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Conserved domains on  [gi|491046221|ref|WP_004907876|]
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MULTISPECIES: sugar ABC transporter ATP-binding protein [Providencia]

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

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List of domain hits

Name Accession Description Interval E-value
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
10-505 0e+00

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


:

Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 649.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:COG1129    1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGE-ILLDGEPVRFRSPRDAQAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 GVQVIYQDLSLFPNLTVAENIAFElNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:COG1129   80 GIAIIHQELNLVPNLSVAENIFLG-REPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMTG 249
Cdd:COG1129  159 ARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 250 LDIvHERKPPNNAEDRRTVLEIKNLSRAGQYRDINLNLKRGEVlglcgllgsgRTELALSLFGITHPDSGELFIEGKPVK 329
Cdd:COG1129  239 REL-EDLFPKRAAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEIlgiaglvgagRTELARALFGADPADSGEIRLDGKPVR 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 330 LKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLkTPWHLIDEKQCQDIVQEWIADLDIKVTDPNNALSTLS 409
Cdd:COG1129  318 IRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRL-SRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLS 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 410 GGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKEI 489
Cdd:COG1129  397 GGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGEL 476
                        490
                 ....*....|....*.
gi 491046221 490 VTDSINEQQLEEIING 505
Cdd:COG1129  477 DREEATEEAIMAAATG 492
 
Name Accession Description Interval E-value
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
10-505 0e+00

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 649.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:COG1129    1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGE-ILLDGEPVRFRSPRDAQAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 GVQVIYQDLSLFPNLTVAENIAFElNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:COG1129   80 GIAIIHQELNLVPNLSVAENIFLG-REPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMTG 249
Cdd:COG1129  159 ARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 250 LDIvHERKPPNNAEDRRTVLEIKNLSRAGQYRDINLNLKRGEVlglcgllgsgRTELALSLFGITHPDSGELFIEGKPVK 329
Cdd:COG1129  239 REL-EDLFPKRAAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEIlgiaglvgagRTELARALFGADPADSGEIRLDGKPVR 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 330 LKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLkTPWHLIDEKQCQDIVQEWIADLDIKVTDPNNALSTLS 409
Cdd:COG1129  318 IRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRL-SRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLS 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 410 GGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKEI 489
Cdd:COG1129  397 GGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGEL 476
                        490
                 ....*....|....*.
gi 491046221 490 VTDSINEQQLEEIING 505
Cdd:COG1129  477 DREEATEEAIMAAATG 492
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
10-498 2.89e-141

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 415.87  E-value: 2.89e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS-KIEIDGKSYHRLTPDKARE 88
Cdd:PRK13549   2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEgEIIFEGEELQASNIRDTER 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  89 LGVQVIYQDLSLFPNLTVAENIaFELNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVA 168
Cdd:PRK13549  82 AGIAIIHQELALVKELSVLENI-FLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 169 DARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMT 248
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 249 GLDIVhERKPPNNAEDRRTVLEIKNLS-------RAGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDS-GE 320
Cdd:PRK13549 241 GRELT-ALYPREPHTIGEVILEVRNLTawdpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 321 LFIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLkTPWHLIDEKQCQDIVQEWIADLDIKVTD 400
Cdd:PRK13549 320 IFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRF-TGGSRIDDAAELKTILESIQRLKVKTAS 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 401 PNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHM 480
Cdd:PRK13549 399 PELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVM 478
                        490
                 ....*....|....*...
gi 491046221 481 KQGSIVKEIVTDSINEQQ 498
Cdd:PRK13549 479 HEGKLKGDLINHNLTQEQ 496
GguA NF040905
sugar ABC transporter ATP-binding protein;
16-489 5.47e-116

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 351.01  E-value: 5.47e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  16 LRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYApdDGS---KIEIDGKSYHRLTPDKARELGVQ 92
Cdd:NF040905   4 MRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP--HGSyegEILFDGEVCRFKDIRDSEALGIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  93 VIYQDLSLFPNLTVAENIaFELNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARL 172
Cdd:NF040905  82 IIHQELALIPYLSIAENI-FLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 173 VIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWP--AEGLTTRKITELMTGL 250
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDcrADEVTEDRIIRGMVGR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 251 DIVHeRKPPNNAEDRRTVLEIKNLSRAGQY-------RDINLNLKRGEVLGLCGLLGSGRTELALSLFGIT--HPDSGEL 321
Cdd:NF040905 241 DLED-RYPERTPKIGEVVFEVKNWTVYHPLhperkvvDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTV 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 322 FIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLkTPWHLIDEKQCQDIVQEWIADLDIKVTDP 401
Cdd:NF040905 320 FKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKV-SRRGVIDENEEIKVAEEYRKKMNIKTPSV 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 402 NNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMK 481
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478

                 ....*...
gi 491046221 482 QGSIVKEI 489
Cdd:NF040905 479 EGRITGEL 486
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
13-501 4.21e-113

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: 343.73  E-value: 4.21e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDgskieIDGKSYHRLTPDKAR----- 87
Cdd:TIGR02633   1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGT-----WDGEIYWSGSPLKASnirdt 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   88 -ELGVQVIYQDLSLFPNLTVAENIAF--ELNLKGYFGWFRKKQLREKALeiLNELAFTIDPDT-PVQFLPIAQRQQVAIC 163
Cdd:TIGR02633  76 eRAGIVIIHQELTLVPELSVAENIFLgnEITLPGGRMAYNAMYLRAKNL--LRELQLDADNVTrPVGDYGGGQQQLVEIA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  164 RALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKI 243
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  244 TELMTGLDI--VHERKPPNNAEDrrtVLEIKNLS-------RAGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGiT 314
Cdd:TIGR02633 234 ITMMVGREItsLYPHEPHEIGDV---ILEARNLTcwdvinpHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-A 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  315 HPD--SGELFIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLKTPWHLIDEKQcQDIVQEWIA 392
Cdd:TIGR02633 310 YPGkfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAE-LQIIGSAIQ 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  393 DLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYY 472
Cdd:TIGR02633 389 RLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLG 468
                         490       500
                  ....*....|....*....|....*....
gi 491046221  473 NCDRILHMKQGSIVKEIVTDSINEQQLEE 501
Cdd:TIGR02633 469 LSDRVLVIGEGKLKGDFVNHALTQEQVLA 497
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
14-232 1.01e-74

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: 232.70  E-value: 1.01e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGVQV 93
Cdd:cd03216    1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE-ILVDGKEVSFASPRDARRAGIAM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQdlslfpnltvaeniafelnlkgyfgwfrkkqlrekaleilnelaftidpdtpvqfLPIAQRQQVAICRALVADARLV 173
Cdd:cd03216   80 VYQ-------------------------------------------------------LSVGERQMVEIARALARNARLL 104
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 174 IMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGT 232
Cdd:cd03216  105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
29-180 2.61e-37

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: 134.31  E-value: 2.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARElGVQVIYQDLSLFPNLTVAE 108
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGT-ILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVRE 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221  109 NIAFELNLKGYFgwfrKKQLREKALEILNELAFTIDPDTPVQFLPIA----QRQQVAICRALVADARLVIMDEPTA 180
Cdd:pfam00005  79 NLRLGLLLKGLS----KREKDARAEEALEKLGLGDLADRPVGERPGTlsggQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
22-222 5.63e-22

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 93.45  E-value: 5.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  22 SFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKieidgksyhrltpdkARELGVQVIY--QDLS 99
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYvpQRSE 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 100 L---FPnLTVAEniAFELNLKGYFGWFRK-----KQLREKALEI--LNELAftidpDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:NF040873  66 VpdsLP-LTVRD--LVAMGRWARRGLWRRltrddRAAVDDALERvgLADLA-----GRQLGELSGGQRQRALLAQGLAQE 137
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRIT 222
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
14-483 2.52e-11

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 66.30  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDG----KSYHRltpdkaREL 89
Cdd:NF033858   2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGR-VEVLGgdmaDARHR------RAV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 GVQVIY--QDL--SLFPNLTVAENIAFELNLkgyFGwFRKKQLREKALEILNE---LAFtidPDTPVQFLPIAQRQQVAI 162
Cdd:NF033858  75 CPRIAYmpQGLgkNLYPTLSVFENLDFFGRL---FG-QDAAERRRRIDELLRAtglAPF---ADRPAGKLSGGMKQKLGL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 163 CRALVADARLVIMDEPTAS---LTRtevNQLLSTVNYLKDK--GITVVFVSHRLEEVkEISDRITVIRDGQKIGTWPAEG 237
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGvdpLSR---RQFWELIDRIRAErpGMSVLVATAYMEEA-ERFDWLVAMDAGRVLATGTPAE 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 238 LTTRkitelmTG---LD--IVH----ERK---------PPNNAEDRRTVLEIKNLS-RAGQY---RDINLNLKRGEVlgl 295
Cdd:NF033858 224 LLAR------TGadtLEaaFIAllpeEKRrghqpvvipPRPADDDDEPAIEARGLTmRFGDFtavDHVSFRIRRGEI--- 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 296 cgllgsgrtelalslFG---------------IT---HPDSGE--LFieGKPVKLKNNtdAIKRGIGYVSE--------- 346
Cdd:NF033858 295 ---------------FGflgsngcgksttmkmLTgllPASEGEawLF--GQPVDAGDI--ATRRRVGYMSQafslygelt 355
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 347 --DRLTLGAilqqsiadnmvisildRLktpWHLiDEKQCQDIVQEWIADLDIK-VTDpnnAL-STLSGGNQQKVVLAKWI 422
Cdd:NF033858 356 vrQNLELHA----------------RL---FHL-PAAEIAARVAEMLERFDLAdVAD---ALpDSLPLGIRQRLSLAVAV 412
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 423 LTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS---GVGISIllitdeaSEAYYN----CDRILHMKQG 483
Cdd:NF033858 413 IHKPELLILDEPTSGVDPVARDMFWRLLIELSredGVTIFI-------STHFMNeaerCDRISLMHAG 473
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
7-179 2.10e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 47.43  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   7 ADKSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS-KI---EIDgksyhrlt 82
Cdd:NF033858 260 DDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEaWLfgqPVD-------- 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  83 pdkARELGV--QVIY--QDLSLFPNLTVAENIafELNLKGYfgwfrkkQL-REKALEILNELA--FTIDP--DTPVQFLP 153
Cdd:NF033858 332 ---AGDIATrrRVGYmsQAFSLYGELTVRQNL--ELHARLF-------HLpAAEIAARVAEMLerFDLADvaDALPDSLP 399
                        170       180
                 ....*....|....*....|....*...
gi 491046221 154 --IAQRQQVAIcrALVADARLVIMDEPT 179
Cdd:NF033858 400 lgIRQRLSLAV--AVIHKPELLILDEPT 425
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
1-241 5.25e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 45.50  E-value: 5.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   1 MTSTSKADKSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCG--KSTLIKTISGvyaPDDGSKieidgkSY 78
Cdd:NF000106   1 MTRKTISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRR------PW 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  79 HRLTPDKARelgvQVIYQDLSLFPNLTVAENIAFE----LNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPI 154
Cdd:NF000106  72 RF*TWCANR----RALRRTIG*HRPVR*GRRESFSgrenLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 155 AQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWP 234
Cdd:NF000106 148 GMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227

                 ....*..
gi 491046221 235 AEGLTTR 241
Cdd:NF000106 228 VDELKTK 234
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
404-497 7.94e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 44.73  E-value: 7.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 404 ALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:NF000106 141 AAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRG 220
                         90
                 ....*....|....
gi 491046221 484 SIVKEIVTDSINEQ 497
Cdd:NF000106 221 RVIADGKVDELKTK 234
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
38-227 6.40e-04

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: 40.43  E-value: 6.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221    38 KGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEIDGKSYHRLTPDKARELGVQVIYQDLSlfpnltvaeniafelnlk 117
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS------------------ 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   118 gyfgwfrkkqlREKALEILNELAFTIDPDtpvqflpiaqrqqvaicralvadarLVIMDEPTASLTRTEVNQLLSTV--- 194
Cdd:smart00382  63 -----------GELRLRLALALARKLKPD-------------------------VLILDEITSLLDAEQEALLLLLEelr 106
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 491046221   195 ---NYLKDKGITVVFVSHRLEEVKE-----ISDRITVIRDG 227
Cdd:smart00382 107 lllLLKSEKNLTVILTTNDEKDLGPallrrRFDRRIVLLLI 147
GguA NF040905
sugar ABC transporter ATP-binding protein;
29-247 4.06e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 39.77  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISG-VYAPDDGSKIEIDGKSYHRLTPDKARELGVQVIYQD---LSLfpNL 104
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrSYGRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDrkgYGL--NL 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 105 --TVAENIAFElNLKGY--FGW------------FRKKqLREKALEIlnelaftidpDTPVQFLPIAQRQQVAICRALVA 168
Cdd:NF040905 354 idDIKRNITLA-NLGKVsrRGVideneeikvaeeYRKK-MNIKTPSV----------FQKVGNLSGGNQQKVVLSKWLFT 421
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 169 DARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELM 247
Cdd:NF040905 422 DPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQERIMRLI 500
 
Name Accession Description Interval E-value
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
10-505 0e+00

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 649.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:COG1129    1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGE-ILLDGEPVRFRSPRDAQAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 GVQVIYQDLSLFPNLTVAENIAFElNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:COG1129   80 GIAIIHQELNLVPNLSVAENIFLG-REPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMTG 249
Cdd:COG1129  159 ARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 250 LDIvHERKPPNNAEDRRTVLEIKNLSRAGQYRDINLNLKRGEVlglcgllgsgRTELALSLFGITHPDSGELFIEGKPVK 329
Cdd:COG1129  239 REL-EDLFPKRAAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEIlgiaglvgagRTELARALFGADPADSGEIRLDGKPVR 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 330 LKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLkTPWHLIDEKQCQDIVQEWIADLDIKVTDPNNALSTLS 409
Cdd:COG1129  318 IRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRL-SRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLS 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 410 GGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKEI 489
Cdd:COG1129  397 GGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGEL 476
                        490
                 ....*....|....*.
gi 491046221 490 VTDSINEQQLEEIING 505
Cdd:COG1129  477 DREEATEEAIMAAATG 492
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
10-499 2.13e-148

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 434.07  E-value: 2.13e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:COG3845    2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGE-ILIDGKPVRIRSPRDAIAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 GVQVIYQDLSLFPNLTVAENIAfeLNLKGYFGWF-RKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVA 168
Cdd:COG3845   81 GIGMVHQHFMLVPNLTVAENIV--LGLEPTKGGRlDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 169 DARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMT 248
Cdd:COG3845  159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 249 GLDIV-HERKPPnnAEDRRTVLEIKNLSRAGQY-----RDINLNLKRGEVlglcgllgsgrTELALSLFGITHPDSGELF 322
Cdd:COG3845  239 GREVLlRVEKAP--AEPGEVVLEVENLSVRDDRgvpalKDVSLEVRAGEIlgiagvagngqSELAEALAGLRPPASGSIR 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 323 IEGKPVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLK-TPWHLIDEKQCQDIVQEWIADLDIKVTDP 401
Cdd:COG3845  317 LDGEDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRPPfSRGGFLDRKAIRAFAEELIEEFDVRTPGP 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 402 NNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMK 481
Cdd:COG3845  397 DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMY 476
                        490
                 ....*....|....*...
gi 491046221 482 QGSIVKEIVTDSINEQQL 499
Cdd:COG3845  477 EGRIVGEVPAAEATREEI 494
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
10-498 2.89e-141

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 415.87  E-value: 2.89e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS-KIEIDGKSYHRLTPDKARE 88
Cdd:PRK13549   2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEgEIIFEGEELQASNIRDTER 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  89 LGVQVIYQDLSLFPNLTVAENIaFELNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVA 168
Cdd:PRK13549  82 AGIAIIHQELALVKELSVLENI-FLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 169 DARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMT 248
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 249 GLDIVhERKPPNNAEDRRTVLEIKNLS-------RAGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDS-GE 320
Cdd:PRK13549 241 GRELT-ALYPREPHTIGEVILEVRNLTawdpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 321 LFIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLkTPWHLIDEKQCQDIVQEWIADLDIKVTD 400
Cdd:PRK13549 320 IFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRF-TGGSRIDDAAELKTILESIQRLKVKTAS 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 401 PNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHM 480
Cdd:PRK13549 399 PELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVM 478
                        490
                 ....*....|....*...
gi 491046221 481 KQGSIVKEIVTDSINEQQ 498
Cdd:PRK13549 479 HEGKLKGDLINHNLTQEQ 496
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
10-499 2.74e-135

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 400.44  E-value: 2.74e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:PRK11288   1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGS-ILIDGQEMRFASTTAALAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 GVQVIYQDLSLFPNLTVAENIaFELNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:PRK11288  80 GVAIIYQELHLVPEMTVAENL-YLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPA-EGLTTRKITELMT 248
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDmAQVDRDQLVQAMV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 249 GLDI--VHERKPPNNAEDRrtvLEIKNLSRAGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGK 326
Cdd:PRK11288 239 GREIgdIYGYRPRPLGEVR---LRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 327 PVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISIlDRLKTPW-HLIDEKQCQDIVQEWIADLDIKVTDPNNAL 405
Cdd:PRK11288 316 PIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISA-RRHHLRAgCLINNRWEAENADRFIRSLNIKTPSREQLI 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 406 STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSI 485
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
                        490
                 ....*....|....
gi 491046221 486 VKEIVTDSINEQQL 499
Cdd:PRK11288 475 AGELAREQATERQA 488
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
12-503 5.12e-127

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 379.90  E-value: 5.12e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGV 91
Cdd:PRK09700   4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGT-ITINNINYNKLDHKLAAQLGI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIYQDLSLFPNLTVAENIAF-ELNLKGYFG-----WfrkKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRA 165
Cdd:PRK09700  83 GIIYQELSVIDELTVLENLYIgRHLTKKVCGvniidW---REMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 166 LVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITE 245
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 246 LMTGLDIVHE---RKPPNNAEDRRTVLEIKNLSR--AGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGE 320
Cdd:PRK09700 240 LMVGRELQNRfnaMKENVSNLAHETVFEVRNVTSrdRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 321 LFIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVIS---ILDRLKTPWHLIDEKQCQDIVQEWIADLDIK 397
Cdd:PRK09700 320 IRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrslKDGGYKGAMGLFHEVDEQRTAENQRELLALK 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 398 VTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRI 477
Cdd:PRK09700 400 CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRI 479
                        490       500
                 ....*....|....*....|....*..
gi 491046221 478 LHMKQGSIVKEIV-TDSINEqqlEEII 503
Cdd:PRK09700 480 AVFCEGRLTQILTnRDDMSE---EEIM 503
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
12-495 1.81e-120

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 362.83  E-value: 1.81e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGV 91
Cdd:PRK15439  10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGT-LEIGGNPCARLTPAKAHQLGI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIYQDLSLFPNLTVAENIAFELNlkgyfgwfrKKQLREKALE-ILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADA 170
Cdd:PRK15439  89 YLVPQEPLLFPNLSVKENILFGLP---------KRQASMQKMKqLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 171 RLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMT-- 248
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITpa 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 249 --GLDIVHERK----PPNNaedRRT------VLEIKNLSRAGqYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHP 316
Cdd:PRK15439 240 arEKSLSASQKlwleLPGN---RRQqaagapVLTVEDLTGEG-FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPA 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 317 DSGELFIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNmVISILDRLKTPWhlIDEKQCQDIVQEWIADLDI 396
Cdd:PRK15439 316 RGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWN-VCALTHNRRGFW--IKPARENAVLERYRRALNI 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 397 KVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDR 476
Cdd:PRK15439 393 KFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADR 472
                        490
                 ....*....|....*....
gi 491046221 477 ILHMKQGSIVKEIVTDSIN 495
Cdd:PRK15439 473 VLVMHQGEISGALTGAAIN 491
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
12-499 1.17e-116

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 352.77  E-value: 1.17e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGV 91
Cdd:PRK10762   3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGS-ILYLGKEVTFNGPKSSQEAGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIYQDLSLFPNLTVAENIAFELNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADAR 171
Cdd:PRK10762  82 GIIHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMTG-- 249
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGrk 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 250 LDivhERKPPNNAEDRRTVLEIKNLSRAGqYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVK 329
Cdd:PRK10762 242 LE---DQYPRLDKAPGEVRLKVDNLSGPG-VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 330 LKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLKTPWHLIDEKQCQDIVQEWIADLDIKVTDPNNALSTLS 409
Cdd:PRK10762 318 TRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLS 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 410 GGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKEI 489
Cdd:PRK10762 398 GGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEF 477
                        490
                 ....*....|
gi 491046221 490 VTDSINEQQL 499
Cdd:PRK10762 478 TREQATQEKL 487
GguA NF040905
sugar ABC transporter ATP-binding protein;
16-489 5.47e-116

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 351.01  E-value: 5.47e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  16 LRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYApdDGS---KIEIDGKSYHRLTPDKARELGVQ 92
Cdd:NF040905   4 MRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP--HGSyegEILFDGEVCRFKDIRDSEALGIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  93 VIYQDLSLFPNLTVAENIaFELNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARL 172
Cdd:NF040905  82 IIHQELALIPYLSIAENI-FLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 173 VIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWP--AEGLTTRKITELMTGL 250
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDcrADEVTEDRIIRGMVGR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 251 DIVHeRKPPNNAEDRRTVLEIKNLSRAGQY-------RDINLNLKRGEVLGLCGLLGSGRTELALSLFGIT--HPDSGEL 321
Cdd:NF040905 241 DLED-RYPERTPKIGEVVFEVKNWTVYHPLhperkvvDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTV 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 322 FIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLkTPWHLIDEKQCQDIVQEWIADLDIKVTDP 401
Cdd:NF040905 320 FKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKV-SRRGVIDENEEIKVAEEYRKKMNIKTPSV 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 402 NNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMK 481
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478

                 ....*...
gi 491046221 482 QGSIVKEI 489
Cdd:NF040905 479 EGRITGEL 486
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
13-501 4.21e-113

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: 343.73  E-value: 4.21e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDgskieIDGKSYHRLTPDKAR----- 87
Cdd:TIGR02633   1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGT-----WDGEIYWSGSPLKASnirdt 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   88 -ELGVQVIYQDLSLFPNLTVAENIAF--ELNLKGYFGWFRKKQLREKALeiLNELAFTIDPDT-PVQFLPIAQRQQVAIC 163
Cdd:TIGR02633  76 eRAGIVIIHQELTLVPELSVAENIFLgnEITLPGGRMAYNAMYLRAKNL--LRELQLDADNVTrPVGDYGGGQQQLVEIA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  164 RALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKI 243
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  244 TELMTGLDI--VHERKPPNNAEDrrtVLEIKNLS-------RAGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGiT 314
Cdd:TIGR02633 234 ITMMVGREItsLYPHEPHEIGDV---ILEARNLTcwdvinpHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-A 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  315 HPD--SGELFIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLKTPWHLIDEKQcQDIVQEWIA 392
Cdd:TIGR02633 310 YPGkfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAE-LQIIGSAIQ 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  393 DLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYY 472
Cdd:TIGR02633 389 RLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLG 468
                         490       500
                  ....*....|....*....|....*....
gi 491046221  473 NCDRILHMKQGSIVKEIVTDSINEQQLEE 501
Cdd:TIGR02633 469 LSDRVLVIGEGKLKGDFVNHALTQEQVLA 497
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
16-503 1.64e-109

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 334.01  E-value: 1.64e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  16 LRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGVQVIY 95
Cdd:PRK10982   1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGS-ILFQGKEIDFKSSKEALENGISMVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  96 QDLSLFPNLTVAENIAF-ELNLKGYFgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVI 174
Cdd:PRK10982  80 QELNLVLQRSVMDNMWLgRYPTKGMF--VDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 175 MDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMTGLDIVH 254
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQ 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 255 eRKPPNNAEDRRTVLEIKNLSRAGQ--YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKN 332
Cdd:PRK10982 238 -RFPDKENKPGEVILEVRNLTSLRQpsIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHN 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 333 NTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLKTPWHLIDEKQCQDIVQeWIAD-LDIKVTDPNNALSTLSGG 411
Cdd:PRK10982 317 ANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQ-WVIDsMRVKTPGHRTQIGSLSGG 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 412 NQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSiVKEIVT 491
Cdd:PRK10982 396 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGL-VAGIVD 474
                        490
                 ....*....|..
gi 491046221 492 DSINEQqlEEII 503
Cdd:PRK10982 475 TKTTTQ--NEIL 484
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
14-232 1.01e-74

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: 232.70  E-value: 1.01e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGVQV 93
Cdd:cd03216    1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE-ILVDGKEVSFASPRDARRAGIAM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQdlslfpnltvaeniafelnlkgyfgwfrkkqlrekaleilnelaftidpdtpvqfLPIAQRQQVAICRALVADARLV 173
Cdd:cd03216   80 VYQ-------------------------------------------------------LSVGERQMVEIARALARNARLL 104
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 174 IMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGT 232
Cdd:cd03216  105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
266-485 3.88e-68

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: 216.53  E-value: 3.88e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 266 RTVLEIKNLSRAGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKRGIGYVS 345
Cdd:cd03215    2 EPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 346 EDRLTLGAILQQSIADNMVISILdrlktpwhlidekqcqdivqewiadldikvtdpnnalstLSGGNQQKVVLAKWILTR 425
Cdd:cd03215   82 EDRKREGLVLDLSVAENIALSSL---------------------------------------LSGGNQQKVVLARWLARD 122
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 426 PKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSI 485
Cdd:cd03215  123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
11-486 1.58e-63

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: 215.15  E-value: 1.58e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  11 DPLITLRDLSKSF--GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGvYAPDDGS---KIEIDGKSYHRLTPdK 85
Cdd:COG1123    2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRisgEVLLDGRDLLELSE-A 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  86 ARELGVQVIYQD--LSLFPnLTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAIC 163
Cdd:COG1123   80 LRGRRIGMVFQDpmTQLNP-VTVGDQIAEALENLG----LSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 164 RALVADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRK 242
Cdd:COG1123  155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 243 ITELMTGLDIVHERKPPNNAEDRRTVLEIKNLS-----RAGQY----RDINLNLKRGEVlglcgllgsgrteLAL----- 308
Cdd:COG1123  235 QALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSkrypvRGKGGvravDDVSLTLRRGET-------------LGLvgesg 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 309 --------SLFGITHPDSGELFIEGKPV--KLKNNTDAIKRGIGYVSED-------RLTLGAIlqqsIADNMVISildrl 371
Cdd:COG1123  302 sgkstlarLLLGLLRPTSGSILFDGKDLtkLSRRSLRELRRRVQMVFQDpysslnpRMTVGDI----IAEPLRLH----- 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 372 ktpwHLIDEKQCQDIVQEWIAD--LDIKVTD--PnnalSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIY 447
Cdd:COG1123  373 ----GLLSRAERRERVAELLERvgLPPDLADryP----HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQIL 444
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 491046221 448 KLIHRLSG-VGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:COG1123  445 NLLRDLQReLGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
16-237 2.45e-61

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: 200.74  E-value: 2.45e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  16 LRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGVQVIY 95
Cdd:cd03219    3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGS-VLFDGEDITGLPPHEIARLGIGRTF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  96 QDLSLFPNLTVAEN--IAFELNLKGYFGWFR----KKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:cd03219   82 QIPRLFPELTVLENvmVAAQARTGSGLLLARarreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIgtwpAEG 237
Cdd:cd03219  162 PKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI----AEG 225
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
10-236 4.98e-61

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: 200.65  E-value: 4.98e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:COG0411    1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGR-ILFDGRDITGLPPHRIARL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 GVQVIYQDLSLFPNLTVAENIA----------FELNLKGYFGWFRK-KQLREKALEILNELAFTIDPDTPVQFLPIAQRQ 158
Cdd:COG0411   80 GIARTFQNPRLFPELTVLENVLvaaharlgrgLLAALLRLPRARREeREARERAEELLERVGLADRADEPAGNLSYGQQR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 159 QVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDGQKI--GTwPA 235
Cdd:COG0411  160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIaeGT-PA 238

                 .
gi 491046221 236 E 236
Cdd:COG0411  239 E 239
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
14-241 1.77e-58

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 193.36  E-value: 1.77e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGvqV 93
Cdd:COG1131    1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGE-VRVLGEDVARDPAEVRRRIG--Y 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENIAFelnLKGYFGwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLV 173
Cdd:COG1131   78 VPQEPALYPDLTVRENLRF---FARLYG-LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 174 IMDEPTASL---TRTEVNQLLSTvnyLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTR 241
Cdd:COG1131  154 ILDEPTSGLdpeARRELWELLRE---LAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
10-236 3.16e-55

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 188.77  E-value: 3.16e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKaREL 89
Cdd:COG3842    2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGR-ILLDGRDVTGLPPEK-RNV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 GvqVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILN-----ELAftidpDTPVQFLPIAQRQQVAICR 164
Cdd:COG3842   80 G--MVFQDYALFPHLTVAENVAFGLRMRG----VPKAEIRARVAELLElvgleGLA-----DRYPHQLSGGQQQRVALAR 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 165 ALVADARLVIMDEPTASL---TRTEVNQLLstVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDG--QKIGTwPAE 236
Cdd:COG3842  149 ALAPEPRVLLLDEPLSALdakLREEMREEL--RRLQRELGITFIYVTHDQEEALALADRIAVMNDGriEQVGT-PEE 222
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
3-228 2.66e-53

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 187.80  E-value: 2.66e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   3 STSKADKSDPLITLRDLSKSF-----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKS 77
Cdd:COG1123  250 AAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGS-ILFDGKD 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  78 YHRLTPDKARELG--VQVIYQD--LSLFPNLTVAENIAFELNLkgyFGWFRKKQLREKALEILNELAftIDPDT----PV 149
Cdd:COG1123  329 LTKLSRRSLRELRrrVQMVFQDpySSLNPRMTVGDIIAEPLRL---HGLLSRAERRERVAELLERVG--LPPDLadryPH 403
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 150 QFlpiaQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRD 226
Cdd:COG1123  404 ELsg-gQRQRVAIARALALEPKLLILDEPTSALdvsVQAQILNLLRDLQ--RELGLTYLFISHDLAVVRYIADRVAVMYD 480

                 ..
gi 491046221 227 GQ 228
Cdd:COG1123  481 GR 482
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
14-228 7.42e-53

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: 177.71  E-value: 7.42e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKaRELGvqV 93
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGE-ILIDGRDVTGVPPER-RNIG--M 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLV 173
Cdd:cd03259   77 VFQDYALFPHLTVAENIAFGLKLRG----VPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 174 IMDEPTASL---TRTEVNQLLSTVnyLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03259  153 LLDEPLSALdakLREELREELKEL--QRELGITTIYVTHDQEEALALADRIAVMNEGR 208
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
14-228 1.07e-49

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: 167.96  E-value: 1.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGvqV 93
Cdd:cd03230    1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGE-IKVLGKDIKKEPEEVKRRIG--Y 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENIAFElnlKGyfgwfrkkqlrekaleilnelaftidpdtpvqflpiaQRQQVAICRALVADARLV 173
Cdd:cd03230   78 LPEEPSLYENLTVRENLKLS---GG-------------------------------------MKQRLALAQALLHDPELL 117
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 174 IMDEPTASL---TRTEVNQLLSTvnyLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03230  118 ILDEPTSGLdpeSRREFWELLRE---LKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
10-236 1.06e-48

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: 167.85  E-value: 1.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:COG1127    2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGE-ILVDGQDITGLSEKELYEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 ----GvqVIYQDLSLFPNLTVAENIAFELNlkgYFGWFRKKQLREKALEILN--ELAFTIDpdtpvqFLPiAQ-----RQ 158
Cdd:COG1127   81 rrriG--MLFQGGALFDSLTVFENVAFPLR---EHTDLSEAEIRELVLEKLElvGLPGAAD------KMP-SElsggmRK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 159 QVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI--GTw 233
Cdd:COG1127  149 RVALARALALDPEILLYDEPTAGLdpiTSAVIDELIRELR--DELGLTSVVVTHDLDSAFAIADRVAVLADGKIIaeGT- 225

                 ...
gi 491046221 234 PAE 236
Cdd:COG1127  226 PEE 228
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
10-223 8.70e-48

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 166.03  E-value: 8.70e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSF----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDK 85
Cdd:COG1116    4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGE-VLVDGKPVTGPGPDR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  86 ArelgvqVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNE--LAFTID--PDTpvqfLPIAQRQQVA 161
Cdd:COG1116   83 G------VVFQEPALLPWLTVLDNVALGLELRG----VPKAERRERARELLELvgLAGFEDayPHQ----LSGGMRQRVA 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 162 ICRALVADARLVIMDEPTASL---TRTEVNQLLstVNYLKDKGITVVFVSHRLEEVKEISDRITV 223
Cdd:COG1116  149 IARALANDPEVLLMDEPFGALdalTRERLQDEL--LRLWQETGKTVLFVTHDVDEAVFLADRVVV 211
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
11-228 1.11e-47

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 164.45  E-value: 1.11e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  11 DPLITLRDLSKSFG----GHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDK- 85
Cdd:COG1136    2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE-VLIDGQDISSLSEREl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  86 ----ARELGvqVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNEL-------AFtidpdtPVQfLPI 154
Cdd:COG1136   81 arlrRRHIG--FVFQFFNLLPELTALENVALPLLLAG----VSRKERRERARELLERVglgdrldHR------PSQ-LSG 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 155 AQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRlEEVKEISDRITVIRDGQ 228
Cdd:COG1136  148 GQQQRVAIARALVNRPKLILADEPTGNLdskTGEEVLELLRELN--RELGTTIVMVTHD-PELAARADRVIRLRDGR 221
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
14-236 2.44e-46

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 164.86  E-value: 2.44e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPdKARelGVQV 93
Cdd:COG3839    4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSG-EILIGGRDVTDLPP-KDR--NIAM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREK---ALEILNelaftIDPdtpvqFL---PIA----QRQQVAIC 163
Cdd:COG3839   80 VFQSYALYPHMTVYENIAFPLKLRK----VPKAEIDRRvreAAELLG-----LED-----LLdrkPKQlsggQRQRVALG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 164 RALVADARLVIMDEPTASL-------TRTEVNQLlstvnyLKDKGITVVFVSHRLEEVKEISDRITVIRDG--QKIGTwP 234
Cdd:COG3839  146 RALVREPKVFLLDEPLSNLdaklrveMRAEIKRL------HRRLGTTTIYVTHDQVEAMTLADRIAVMNDGriQQVGT-P 218

                 ..
gi 491046221 235 AE 236
Cdd:COG3839  219 EE 220
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
14-228 1.86e-45

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: 158.42  E-value: 1.86e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGG----HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDK---- 85
Cdd:cd03255    1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE-VRVDGTDISKLSEKElaaf 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  86 -ARELGvqVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICR 164
Cdd:cd03255   80 rRRHIG--FVFQSFNLLPDLTALENVELPLLLAG----VPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIAR 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 165 ALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRlEEVKEISDRITVIRDGQ 228
Cdd:cd03255  154 ALANDPKIILADEPTGNLdseTGKEVMELLRELN--KEAGTTIVVVTHD-PELAEYADRIIELRDGK 217
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
14-240 2.60e-44

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: 156.12  E-value: 2.60e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGVQ- 92
Cdd:cd03261    1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGE-VLIDGEDISGLSEAELYRLRRRm 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  93 -VIYQDLSLFPNLTVAENIAFELNlkgYFGWFRKKQLREKALEILNELAFTIDPDT-PVQfLPIAQRQQVAICRALVADA 170
Cdd:cd03261   80 gMLFQSGALFDSLTVFENVAFPLR---EHTRLSEEEIREIVLEKLEAVGLRGAEDLyPAE-LSGGMKKRVALARALALDP 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 171 RLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTT 240
Cdd:cd03261  156 ELLLYDEPTAGLdpiASGVIDDLIRSLK--KELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
14-234 3.43e-44

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: 154.94  E-value: 3.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGG----HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKArel 89
Cdd:cd03293    1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGE-VLVDGEPVTGPGPDRG--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 gvqVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNE--LAFTIDpDTPVQfLPIAQRQQVAICRALV 167
Cdd:cd03293   77 ---YVFQQDALLPWLTVLDNVALGLELQG----VPKAEARERAEELLELvgLSGFEN-AYPHQ-LSGGMRQRVALARALA 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 168 ADARLVIMDEPTASL---TRTEVNQLLSTVnyLKDKGITVVFVSHRLEEVKEISDRITVI--RDGQKIGTWP 234
Cdd:cd03293  148 VDPDVLLLDEPFSALdalTREQLQEELLDI--WRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVE 217
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
14-230 3.65e-44

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: 155.18  E-value: 3.65e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELgVQ 92
Cdd:COG1122    1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSG-EVLVDGKDITKKNLRELRRK-VG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  93 VIYQ--DLSLFpNLTVAENIAFEL-NLKgyfgwFRKKQLREKALEILN-----ELAftidpDTPVQFLPIAQRQQVAICR 164
Cdd:COG1122   79 LVFQnpDDQLF-APTVEEDVAFGPeNLG-----LPREEIRERVEEALElvgleHLA-----DRPPHELSGGQKQRVAIAG 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 165 ALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:COG1122  148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
9-246 4.12e-44

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 155.63  E-value: 4.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   9 KSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRltpdKARE 88
Cdd:COG1121    2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGT-VRLFGKPPRR----ARRR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  89 LGvqviY--QDLSL---FPnLTVAENIAfeLNLKGYFGWFR--KKQLREKALEILNElaftidpdtpVQFLPIA------ 155
Cdd:COG1121   77 IG----YvpQRAEVdwdFP-ITVRDVVL--MGRYGRRGLFRrpSRADREAVDEALER----------VGLEDLAdrpige 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 156 ----QRQQVAICRALVADARLVIMDEPTASL-TRTEvNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ-K 229
Cdd:COG1121  140 lsggQQQRVLLARALAQDPDLLLLDEPFAGVdAATE-EALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLvA 218
                        250
                 ....*....|....*..
gi 491046221 230 IGTwPAEGLTTRKITEL 246
Cdd:COG1121  219 HGP-PEEVLTPENLSRA 234
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
16-228 5.43e-44

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: 154.16  E-value: 5.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  16 LRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELgVQV 93
Cdd:cd03225    2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSG-EVLVDGKDLTKLSLKELRRK-VGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQ--DLSLFpNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADAR 171
Cdd:cd03225   80 VFQnpDDQFF-GPTVEEEVAFGLENLGL----PEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03225  155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
14-228 4.43e-43

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: 150.80  E-value: 4.43e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGK---SYHRLTPDKARELG 90
Cdd:cd03229    1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGS-ILIDGEdltDLEDELPPLRRRIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  91 vqVIYQDLSLFPNLTVAENIAFELNlkGyfgwfrkkqlrekaleilnelaftidpdtpvqflpiAQRQQVAICRALVADA 170
Cdd:cd03229   80 --MVFQDFALFPHLTVLENIALGLS--G------------------------------------GQQQRVALARALAMDP 119
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 171 RLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03229  120 DVLLLDEPTSALdpiTRREVRALLKSLQ--AQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
14-236 5.50e-43

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: 152.39  E-value: 5.50e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKArelGVQV 93
Cdd:cd03300    1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSG-EILLDGKDITNLPPHKR---PVNT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLV 173
Cdd:cd03300   77 VFQNYALFPHLTVFENIAFGLRLKK----LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 174 IMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDG--QKIGTwPAE 236
Cdd:cd03300  153 LLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGkiQQIGT-PEE 217
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
13-228 3.50e-42

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: 150.04  E-value: 3.50e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFGGHR----ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARE 88
Cdd:cd03258    1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGS-VLVDGTDLTLLSGKELRK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  89 LGVQV--IYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPDT-PVQfLPIAQRQQVAICRA 165
Cdd:cd03258   80 ARRRIgmIFQHFNLLSSRTVFENVALPLEIAGV----PKAEIEERVLELLELVGLEDKADAyPAQ-LSGGQKQRVGIARA 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 166 LVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03258  155 LANNPKVLLCDEATSALdpeTTQSILALLRDIN--RELGLTIVLITHEMEVVKRICDRVAVMEKGE 218
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
13-246 1.24e-41

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: 149.42  E-value: 1.24e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTP-DKARELGv 91
Cdd:COG1120    1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGE-VLLDGRDLASLSRrELARRIA- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 qVIYQDLSLFPNLTVAENIAfeLNLKGYFGWFRK-----KQLREKALEILN--ELAftidpDTPVQFLPIAQRQQVAICR 164
Cdd:COG1120   79 -YVPQEPPAPFGLTVRELVA--LGRYPHLGLFGRpsaedREAVEEALERTGleHLA-----DRPVDELSGGERQRVLIAR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 165 ALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI--GTwPAEGLT 239
Cdd:COG1120  151 ALAQEPPLLLLDEPTSHLdlaHQLEVLELLRRLA--RERGRTVVMVLHDLNLAARYADRLVLLKDGRIVaqGP-PEEVLT 227

                 ....*..
gi 491046221 240 TRKITEL 246
Cdd:COG1120  228 PELLEEV 234
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
13-228 2.02e-41

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: 148.04  E-value: 2.02e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSF----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARE 88
Cdd:cd03257    1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSG-SIIFDGKDLLKLSRRLRKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  89 LG--VQVIYQD--LSLFPNLTVAENIAfELnLKGYFGWFRKKQLREKALEILNELaftIDPDTPVQFLPIA----QRQQV 160
Cdd:cd03257   80 RRkeIQMVFQDpmSSLNPRMTIGEQIA-EP-LRIHGKLSKKEARKEAVLLLLVGV---GLPEEVLNRYPHElsggQRQRV 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 161 AICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03257  155 AIARALALNPKLLIADEPTSALdvsVQAQILDLLKKLQ--EELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
14-236 9.20e-41

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 149.91  E-value: 9.20e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPdkARELGVQV 93
Cdd:COG1118    3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSG-RIVLNGRDLFTNLP--PRERRVGF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENIAFELNLKGYFgwfrKKQLREKALEILNElaftidpdtpVQFLPIA----------QRQQVAIC 163
Cdd:COG1118   80 VFQHYALFPHMTVAENIAFGLRVRPPS----KAEIRARVEELLEL----------VQLEGLAdrypsqlsggQRQRVALA 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 164 RALVADARLVIMDEPTASL---TRTEVNQLLStvNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ--KIGTwPAE 236
Cdd:COG1118  146 RALAVEPEVLLLDEPFGALdakVRKELRRWLR--RLHDELGGTTVFVTHDQEEALELADRVVVMNQGRieQVGT-PDE 220
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
14-228 1.76e-40

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: 145.27  E-value: 1.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGVQV 93
Cdd:cd03224    1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGS-IRFDGRDITGLPPHERARAGIGY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENiafeLNLKGYFGWFRK-KQLREKALE---ILNELAftidpDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:cd03224   80 VPEGRRIFPELTVEEN----LLLGAYARRRAKrKARLERVYElfpRLKERR-----KQLAGTLSGGEQQMLAIARALMSR 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03224  151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
14-228 2.15e-39

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: 142.01  E-value: 2.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKsyhRLTPDKARELGVQV 93
Cdd:cd03301    1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSG-RIYIGGR---DVTDLPPKDRDIAM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEIlnelAFTIDPDTPVQFLPIA----QRQQVAICRALVAD 169
Cdd:cd03301   77 VFQNYALYPHMTVYDNIAFGLKLRK----VPKDEIDERVREV----AELLQIEHLLDRKPKQlsggQRQRVALGRAIVRE 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 170 ARLVIMDEPTASL-------TRTEVNQLlstvnyLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03301  149 PKVFLMDEPLSNLdaklrvqMRAELKRL------QQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
11-238 4.18e-39

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: 142.04  E-value: 4.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  11 DPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELG 90
Cdd:COG0410    1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGS-IRFDGEDITGLPPHRIARLG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  91 VQVIYQDLSLFPNLTVAENiafeLNLKGYFGwfRKKQLREKALE-------ILNELAftidpDTPVQFLPIAQRQQVAIC 163
Cdd:COG0410   80 IGYVPEGRRIFPSLTVEEN----LLLGAYAR--RDRAEVRADLErvyelfpRLKERR-----RQRAGTLSGGEQQMLAIG 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 164 RALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGL 238
Cdd:COG0410  149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
13-228 6.28e-39

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: 141.86  E-value: 6.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFG----GHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRlTPDKARE 88
Cdd:COG1124    1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGE-VTFDGRPVTR-RRRKAFR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  89 LGVQVIYQD--LSLFPNLTVAENIAFELNLKGyfgwfrKKQLREKALEILNELAftIDPD----TPVQfLPIAQRQQVAI 162
Cdd:COG1124   79 RRVQMVFQDpyASLHPRHTVDRILAEPLRIHG------LPDREERIAELLEQVG--LPPSfldrYPHQ-LSGGQRQRVAI 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 163 CRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:COG1124  150 ARALILEPELLLLDEPTSALdvsVQAEILNLLKDLR--EERGLTYLFVSHDLAVVAHLCDRVAVMQNGR 216
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
14-246 1.18e-38

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: 141.17  E-value: 1.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFG-GHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGVQ 92
Cdd:cd03256    1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGS-VLIDGTDINKLKGKALRQLRRQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  93 V--IYQDLSLFPNLTVAENI-----AFELNLKGYFGWFrKKQLREKALEILN-----ELAFtidpdTPVQFLPIAQRQQV 160
Cdd:cd03256   80 IgmIFQQFNLIERLSVLENVlsgrlGRRSTWRSLFGLF-PKEEKQRALAALErvgllDKAY-----QRADQLSGGQQQRV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 161 AICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEG 237
Cdd:cd03256  154 AIARALMQQPKLILADEPVASLdpaSSRQVMDLLKRIN--REEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE 231

                 ....*....
gi 491046221 238 LTTRKITEL 246
Cdd:cd03256  232 LTDEVLDEI 240
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
12-214 1.29e-38

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: 139.92  E-value: 1.29e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGv 91
Cdd:COG4133    1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGE-VLWNGEPIRDAREDYRRRLA- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 qVIYQDLSLFPNLTVAENIAFELNLKGYFGwfRKKQLREkALEILN--ELAftidpDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:COG4133   79 -YLGHADGLKPELTVRENLRFWAALYGLRA--DREAIDE-ALEAVGlaGLA-----DLPVRQLSAGQKRRVALARLLLSP 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEV 214
Cdd:COG4133  150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLEL 194
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
14-228 1.36e-38

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: 139.97  E-value: 1.36e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKsyhRLTPDKA--RELGV 91
Cdd:cd03262    1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSG-TIIIDGL---KLTDDKKniNELRQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QV--IYQDLSLFPNLTVAENIAFEL-NLKGyfgwFRKKQLREKALEILNE--LAFTIDpDTPVQfLPIAQRQQVAICRAL 166
Cdd:cd03262   77 KVgmVFQQFNLFPHLTVLENITLAPiKVKG----MSKAEAEERALELLEKvgLADKAD-AYPAQ-LSGGQQQRVAIARAL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 167 VADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03262  151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
11-232 2.66e-38

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 143.93  E-value: 2.66e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  11 DPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKaRElg 90
Cdd:PRK09452  12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGR-IMLDGQDITHVPAEN-RH-- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  91 VQVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEI-----LNELAftidPDTPVQfLPIAQRQQVAICRA 165
Cdd:PRK09452  88 VNTVFQSYALFPHMTVFENVAFGLRMQK----TPAAEITPRVMEAlrmvqLEEFA----QRKPHQ-LSGGQQQRVAIARA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 166 LVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDG--QKIGT 232
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGriEQDGT 228
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
14-236 3.75e-38

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: 139.78  E-value: 3.75e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKsyhRLTPDKARELGVQV 93
Cdd:cd03296    3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGT-ILFGGE---DATDVPVQERNVGF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENIAFELNLKGYFGWFRKKQLREKALEILNELAFTIDPDT-PVQfLPIAQRQQVAICRALVADARL 172
Cdd:cd03296   79 VFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRyPAQ-LSGGQRQRVALARALAVEPKV 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 173 VIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDGQ--KIGTwPAE 236
Cdd:cd03296  158 LLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRieQVGT-PDE 223
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
14-228 5.27e-38

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 138.65  E-value: 5.27e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKA----RE 88
Cdd:COG2884    2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSG-QVLVNGQDLSRLKRREIpylrRR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  89 LGvqVIYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNEL-------AFtidpdtPVQfLPIAQRQQVA 161
Cdd:COG2884   81 IG--VVFQDFRLLPDRTVYENVALPLRVTGK----SRKEIRRRVREVLDLVglsdkakAL------PHE-LSGGEQQRVA 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 162 ICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylkDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:COG2884  148 IARALVNRPELLLADEPTGNLdpeTSWEIMELLEEIN---RRGTTVLIATHDLELVDRMPKRVLELEDGR 214
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
14-240 7.33e-38

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


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 138.97  E-value: 7.33e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHR-ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELGVQ 92
Cdd:cd03295    1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSG-EIFIDGEDIREQDPVELRRKIGY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  93 VIyQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAftIDPDTPVQFLPI----AQRQQVAICRALVA 168
Cdd:cd03295   80 VI-QQIGLFPHMTVEENIALVPKLLKW----PKEKIRERADELLALVG--LDPAEFADRYPHelsgGQQQRVGVARALAA 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 169 DARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDG--QKIGTwPAEGLTT 240
Cdd:cd03295  153 DPPLLLMDEPFGALdpiTRDQLQEEFKRLQ--QELGKTIVFVTHDIDEAFRLADRIAIMKNGeiVQVGT-PDEILRS 226
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
29-180 2.61e-37

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: 134.31  E-value: 2.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARElGVQVIYQDLSLFPNLTVAE 108
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGT-ILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVRE 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221  109 NIAFELNLKGYFgwfrKKQLREKALEILNELAFTIDPDTPVQFLPIA----QRQQVAICRALVADARLVIMDEPTA 180
Cdd:pfam00005  79 NLRLGLLLKGLS----KREKDARAEEALEKLGLGDLADRPVGERPGTlsggQRQRVAIARALLTKPKLLLLDEPTA 150
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
13-228 2.10e-36

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 134.74  E-value: 2.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGksyHRLTPDKA------ 86
Cdd:COG1126    1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGT-ITVDG---EDLTDSKKdinklr 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  87 RELGVqvIYQDLSLFPNLTVAENIAFEL-NLKGYfgwfRKKQLREKALEILNEL-------AFtidpdtPVQfLPIAQRQ 158
Cdd:COG1126   77 RKVGM--VFQQFNLFPHLTVLENVTLAPiKVKKM----SKAEAEERAMELLERVgladkadAY------PAQ-LSGGQQQ 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 159 QVAICRALVADARLVIMDEPTASL---TRTEVnqlLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:COG1126  144 RVAIARALAMEPKVMLFDEPTSALdpeLVGEV---LDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGR 213
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
14-240 2.83e-36

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: 135.46  E-value: 2.83e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHR------------------------ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGs 69
Cdd:cd03294    1 IKIKGLYKIFGKNPqkafkllakgkskeeilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSG- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  70 KIEIDGKSYHRLTPDKAREL---GVQVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPD 146
Cdd:cd03294   80 KVLIDGQDIAAMSRKELRELrrkKISMVFQSFALLPHRTVLENVAFGLEVQG----VPRAEREERAAEALELVGLEGWEH 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 147 TPVQFLPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEV-NQLLSTVnylKDKGITVVFVSHRLEEVKEISDRIT 222
Cdd:cd03294  156 KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALdplIRREMqDELLRLQ---AELQKTIVFITHDLDEALRLGDRIA 232
                        250       260
                 ....*....|....*....|
gi 491046221 223 VIRDGQ--KIGTwPAEGLTT 240
Cdd:cd03294  233 IMKDGRlvQVGT-PEEILTN 251
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
14-228 8.62e-36

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: 133.23  E-value: 8.62e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRaLRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKArelGVQV 93
Cdd:cd03299    1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSG-KILLNGKDITNLPPEKR---DISY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLV 173
Cdd:cd03299   76 VPQNYALFPHMTVYKNIAYGLKKRKV----DKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 174 IMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03299  152 LLDEPFSALdvrTKEKLREELKKIR--KEFGVTVLHVTHDFEEAWALADKVAIMLNGK 207
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
14-230 8.77e-36

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 134.85  E-value: 8.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGksyHRLTPDKARELGvqv 93
Cdd:COG4152    2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGE-VLWDG---EPLDPEDRRRIG--- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 iYqdL----SLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:COG4152   75 -Y--LpeerGLYPKMKVGEQLVYLARLKGL----SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:COG4152  148 PELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
13-223 9.61e-36

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: 135.18  E-value: 9.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSF----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAP---DDGSkIEIDGKSYHRLTPDK 85
Cdd:COG0444    1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGE-ILFDGEDLLKLSEKE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  86 AREL---GVQVIYQD--LSLFPNLTVAENIAFELNLkgyFGWFRKKQLREKALEILNELAFTIDPDT----PVQFLPiAQ 156
Cdd:COG0444   80 LRKIrgrEIQMIFQDpmTSLNPVMTVGDQIAEPLRI---HGGLSKAEARERAIELLERVGLPDPERRldryPHELSG-GM 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 157 RQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITV 223
Cdd:COG0444  156 RQRVMIARALALEPKLLIADEPTTALdvtIQAQILNLLKDLQ--RELGLAILFITHDLGVVAEIADRVAV 223
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
18-233 1.14e-35

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: 132.03  E-value: 1.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  18 DLSKSFGGHRAlrNIDLTLNkGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDG-------KSYHrlTPDKARELG 90
Cdd:cd03297    5 DIEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGG-TIVLNGtvlfdsrKKIN--LPPQQRKIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  91 VqvIYQDLSLFPNLTVAENIAFELNLKgyfgwfRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADA 170
Cdd:cd03297   79 L--VFQQYALFPHLNVRENLAFGLKRK------RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQP 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 171 RLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTW 233
Cdd:cd03297  151 ELLLLDEPFSALDRALRLQLLPELKQIkKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
18-227 2.75e-35

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: 131.12  E-value: 2.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  18 DLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKsyhrltpdKARELGVQVIY-- 95
Cdd:cd03235    4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSG-SIRVFGK--------PLEKERKRIGYvp 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  96 QDLSL---FPnLTVAENIAFELNLK-GYFGWFRKKQlREKALEIL-----NELAftidpDTPVQFLPIAQRQQVAICRAL 166
Cdd:cd03235   75 QRRSIdrdFP-ISVRDVVLMGLYGHkGLFRRLSKAD-KAKVDEALervglSELA-----DRQIGELSGGQQQRVLLARAL 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 167 VADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRI-----TVIRDG 227
Cdd:cd03235  148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVlllnrTVVASG 213
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
6-250 3.57e-35

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 137.47  E-value: 3.57e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   6 KADKSDPLITLRDLS-KSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPD 84
Cdd:COG3845  250 PAEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGS-IRLDGEDITGLSPR 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  85 KARELGVQVIYQD---LSLFPNLTVAENIAFELNLKGYF---GWFRKKQLREKALEILNElaFTI---DPDTPVQFLPIA 155
Cdd:COG3845  329 ERRRLGVAYIPEDrlgRGLVPDMSVAENLILGRYRRPPFsrgGFLDRKAIRAFAEELIEE--FDVrtpGPDTPARSLSGG 406
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 156 QRQQVAICRALVADARLVIMDEPT-------ASLTRtevNQLLStvnyLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:COG3845  407 NQQKVILARELSRDPKLLIAAQPTrgldvgaIEFIH---QRLLE----LRDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
                        250       260
                 ....*....|....*....|..
gi 491046221 229 KIGTWPAEGLTTRKITELMTGL 250
Cdd:COG3845  480 IVGEVPAAEATREEIGLLMAGV 501
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
14-228 1.26e-34

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 132.89  E-value: 1.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSF----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:COG1135    2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGS-VLVDGVDLTALSERELRAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 --GVQVIYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILnEL--------AFtidpdtPVQfLPIAQRQQ 159
Cdd:COG1135   81 rrKIGMIFQHFNLLSSRTVAENVALPLEIAGV----PKAEIRKRVAELL-ELvglsdkadAY------PSQ-LSGGQKQR 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 160 VAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:COG1135  149 VGIARALANNPKVLLCDEATSALdpeTTRSILDLLKDIN--RELGLTIVLITHEMDVVRRICDRVAVLENGR 218
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
15-228 7.74e-34

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: 125.05  E-value: 7.74e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  15 TLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARElGVQVI 94
Cdd:cd00267    1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE-ILIDGKDIAKLPLEELRR-RIGYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  95 YQdLSlfpnltvaeniafelnlKGyfgwfrkkqlrekaleilnelaftidpdtpvqflpiaQRQQVAICRALVADARLVI 174
Cdd:cd00267   79 PQ-LS-----------------GG-------------------------------------QRQRVALARALLLNPDLLL 103
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491046221 175 MDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd00267  104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
14-230 1.06e-33

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: 126.63  E-value: 1.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSyhrLTPDKARELGvqv 93
Cdd:cd03269    1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSG-EVLFDGKP---LDIAARNRIG--- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 iY--QDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADAR 171
Cdd:cd03269   74 -YlpEERGLYPKMKVIDQLVYLAQLKGL----KKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:cd03269  149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
13-227 1.11e-33

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: 126.71  E-value: 1.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFGGHR----ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARE 88
Cdd:cd03266    1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG-FATVDGFDVVKEPAEARRR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  89 LGVqvIYQDLSLFPNLTVAENIafelnlkGYFGWFRKKQlREKALEILNELAFTID----PDTPVQFLPIAQRQQVAICR 164
Cdd:cd03266   80 LGF--VSDSTGLYDRLTARENL-------EYFAGLYGLK-GDELTARLEELADRLGmeelLDRRVGGFSTGMRQKVAIAR 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 165 ALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDG 227
Cdd:cd03266  150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
14-228 1.12e-33

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: 125.19  E-value: 1.12e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGG--HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELgV 91
Cdd:cd03228    1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE-ILIDGVDLRDLDLESLRKN-I 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIYQDLSLFpNLTVAENIafelnlkgyfgwfrkkqlrekaleilnelaftidpdtpvqfLPIAQRQQVAICRALVADAR 171
Cdd:cd03228   79 AYVPQDPFLF-SGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPP 116
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 172 LVIMDEPTASL-TRTEvNQLLSTVNYLKdKGITVVFVSHRLEEVKeISDRITVIRDGQ 228
Cdd:cd03228  117 ILILDEATSALdPETE-ALILEALRALA-KGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
14-228 1.80e-33

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: 134.58  E-value: 1.80e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARElgv 91
Cdd:COG2274  474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR-ILIDGIDLRQIDPASLRR--- 549
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIY--QDLSLFpNLTVAENIAF---ELNLkgyfgwfrkKQLREkALEILNELAFTID-P---DTPV----QFLPIAQRQ 158
Cdd:COG2274  550 QIGVvlQDVFLF-SGTIRENITLgdpDATD---------EEIIE-AARLAGLHDFIEAlPmgyDTVVgeggSNLSGGQRQ 618
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 159 QVAICRALVADARLVIMDEPTASL-TRTE--VNQLLSTVnylkDKGITVVFVSHRLEEVKeISDRITVIRDGQ 228
Cdd:COG2274  619 RLAIARALLRNPRILILDEATSALdAETEaiILENLRRL----LKGRTVIIIAHRLSTIR-LADRIIVLDKGR 686
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
14-232 2.91e-33

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: 125.70  E-value: 2.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGG--HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRlTPDKAR-ELG 90
Cdd:cd03263    1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGT-AYINGYSIRT-DRKAARqSLG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  91 vqVIYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADA 170
Cdd:cd03263   79 --YCPQFDALFDELTVREHLRFYARLKGL----PKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 171 RLVIMDEPTASL---TRTEVNQLLSTVNylkdKGITVVFVSHRLEEVKEISDRITVIRDGQK--IGT 232
Cdd:cd03263  153 SVLLLDEPTSGLdpaSRRAIWDLILEVR----KGRSIILTTHSMDEAEALCDRIAIMSDGKLrcIGS 215
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
3-228 3.44e-33

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: 132.57  E-value: 3.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   3 STSKADKSDPLITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRL 81
Cdd:COG4988  326 TAPLPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS-ILINGVDLSDL 404
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  82 TPDKARElgvQVIY--QDLSLFPnLTVAENIAF--------ELnlkgyfgwfrkkqlrEKALEILNELAFtID-----PD 146
Cdd:COG4988  405 DPASWRR---QIAWvpQNPYLFA-GTIRENLRLgrpdasdeEL---------------EAALEAAGLDEF-VAalpdgLD 464
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 147 TPV----QFLPIAQRQQVAICRALVADARLVIMDEPTASL-TRTEvNQLLSTVNYLKdKGITVVFVSHRLEEVKEiSDRI 221
Cdd:COG4988  465 TPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLdAETE-AEILQALRRLA-KGRTVILITHRLALLAQ-ADRI 541

                 ....*..
gi 491046221 222 TVIRDGQ 228
Cdd:COG4988  542 LVLDDGR 548
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
11-228 1.35e-32

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: 122.54  E-value: 1.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  11 DPLITLRDLSksfgGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELG 90
Cdd:cd03215    2 EPVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASG-EITLDGKPVTRRSPRDAIRAG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  91 VQVIYQD---LSLFPNLTVAENIAFELNLKGyfGwfrkkqlrekaleilNelaftidpdtpvqflpiaqrQQ-VAICRAL 166
Cdd:cd03215   77 IAYVPEDrkrEGLVLDLSVAENIALSSLLSG--G---------------N--------------------QQkVVLARWL 119
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 167 VADARLVIMDEPTASL---TRTEVNQLLstvNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03215  120 ARDPRVLILDEPTRGVdvgAKAEIYRLI---RELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
14-228 1.50e-32

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: 124.19  E-value: 1.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELGVQV 93
Cdd:cd03218    1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSG-KILLDGQDITKLPMHKRARLGIGY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLV 173
Cdd:cd03218   80 LPQEASIFRKLTVEENILAVLEIRGL----SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 174 IMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03218  156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGK 210
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
10-223 2.50e-32

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 126.00  E-value: 2.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSF----------GGH-RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSY 78
Cdd:COG4608    4 AEPLLEVRDLKKHFpvrgglfgrtVGVvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGE-ILFDGQDI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  79 HRLTPDKAREL--GVQVIYQD--LSLFPNLTVAENIAFELNLkgyFGWFRKKQLREKALEILNELAftIDPDT----PVQ 150
Cdd:COG4608   83 TGLSGRELRPLrrRMQMVFQDpyASLNPRMTVGDIIAEPLRI---HGLASKAERRERVAELLELVG--LRPEHadryPHE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 151 FlPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVnqllstVNYLKD----KGITVVFVSHRLEEVKEISDRITV 223
Cdd:COG4608  158 F-SGGQRQRIGIARALALNPKLIVCDEPVSALdvsIQAQV------LNLLEDlqdeLGLTYLFISHDLSVVRHISDRVAV 230
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
14-230 5.51e-32

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 122.81  E-value: 5.51e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSY---HRLTPDKAREL- 89
Cdd:COG4161    3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQ-LNIAGHQFdfsQKPSEKAIRLLr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 -GVQVIYQDLSLFPNLTVAEN-IAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALV 167
Cdd:COG4161   82 qKVGMVFQQYNLWPHLTVMENlIEAPCKVLG----LSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 168 ADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:COG4161  158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
12-213 1.69e-31

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 121.89  E-value: 1.69e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGGHR----ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAr 87
Cdd:COG4525    2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGE-ITLDGVPVTGPGADRG- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  88 elgvqVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALV 167
Cdd:COG4525   80 -----VVFQKDALLPWLNVLDNVAFGLRLRG----VPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 491046221 168 ADARLVIMDEPTASL---TRTEVNQLLSTVnyLKDKGITVVFVSHRLEE 213
Cdd:COG4525  151 ADPRFLLMDEPFGALdalTREQMQELLLDV--WQRTGKGVFLITHSVEE 197
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
14-228 9.11e-31

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 119.09  E-value: 9.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGgHRALRnIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKaRelGVQV 93
Cdd:COG3840    2 LRLDDLTYRYG-DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGR-ILWNGQDLTALPPAE-R--PVSM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENIAFEL--NLKgyfgwFRKKQlREKALEI-----LNELAftidpdtpvQFLPIA----QRQQVAI 162
Cdd:COG3840   76 LFQENNLFPHLTVAQNIGLGLrpGLK-----LTAEQ-RAQVEQAlervgLAGLL---------DRLPGQlsggQRQRVAL 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 163 CRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:COG3840  141 ARCLVRKRPILLLDEPFSALdpaLRQEMLDLVDELC--RERGLTVLMVTHDPEDAARIADRVLLVADGR 207
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
5-236 1.27e-30

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 122.64  E-value: 1.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   5 SKADKS-DPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTP 83
Cdd:PRK11607  10 AKTRKAlTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAG-QIMLDGVDLSHVPP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  84 DKARelgVQVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILN-----ELAftidPDTPVQfLPIAQRQ 158
Cdd:PRK11607  89 YQRP---INMMFQSYALFPHMTVEQNIAFGLKQDK----LPKAEIASRVNEMLGlvhmqEFA----KRKPHQ-LSGGQRQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 159 QVAICRALVADARLVIMDEPTASLTRTEVNQL-LSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ--KIGTwPA 235
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKfvQIGE-PE 235

                 .
gi 491046221 236 E 236
Cdd:PRK11607 236 E 236
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
15-228 1.43e-30

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: 117.15  E-value: 1.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  15 TLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTP-DKARELGV-- 91
Cdd:cd03214    1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE-ILLDGKDLASLSPkELARKIAYvp 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIYQdlslfpnltvaeniafeLNLkgyfgwfrkKQLREKaleILNELAFtidpdtpvqflpiAQRQQVAICRALVADAR 171
Cdd:cd03214   80 QALEL-----------------LGL---------AHLADR---PFNELSG-------------GERQRVLLARALAQEPP 117
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 172 LVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03214  118 ILLLDEPTSHLdiaHQIELLELLRRLA--RERGKTVVMVLHDLNLAARYADRVILLKDGR 175
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
11-256 5.67e-30

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: 117.49  E-value: 5.67e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  11 DPLITLRDLSKSFGGHRALRNIDLTLNKGEvHC-LAGTNGCGKSTLIKTISGVYAPDDGSKIEIDGKSYHRLTPDKARE- 88
Cdd:COG1119    1 DPLLELRNVTVRRGGKTILDDISWTVKPGE-HWaILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRGGEDVWELRKr 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  89 LGVqvIYQDLSL-FPNLTVAENIAfelnLKGYF---GWFRK--KQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAI 162
Cdd:COG1119   80 IGL--VSPALQLrFPRDETVLDVV----LSGFFdsiGLYREptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 163 CRALVADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWP-AEGLTT 240
Cdd:COG1119  154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPkEEVLTS 233
                        250
                 ....*....|....*.
gi 491046221 241 RKITELMtGLDIVHER 256
Cdd:COG1119  234 ENLSEAF-GLPVEVER 248
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
10-236 6.50e-30

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 117.40  E-value: 6.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:PRK11300   2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGT-ILLRGQHIEGLPGHQIARM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 GVQVIYQDLSLFPNLTVAEN--IAFELNLK-GYF-GWFRKKQLREKALEILNELAFTIDpdtPVQFLPIAQRQ------- 158
Cdd:PRK11300  81 GVVRTFQHVRLFREMTVIENllVAQHQQLKtGLFsGLLKTPAFRRAESEALDRAATWLE---RVGLLEHANRQagnlayg 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 159 ---QVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDGQKI--GT 232
Cdd:PRK11300 158 qqrRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLanGT 237

                 ....
gi 491046221 233 wPAE 236
Cdd:PRK11300 238 -PEE 240
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
269-502 1.63e-29

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 115.93  E-value: 1.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRagQY------RDINLNLKRGEVlglcgllgsgrteLAL-------------SLFGITHPDSGELFIEGKPVK 329
Cdd:COG1131    1 IEVRGLTK--RYgdktalDGVSLTVEPGEI-------------FGLlgpngagktttirMLLGLLRPTSGEVRVLGEDVA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 330 lkNNTDAIKRGIGYVSED-----RLTLGAILQqsiadnmvisILDRLktpwHLIDEKQCQDIVQEWIADLDIKvTDPNNA 404
Cdd:COG1131   66 --RDPAEVRRRIGYVPQEpalypDLTVRENLR----------FFARL----YGLPRKEARERIDELLELFGLT-DAADRK 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 405 LSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGS 484
Cdd:COG1131  129 VGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGR 208
                        250
                 ....*....|....*...
gi 491046221 485 IVKEIVTDSINEQQLEEI 502
Cdd:COG1131  209 IVADGTPDELKARLLEDV 226
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
14-228 2.51e-29

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 121.43  E-value: 2.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSksF---GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELg 90
Cdd:COG1132  340 IEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR-ILIDGVDIRDLTLESLRRQ- 415
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  91 VQVIYQDLSLFpNLTVAENIAF--------ELnlkgyfgwfrkkqlrEKALEILNELAFtID--P---DTPV----QFLP 153
Cdd:COG1132  416 IGVVPQDTFLF-SGTIRENIRYgrpdatdeEV---------------EEAAKAAQAHEF-IEalPdgyDTVVgergVNLS 478
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 154 IAQRQQVAICRALVADARLVIMDEPTASL-TRTE--VNQLLSTVnyLKDKgiTVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:COG1132  479 GGQRQRIAIARALLKDPPILILDEATSALdTETEalIQEALERL--MKGR--TTIVIAHRLSTIRN-ADRILVLDDGR 551
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
10-228 4.11e-29

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: 114.45  E-value: 4.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRA----LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPD- 84
Cdd:COG4181    5 SAPIIELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGT-VRLAGQDLFALDEDa 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  85 ----KARELGVqvIYQDLSLFPNLTVAENIAFELNLKGyfgwfrKKQLREKALEILNE--LAFTIDpDTPVQfLPIAQRQ 158
Cdd:COG4181   84 rarlRARHVGF--VFQSFQLLPTLTALENVMLPLELAG------RRDARARARALLERvgLGHRLD-HYPAQ-LSGGEQQ 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 159 QVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRlEEVKEISDRITVIRDGQ 228
Cdd:COG4181  154 RVALARAFATEPAILFADEPTGNLdaaTGEQIIDLLFELN--RERGTTLVLVTHD-PALAARCDRVLRLRAGR 223
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
14-238 4.63e-29

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: 114.20  E-value: 4.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVY-----APDDGsKIEIDGKS-YHRLTPDKAR 87
Cdd:cd03260    1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEG-EVLLDGKDiYDLDVDVLEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  88 ELGVQVIYQDLSLFPnLTVAENIAFELNLKGYfgwFRKKQLREKALEILNELAFT--IDPDTPVQFLPIAQRQQVAICRA 165
Cdd:cd03260   80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGI---KLKEELDERVEEALRKAALWdeVKDRLHALGLSGGQQQRLCLARA 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 166 LVADARLVIMDEPTASL---TRTEVNQLLSTvnyLKDKgITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGL 238
Cdd:cd03260  156 LANEPEVLLLDEPTSALdpiSTAKIEELIAE---LKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
14-230 4.66e-29

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 114.73  E-value: 4.66e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSY---HRLTPDKAREL- 89
Cdd:PRK11124   3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSG-TLNIAGNHFdfsKTPSDKAIRELr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 -GVQVIYQDLSLFPNLTVAEN-IAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDT-PVQfLPIAQRQQVAICRAL 166
Cdd:PRK11124  82 rNVGMVFQQYNLWPHLTVQQNlIEAPCRVLG----LSKDQALARAEKLLERLRLKPYADRfPLH-LSGGQQQRVAIARAL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 167 VADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
3-228 9.69e-29

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: 119.49  E-value: 9.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   3 STSKADKSDPLITLRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHR 80
Cdd:COG4987  323 AEPAPAPGGPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS-ITLGGVDLRD 401
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  81 LTPDKARELgVQVIYQDLSLFpNLTVAENIAF--------ELnlkgyfgwfrkkqlrEKALEI--LNELAFTIDP--DTP 148
Cdd:COG4987  402 LDEDDLRRR-IAVVPQRPHLF-DTTLRENLRLarpdatdeEL---------------WAALERvgLGDWLAALPDglDTW 464
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 149 V----QFLPIAQRQQVAICRALVADARLVIMDEPTASL-TRTEvNQLLSTV-NYLKDKgiTVVFVSHRLEEVkEISDRIT 222
Cdd:COG4987  465 LgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLdAATE-QALLADLlEALAGR--TVLLITHRLAGL-ERMDRIL 540

                 ....*.
gi 491046221 223 VIRDGQ 228
Cdd:COG4987  541 VLEDGR 546
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
10-486 1.50e-28

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: 118.63  E-value: 1.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGG----HRALRNIDLTLNKGEVHCLAGTNGCGKS----TLIKTISGVYAPDDGSkIEIDGKSYHRL 81
Cdd:COG4172    3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGS-ILFDGQDLLGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  82 TPDKAREL-GVQV--IYQD--LSLFPNLTVAENIAFELNL-KGyfgwFRKKQLREKALEILNELAFTiDPDTPVQFLPI- 154
Cdd:COG4172   82 SERELRRIrGNRIamIFQEpmTSLNPLHTIGKQIAEVLRLhRG----LSGAAARARALELLERVGIP-DPERRLDAYPHq 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 155 ---AQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTvnyLKDK-GITVVFVSHRLEEVKEISDRITVIRDG 227
Cdd:COG4172  157 lsgGQRQRVMIAMALANEPDLLIADEPTTALdvtVQAQILDLLKD---LQRElGMALLLITHDLGVVRRFADRVAVMRQG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 228 QKIGTWPAEGLT-------TRKItelmtgLDIVHERKPPNNAEDRRTVLEIKNLS-----RAGQYR----------DINL 285
Cdd:COG4172  234 EIVEQGPTAELFaapqhpyTRKL------LAAEPRGDPRPVPPDAPPLLEARDLKvwfpiKRGLFRrtvghvkavdGVSL 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 286 NLKRGEvlglcgllgsgrT-----E-------LALSLFGItHPDSGELFIEGKPVKLKNNTD--AIKRGIGYVSED---- 347
Cdd:COG4172  308 TLRRGE------------TlglvgEsgsgkstLGLALLRL-IPSEGEIRFDGQDLDGLSRRAlrPLRRRMQVVFQDpfgs 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 348 ---RLTLGAIlqqsIADNMVIsildrlktpwHLI--DEKQCQDIVQEWIAD--LDIKVTD--PNnalsTLSGGNQQKVVL 418
Cdd:COG4172  375 lspRMTVGQI----IAEGLRV----------HGPglSAAERRARVAEALEEvgLDPAARHryPH----EFSGGQRQRIAI 436
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 419 AKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGV-GISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:COG4172  437 ARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
44-232 2.28e-28

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


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 114.90  E-value: 2.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   44 LAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKArelGVQVIYQDLSLFPNLTVAENIAFELNLKGYFGWF 123
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGS-IMLDGEDVTNVPPHLR---HINMVFQSYALFPHMTVEENVAFGLKMRKVPRAE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  124 RKKQLREkALEILNELAFTidPDTPVQfLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GI 202
Cdd:TIGR01187  77 IKPRVLE-ALRLVQLEEFA--DRKPHQ-LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGI 152
                         170       180       190
                  ....*....|....*....|....*....|..
gi 491046221  203 TVVFVSHRLEEVKEISDRITVIRDGQ--KIGT 232
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKiaQIGT 184
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
14-237 3.39e-28

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: 111.69  E-value: 3.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIeIDGKSYHRLTPDKARELGvqV 93
Cdd:cd03265    1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-VAGHDVVREPREVRRRIG--I 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENIAFELNLKGYFGwfrkKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLV 173
Cdd:cd03265   78 VFQDLSVDDELTGWENLYIHARLYGVPG----AERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 174 IMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIgtwpAEG 237
Cdd:cd03265  154 FLDEPTIGLdpqTRAHVWEYIEKLK--EEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII----AEG 214
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
14-227 5.60e-28

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: 110.96  E-value: 5.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRL----TPDKARE 88
Cdd:cd03292    1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGT-IRVNGQDVSDLrgraIPYLRRK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  89 LGVqvIYQDLSLFPNLTVAENIAFELNLKGYFGwfrkKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVA 168
Cdd:cd03292   80 IGV--VFQDFRLLPDRNVYENVAFALEVTGVPP----REIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVN 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 169 DARLVIMDEPTASL---TRTEVNQLLSTVNylkDKGITVVFVSHRLEEVKEISDRITVIRDG 227
Cdd:cd03292  154 SPTILIADEPTGNLdpdTTWEIMNLLKKIN---KAGTTVVVATHAKELVDTTRHRVIALERG 212
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
14-238 1.28e-27

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 111.00  E-value: 1.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS----KIEIDGKSYHRLTPDKAREL 89
Cdd:PRK11264   4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTirvgDITIDTARSLSQQKGLIRQL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 GVQV--IYQDLSLFPNLTVAENIafelnLKGYFgwFRKKQLREKAL----EILNELAFTIDPDTPVQFLPIAQRQQVAIC 163
Cdd:PRK11264  84 RQHVgfVFQNFNLFPHRTVLENI-----IEGPV--IVKGEPKEEATararELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 164 RALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGL 238
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
18-270 1.30e-27

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: 113.66  E-value: 1.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  18 DLSKSFGGHrALrNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGK------SYHRLTPDKaRELGV 91
Cdd:COG4148    6 DFRLRRGGF-TL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGR-IRLGGEvlqdsaRGIFLPPHR-RRIGY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 qvIYQDLSLFPNLTVAENIAFelnlkGYfgWFRKKQLRekaleilnelafTIDPDTPVQFLPIA-------------QRQ 158
Cdd:COG4148   82 --VFQEARLFPHLSVRGNLLY-----GR--KRAPRAER------------RISFDEVVELLGIGhlldrrpatlsggERQ 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 159 QVAICRALVADARLVIMDEPTASLTRTEVNQLLStvnYL----KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIgtwp 234
Cdd:COG4148  141 RVAIGRALLSSPRLLLMDEPLAALDLARKAEILP---YLerlrDELDIPILYVSHSLDEVARLADHVVLLEQGRVV---- 213
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 491046221 235 AEGlttrKITELMTGLDIVherkPPNNAEDRRTVLE 270
Cdd:COG4148  214 ASG----PLAEVLSRPDLL----PLAGGEEAGSVLE 241
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
13-213 1.41e-27

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 110.94  E-value: 1.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKsyhRLTPDKArELGvq 92
Cdd:PRK11248   1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGS-ITLDGK---PVEGPGA-ERG-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  93 VIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARL 172
Cdd:PRK11248  74 VVFQNEGLLPWRNVQDNVAFGLQLAG----VEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 491046221 173 VIMDEPTASL---TRTEVNQLLSTVnyLKDKGITVVFVSHRLEE 213
Cdd:PRK11248 150 LLLDEPFGALdafTREQMQTLLLKL--WQETGKQVLLITHDIEE 191
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
15-222 3.04e-27

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 108.72  E-value: 3.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  15 TLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPD---DGsKIEIDGKSYHRLtPDKARELGv 91
Cdd:COG4136    3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSG-EVLLNGRRLTAL-PAEQRRIG- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 qVIYQDLSLFPNLTVAENIAFELNLKgyfgwFRKKQLREKALEILNELA----FTIDPDTpvqfLPIAQRQQVAICRALV 167
Cdd:COG4136   80 -ILFQDDLLFPHLSVGENLAFALPPT-----IGRAQRRARVEQALEEAGlagfADRDPAT----LSGGQRARVALLRALL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 168 ADARLVIMDEPTASL---TRTEVNQLlsTVNYLKDKGITVVFVSHRLEEVKEISDRIT 222
Cdd:COG4136  150 AEPRALLLDEPFSKLdaaLRAQFREF--VFEQIRQRGIPALLVTHDEEDAPAAGRVLD 205
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
13-227 3.23e-27

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 109.41  E-value: 3.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIeIDGKSYHRLTPDKA---REL 89
Cdd:PRK09493   1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLI-VDGLKVNDPKVDERlirQEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 GvqVIYQDLSLFPNLTVAENIAF-ELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVA 168
Cdd:PRK09493  80 G--MVFQQFYLFPHLTALENVMFgPLRVRG----ASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 169 DARLVIMDEPTASLT---RTEVnqlLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDG 227
Cdd:PRK09493 154 KPKLMLFDEPTSALDpelRHEV---LKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
13-228 3.69e-27

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 110.10  E-value: 3.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDD--GSKIEIDGKSYH---RLTPD--K 85
Cdd:PRK09984   4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsaGSHIELLGRTVQregRLARDirK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  86 ARElGVQVIYQDLSLFPNLTVAENIafelnLKGYFG----------WFRKKQlREKALEILNELAFTIDPDTPVQFLPIA 155
Cdd:PRK09984  84 SRA-NTGYIFQQFNLVNRLSVLENV-----LIGALGstpfwrtcfsWFTREQ-KQRALQALTRVGMVHFAHQRVSTLSGG 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 156 QRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
29-231 7.47e-27

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: 108.32  E-value: 7.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKarelgvQVIYQDLSLFPNLTVAE 108
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGG-VILEGKQITEPGPDR------MVVFQNYSLLPWLTVRE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  109 NIAfeLNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASL---TRT 185
Cdd:TIGR01184  74 NIA--LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALdalTRG 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 491046221  186 EVNQLLstVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDG--QKIG 231
Cdd:TIGR01184 152 NLQEEL--MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGpaANIG 197
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
24-228 8.51e-27

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 113.69  E-value: 8.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  24 GGHRA-LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDkarELGVQVIY--QDLSL 100
Cdd:COG4618  342 GSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAG-SVRLDGADLSQWDRE---ELGRHIGYlpQDVEL 417
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 101 FPNlTVAENIA-FE--------------------LNL-KGYfgwfrkkqlrekaleilnelaftidpDTPV----QFLPI 154
Cdd:COG4618  418 FDG-TIAENIArFGdadpekvvaaaklagvhemiLRLpDGY--------------------------DTRIgeggARLSG 470
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 155 AQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHR---LEEVkeisDRITVIRDGQ 228
Cdd:COG4618  471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRpslLAAV----DKLLVLRDGR 543
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
16-435 9.68e-27

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 113.24  E-value: 9.68e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  16 LRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGksyhrltpdkarelGVQVIY 95
Cdd:COG0488    1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGE-VSIPK--------------GLRIGY 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  96 --QDLSLFPNLTVAENIA-------------FELNLKGYF-------------------GWfrkkQLREKALEILNELAF 141
Cdd:COG0488   66 lpQEPPLDDDLTVLDTVLdgdaelraleaelEELEAKLAEpdedlerlaelqeefealgGW----EAEARAEEILSGLGF 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 142 T-IDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTasltrtevNQL-LSTV----NYLKDKGITVVFVSH-R--LE 212
Cdd:COG0488  142 PeEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPT--------NHLdLESIewleEFLKNYPGTVLVVSHdRyfLD 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 213 EVkeiSDRITVIrDGQKIGTWP-------------------AEGLTTRKITEL--------------------------M 247
Cdd:COG0488  214 RV---ATRILEL-DRGKLTLYPgnysayleqraerleqeaaAYAKQQKKIAKEeefirrfrakarkakqaqsrikalekL 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 248 TGLDIVHERKPPN---NAEDR--RTVLEIKNLSRAGQ----YRDINLNLKRGEvlglcgllgsgR-----------TELA 307
Cdd:COG0488  290 EREEPPRRDKTVEirfPPPERlgKKVLELEGLSKSYGdktlLDDLSLRIDRGD-----------RigligpngagkSTLL 358
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 308 LSLFGITHPDSGElFIEGKPVKlknntdaikrgIGYVSEDRLTLgaILQQSIADNMvisildrlktpWHLIDEKQCQDIV 387
Cdd:COG0488  359 KLLAGELEPDSGT-VKLGETVK-----------IGYFDQHQEEL--DPDKTVLDEL-----------RDGAPGGTEQEVR 413
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 491046221 388 QeWIADLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPT 435
Cdd:COG0488  414 G-YLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
7-228 1.17e-26

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: 113.24  E-value: 1.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   7 ADKSDPLITLRDLSKSF-----------GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVyAPDDGsKIEIDG 75
Cdd:COG4172  269 PPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEG-EIRFDG 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  76 KSYHRLTPDKAREL--GVQVIYQD--LSLFPNLTVAENIAfElNLKGYFGWFRKKQLREKALEILNELAftIDPDT---- 147
Cdd:COG4172  347 QDLDGLSRRALRPLrrRMQVVFQDpfGSLSPRMTVGQIIA-E-GLRVHGPGLSAAERRARVAEALEEVG--LDPAArhry 422
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 148 PVQFlPIAQRQQVAICRALVADARLVIMDEPTASLTRT---EVNQLLSTvnyLKDK-GITVVFVSHRLEEVKEISDRITV 223
Cdd:COG4172  423 PHEF-SGGQRQRIAIARALILEPKLLVLDEPTSALDVSvqaQILDLLRD---LQREhGLAYLFISHDLAVVRALAHRVMV 498

                 ....*
gi 491046221 224 IRDGQ 228
Cdd:COG4172  499 MKDGK 503
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
1-231 1.30e-26

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 108.23  E-value: 1.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   1 MTSTSKADKSDPLiTLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGskiEIDGKSyhr 80
Cdd:PRK11247   1 MMNTARLNQGTPL-LLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG---ELLAGT--- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  81 lTP-DKARElGVQVIYQDLSLFPNLTVAENIAfeLNLKGyfGWfrkkqlREKALEILNELAFTiD--PDTPVQfLPIAQR 157
Cdd:PRK11247  74 -APlAEARE-DTRLMFQDARLLPWKKVIDNVG--LGLKG--QW------RDAALQALAAVGLA-DraNEWPAA-LSGGQK 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 158 QQVAICRALVADARLVIMDEPTA---SLTRTEVNQLLstVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQkIG 231
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGaldALTRIEMQDLI--ESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK-IG 213
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
14-230 1.90e-26

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 107.86  E-value: 1.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFG-G----HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDK-AR 87
Cdd:COG1101    2 LELKNLSKTFNpGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSG-SILIDGKDVTKLPEYKrAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  88 ELGvQViYQDLSL--FPNLTVAENIAFELNlKG---YFGWFRKKQLREKALEILNELAFTID--PDTPVQFLPIAQRQQV 160
Cdd:COG1101   81 YIG-RV-FQDPMMgtAPSMTIEENLALAYR-RGkrrGLRRGLTKKRRELFRELLATLGLGLEnrLDTKVGLLSGGQRQAL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 161 AICRALVADARLVIMDEPTASL---TRTEVNQLlsTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:COG1101  158 SLLMATLTKPKLLLLDEHTAALdpkTAALVLEL--TEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
14-228 2.35e-26

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 109.51  E-value: 2.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHR----ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKAREL 89
Cdd:PRK11153   2 IELKNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSG-RVLVDGQDLTALSEKELRKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 GVQV--IYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPDT-PVQfLPIAQRQQVAICRAL 166
Cdd:PRK11153  81 RRQIgmIFQHFNLLSSRTVFDNVALPLELAGT----PKAEIKARVTELLELVGLSDKADRyPAQ-LSGGQKQRVAIARAL 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 167 VADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK11153 156 ASNPKVLLCDEATSALdpaTTRSILELLKDIN--RELGLTIVLITHEMDVVKRICDRVAVIDAGR 218
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
14-241 2.37e-26

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 107.41  E-value: 2.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPdkaRELGvqv 93
Cdd:PRK11231   3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSG-TVFLGDKPISMLSS---RQLA--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 iyQDLSLFPN-------LTVAENIAF----ELNLKGYFGWfRKKQLREKALEI--LNELAftidpDTPVQFLPIAQRQQV 160
Cdd:PRK11231  76 --RRLALLPQhhltpegITVRELVAYgrspWLSLWGRLSA-EDNARVNQAMEQtrINHLA-----DRRLTDLSGGQRQRA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 161 AICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI--GTwPAEGL 238
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMaqGT-PEEVM 226

                 ...
gi 491046221 239 TTR 241
Cdd:PRK11231 227 TPG 229
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
14-492 5.42e-26

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: 111.05  E-value: 5.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGV--YAPDDGSKI---------------EIDG- 75
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpSKVGe 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   76 ---KSYHRLTPDKARELG------------VQVIYQ-DLSLFPNLTVAENIAFELNLKGYFGwfrkKQLREKALEILNEL 139
Cdd:TIGR03269  81 pcpVCGGTLEPEEVDFWNlsdklrrrirkrIAIMLQrTFALYGDDTVLDNVLEALEEIGYEG----KEAVGRAVDLIEMV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  140 AFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVnyLKDKGITVVFVSHRLEEVKE 216
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLdpqTAKLVHNALEEA--VKASGISMVLