGDCRVLILDEPTAML---TAREVELLFDQIARlkadGVALVYISHRLEELARVAQRVAVL--- 223
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALdpiSTLRIEELMHELKE----QYTIIIVTHNMQQAARVSDMTAFFnve 226
                         90       100
                 ....*....|....*....|....*..
gi 490656625 224 ------RDGRLVHVDR---IDAQPTER 241
Cdd:PRK14243 227 ltegggRYGYLVEFDRtekIFNSPQQQ 253
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
281-475 1.87e-04

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 42.84  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 281 VSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRhgialvsedRKGEGLLLpQSIA 360
Cdd:PRK10584  29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLR---------AKHVGFVF-QSFM 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 361 ANLSLGQLARVARGGVVDGERENALAARQIDALRIRARG------PAQpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:PRK10584  99 LIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGkrldhlPAQ----LSGGEQQRVALARAFNGRPDVLFADEPT 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 490656625 435 RGIDVGAKFDIYALLDALARE-GRAIVVVSSDLReLMLICDR 475
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQ-LAARCDR 215
PLN03211 PLN03211
ABC transporter G-25; Provisional
288-483 1.94e-04

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 44.10  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 288 GEIFGISGLIGAGRTELLRLVYGADAADG--GTVSIGD--PPRPAAIRS----------PADAVRHGIALVSEDR----- 348
Cdd:PLN03211  94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNrkPTKQILKRTgfvtqddilyPHLTVRETLVFCSLLRlpksl 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 349 -KGEGLLLPQSIAANLSLGQLarvarggvvdgerENALAARQIdalrIRArgpaqpvaeLSGGNQQKVAIGRWLGRDMGV 427
Cdd:PLN03211 174 tKQEKILVAESVISELGLTKC-------------ENTIIGNSF----IRG---------ISGGERKRVSIAHEMLINPSL 227
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 428 LLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVV----SSDLRELMlicDRIGVMSAGR 483
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSmhqpSSRVYQMF---DSVLVLSEGR 284
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
406-478 2.04e-04

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 42.17  E-value: 2.04e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 406 ELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREG-RAIVVVSSDLRELMLICDRIGV 478
Cdd:cd03222   71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIHV 144
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
240-501 2.38e-04

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 43.94  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 240 ERLVALMAGREiaEQAVHGTRTPGAPRLRVERLS---RGD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAA 314
Cdd:PRK10790 316 ERVFELMDGPR--QQYGNDDRPLQSGRIDIDNVSfayRDDnlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL 393
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 315 DGGTVSIGDppRPAAIRSPAdAVRHGIALVSEDRkgegLLLPQSIAANLSLGQlaRVARGGVVDgerenALAARQIDAL- 393
Cdd:PRK10790 394 TEGEIRLDG--RPLSSLSHS-VLRQGVAMVQQDP----VVLADTFLANVTLGR--DISEEQVWQ-----ALETVQLAELa 459
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 394 RIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLdALAREGRAIVVVSSDLREL 469
Cdd:PRK10790 460 RSLPDGLYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLVVIAHRLSTI 538
                        250       260       270
                 ....*....|....*....|....*....|..
gi 490656625 470 mLICDRIGVMSAGRmhaVFERGgwTQDALLGA 501
Cdd:PRK10790 539 -VEADTILVLHRGQ---AVEQG--THQQLLAA 564
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
407-484 2.50e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 43.16  E-value: 2.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 407 LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALArEGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRL 240
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
29-75 3.13e-04

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 43.34  E-value: 3.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 490656625  29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGA 75
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS 86
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
6-181 3.52e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 43.26  E-value: 3.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   6 PDSTPDTPTLVV-TGIGKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAM----RLAgaeYAPh 80
Cdd:PRK13409 331 PRDESERETLVEyPDLTKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelKIS---YKP- 406
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  81 srahaealgvrmvmQELNLVPTLTVAEnlFLDRLPHRFG-------VIDrrrlaadaraamaRVGLDSLdPDTLVGSLGI 153
Cdd:PRK13409 407 --------------QYIKPDYDGTVED--LLRSITDDLGssyykseIIK-------------PLQLERL-LDKNVKDLSG 456
                        170       180
                 ....*....|....*....|....*...
gi 490656625 154 GHQQMVEIARSLAGDCRVLILDEPTAML 181
Cdd:PRK13409 457 GELQRVAIAACLSRDADLYLLDEPSAHL 484
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
267-464 4.49e-04

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 41.71  E-value: 4.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERL--SRGDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRSPADAVR---- 338
Cdd:PRK13538   2 LEARNLacERDERIlfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP----IRRQRDEYHqdll 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 339 ---HGIALVSEDRKGEGLLLPQSIAANLSLGQ----LARVARGGvvdgeRENAlaarqidalrirargpaqPVAELSGGN 411
Cdd:PRK13538  78 ylgHQPGIKTELTALENLRFYQRLHGPGDDEAlweaLAQVGLAG-----FEDV------------------PVRQLSAGQ 134
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490656625 412 QQKVAIGR-WLGRDMGVLLfDEPTRGIDVGAKFDIYALLDALAREGrAIVVVSS 464
Cdd:PRK13538 135 QRRVALARlWLTRAPLWIL-DEPFTAIDKQGVARLEALLAQHAEQG-GMVILTT 186
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
406-483 5.16e-04

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 42.10  E-value: 5.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 406 ELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAR-EGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQ 236
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
277-484 6.27e-04

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 42.00  E-value: 6.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaaiRSPadavrhgialvSEDRKgeglllp 356
Cdd:COG4586   37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-------YVP-----------FKRRK------- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 qsiaanlslgQLARvaRGGVVDGERENA---LAAR----------QIDALRIRAR----------GP--AQPVAELSggn 411
Cdd:COG4586   92 ----------EFAR--RIGVVFGQRSQLwwdLPAIdsfrllkaiyRIPDAEYKKRldelvelldlGEllDTPVRQLS--- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 412 qqkvaigrwLGRDM------------GVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSS-DLRELMLICDRIGV 478
Cdd:COG4586  157 ---------LGQRMrcelaaallhrpKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTShDMDDIEALCDRVIV 227

                 ....*.
gi 490656625 479 MSAGRM 484
Cdd:COG4586  228 IDHGRI 233
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
369-498 6.72e-04

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 42.31  E-value: 6.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 369 ARVARGGVVDGERENALAAR-QIDALRIRargpaqPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYA 447
Cdd:PRK10938 103 AEIIQDEVKDPARCEQLAQQfGITALLDR------RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490656625 448 LLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAVFERGGWTQDAL 498
Cdd:PRK10938 177 LLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQAL 227
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
280-469 6.87e-04

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 41.24  E-value: 6.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 280 DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPP----RPAAIR--------SPA---DAVRHGIALV 344
Cdd:PRK10247  25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDistlKPEIYRqqvsycaqTPTlfgDTVYDNLIFP 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 345 SEDRKGEglLLPQSIAANLSLGQLArvarggvvdgerENALAarqidalrirargpaQPVAELSGGNQQKVAIGRWLGRD 424
Cdd:PRK10247 105 WQIRNQQ--PDPAIFLDDLERFALP------------DTILT---------------KNIAELSGGEKQRISLIRNLQFM 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 490656625 425 MGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLREL 469
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEI 201
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
406-517 7.52e-04

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 41.65  E-value: 7.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 406 ELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAR-EGRAIVVVSSDLRELMLICDRIGVMSA--- 481
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAgqv 232
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 490656625 482 ---GRMHAVFE--RGGWTQdALLGA--AFAGYARRDAALhpPG 517
Cdd:PRK11022 233 vetGKAHDIFRapRHPYTQ-ALLRAlpEFAQDKARLASL--PG 272
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
277-321 9.07e-04

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 41.80  E-value: 9.07e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI 321
Cdd:PRK13545  39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI 83
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
280-438 1.04e-03

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 41.24  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 280 DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAAIRspadavRHGIALVSEDRKgeglLLPQ- 357
Cdd:PRK11432  24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDVTHRSIQ------QRDICMVFQSYA----LFPHm 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 SIAANLSLG-QLARVARGGVVDGEREnALAARQIDALRIRArgpaqpVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:PRK11432  94 SLGENVGYGlKMLGVPKEERKQRVKE-ALELVDLAGFEDRY------VDQISGGQQQRVALARALILKPKVLLFDEPLSN 166

                 ..
gi 490656625 437 ID 438
Cdd:PRK11432 167 LD 168
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
30-211 1.11e-03

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: 40.00  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  30 DDVSLalyPGEAL-ALTGENGAGKSTLskIVAGLVAptTGAMRLAGaeyaphsrahaealgvrmvmqelnLVPTLTVAEN 108
Cdd:cd03238   14 LDVSI---PLNVLvVVTGVSGSGKSTL--VNEGLYA--SGKARLIS------------------------FLPKFSRNKL 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 109 LFLDRLphRFgVIDrrrlaadaraamarVGLDSLDPDTLVGSLGIGHQQMVEIARSLAGDCR--VLILDEPTAMLTAREV 186
Cdd:cd03238   63 IFIDQL--QF-LID--------------VGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
                        170       180
                 ....*....|....*....|....*
gi 490656625 187 ELLFDQIARLKADGVALVYISHRLE 211
Cdd:cd03238  126 NQLLEVIKGLIDLGNTVILIEHNLD 150
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
145-215 1.17e-03

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 41.94  E-value: 1.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625  145 DTLVG----SLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARL--KADGvALVYISHRLEELAR 215
Cdd:PTZ00265 1349 DTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADK-TIITIAHRIASIKR 1424
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
26-211 1.34e-03

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 40.33  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLV--APTTGAMRLAGAEYaPHSRAHAEALGVRM----VMQELNL 99
Cdd:COG2401   43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF-GREASLIDAIGRKGdfkdAVELLNA 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 100 VPTLTVAenLFLDRLPHrfgvidrrrlaadaraamarvgldsldpdtlvgsLGIGHQQMVEIARSLAGDCRVLILDEPTA 179
Cdd:COG2401  122 VGLSDAV--LWLRRFKE----------------------------------LSTGQKFRFRLALLLAERPKLLVIDEFCS 165
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 490656625 180 ML---TAREVELLFDQIARLKadGVALVYISHRLE 211
Cdd:COG2401  166 HLdrqTAKRVARNLQKLARRA--GITLVVATHHYD 198
PLN03232 PLN03232
ABC transporter C family member; Provisional
26-226 1.61e-03

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 41.50  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAP--TTGAMRLAGAEYAPhsrahaealgvrmvmqELNLVPTL 103
Cdd:PLN03232  630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaeTSSVVIRGSVAYVP----------------QVSWIFNA 693
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  104 TVAENLFL--DRLPHRFG-VIDRRRLAADARAAMarvGLDSldpdTLVGSLGI----GHQQMVEIARSLAGDCRVLILDE 176
Cdd:PLN03232  694 TVRENILFgsDFESERYWrAIDVTALQHDLDLLP---GRDL----TEIGERGVnisgGQKQRVSMARAVYSNSDIYIFDD 766
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 490656625  177 PTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVaQRVAVLRDG 226
Cdd:PLN03232  767 PLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEG 815
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
137-220 3.14e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 40.58  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  137 VGLDSLDPDTLVGSLGIGHQQMVEIARSLAGDCR--VLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRlEELA 214
Cdd:PRK00635  463 LGLPYLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMI 541

                  ....*.
gi 490656625  215 RVAQRV 220
Cdd:PRK00635  542 SLADRI 547
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
28-184 3.38e-03

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 40.48  E-value: 3.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625    28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVapTTGAM----RLAGAeyapHSRAHAEALGVRMVMQELNLVPTL 103
Cdd:TIGR00956  778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVItggdRLVNG----RPLDSSFQRSIGYVQQQDLHLPTS 851
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   104 TVAENL----FLdRLPHRFG----------VIDrrrlaadaraamaRVGLDSLdPDTLVGSLGIG----HQQMVEIARSL 165
Cdd:TIGR00956  852 TVRESLrfsaYL-RQPKSVSksekmeyveeVIK-------------LLEMESY-ADAVVGVPGEGlnveQRKRLTIGVEL 916
                          170       180
                   ....*....|....*....|
gi 490656625   166 AGDCRVLI-LDEPTAMLTAR 184
Cdd:TIGR00956  917 VAKPKLLLfLDEPTSGLDSQ 936
PLN03130 PLN03130
ABC transporter C family member; Provisional
281-508 3.54e-03

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 40.11  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  281 VSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairspADAVRHGIAlvsEDRKGEGLLlPQSia 360
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG----------CDISKFGLM---DLRKVLGII-PQA-- 1321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  361 anlslgqlaRVARGGVV-----------DGERENALA-ARQIDALRIRARGPAQPVAE----LSGGNQQKVAIGRWLGRD 424
Cdd:PLN03130 1322 ---------PVLFSGTVrfnldpfnehnDADLWESLErAHLKDVIRRNSLGLDAEVSEagenFSVGQRQLLSLARALLRR 1392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  425 MGVLLFDEPTRGIDVGAkfdiyallDALaregraivvVSSDLRE-----LMLI----------CDRIGVMSAGRmhaVFE 489
Cdd:PLN03130 1393 SKILVLDEATAAVDVRT--------DAL---------IQKTIREefkscTMLIiahrlntiidCDRILVLDAGR---VVE 1452
                         250       260
                  ....*....|....*....|..
gi 490656625  490 RGgwTQDALL---GAAFAGYAR 508
Cdd:PLN03130 1453 FD--TPENLLsneGSAFSKMVQ 1472
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
27-226 3.74e-03

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: 38.85  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG---VRMVMQELNLVpTL 103
Cdd:cd03290   15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQKPWLL-NA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLFLDRlP---HRF-GVIDRRrlaadaraamarvgldSLDPD---------TLVGSLGI----GHQQMVEIARSLA 166
Cdd:cd03290   94 TVEENITFGS-PfnkQRYkAVTDAC----------------SLQPDidllpfgdqTEIGERGInlsgGQRQRICVARALY 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 167 GDCRVLILDEPTAMLTAREVELLFDQ--IARLKADGVALVYISHRLEELARvAQRVAVLRDG 226
Cdd:cd03290  157 QNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
407-466 3.85e-03

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 40.09  E-value: 3.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  407 LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKfdiYALLDALAREGRAIVVVSSDL 466
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECE---QLLQESRSRASRTVLLIAHRL 674
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
27-95 4.09e-03

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 39.00  E-value: 4.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625  27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGL--VAPTTGAMRLAGA---EYAPHSRAhaeALGVRMVMQ 95
Cdd:PRK09580  15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKdllELSPEDRA---GEGIFMAFQ 85
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
405-464 4.19e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 39.05  E-value: 4.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 405 AELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGID-VGAKfDIYALLDALAREGRAIVVVSS 464
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDpVGTA-KIEELLFELKKEYTIVLVTHS 207
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
400-476 4.94e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 39.81  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  400 PAQPVAELSGGNQQKVAIGRWLGRD-MGVL-LFDEPTRGIDvgaKFDIYALLDALAR---EGRAIVVVSSDlrELML-IC 473
Cdd:PRK00635  470 PERALATLSGGEQERTALAKHLGAElIGITyILDEPSIGLH---PQDTHKLINVIKKlrdQGNTVLLVEHD--EQMIsLA 544

                  ...
gi 490656625  474 DRI 476
Cdd:PRK00635  545 DRI 547
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
407-501 5.21e-03

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 39.63  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625  407 LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGA-KFDIYALLDALAREGRAIVVVSSDLRELMLiCDRIGVMSAGRMH 485
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSeKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNPDRT 1437
                          90
                  ....*....|....*.
gi 490656625  486 AVFERGGWTQDALLGA 501
Cdd:PTZ00265 1438 GSFVQAHGTHEELLSV 1453
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
10-61 5.29e-03

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 39.23  E-value: 5.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490656625  10 PDTPTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAG 61
Cdd:PRK10938 256 ANEPRIVLNNGVVSYNDrPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
402-467 5.65e-03

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: 38.07  E-value: 5.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 402 QPVAELSGGNQQKVAIGRWLGRDMG--VLLFDEPTRGIDvgaKFDIYALLDALAR---EGRAIVVVSSDLR 467
Cdd:cd03238   83 QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH---QQDINQLLEVIKGlidLGNTVILIEHNLD 150
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
25-68 5.73e-03

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 39.49  E-value: 5.73e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 490656625  25 AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTG 68
Cdd:PRK15064  13 AKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAG 56
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
278-490 8.17e-03

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 38.14  E-value: 8.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRT----ELLRLVYGADAADGGTVSI-GDPPRPAAIRSpadavRHGIALVSEDRKGEG 352
Cdd:PRK10418  19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLdGKPVAPCALRG-----RKIATIMQNPRSAFN 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 353 LLlpQSIAAN-----LSLGQLARVARggVVDGERENALAarqiDALRIRARGPaqpvAELSGGNQQKVAIGRWLGRDMGV 427
Cdd:PRK10418  94 PL--HTMHTHaretcLALGKPADDAT--LTAALEAVGLE----NAARVLKLYP----FEMSGGMLQRMMIALALLCEAPF 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 428 LLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRM------HAVFER 490
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIveqgdvETLFNA 231
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
38-235 8.40e-03

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: 36.97  E-value: 8.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625    38 PGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEyaphsrahaealgvrmvmqelnlvptltvaenlfldrlphr 117
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625   118 fgvidrrrlaadarAAMARVGLDSLDPDTLVGSLGIGHQQMVEIARSLA--GDCRVLILDEPTAMLTAREVELLFDQIA- 194
Cdd:smart00382  40 --------------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALArkLKPDVLILDEITSLLDAEQEALLLLLEEl 105
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 490656625   195 -----RLKADGVALVYISHRLEELARvaqRVAVLRDGRLVHVDRID 235
Cdd:smart00382 106 rllllLKSEKNLTVILTTNDEKDLGP---ALLRRRFDRRIVLLLIL 148
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
390-477 8.46e-03

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: 37.61  E-value: 8.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 390 IDALRIRA--RGpaqpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVV----S 463
Cdd:cd03232   97 REALRFSAllRG-------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTihqpS 169
                         90
                 ....*....|....*..
gi 490656625 464 SDLREL---MLICDRIG 477
Cdd:cd03232  170 ASIFEKfdrLLLLKRGG 186
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
279-463 1.00e-02

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 37.63  E-value: 1.00e-02
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 279 RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGA--DAADGGTVSIGD--PPRPAAIrspADAVrhgialvseDRKGEgll 354
Cdd:COG2401   47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDVPDnqFGREASL---IDAI---------GRKGD--- 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 lpqsiaANLSLGQLARVARGgvvdgerenalaarqiDALRIRArgpaqPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:COG2401  112 ------FKDAVELLNAVGLS----------------DAVLWLR-----RFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
                        170       180       190
                 ....*....|....*....|....*....|
gi 490656625 435 RGID-VGAKFDIYALLDALAREGRAIVVVS 463
Cdd:COG2401  165 SHLDrQTAKRVARNLQKLARRAGITLVVAT 194
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH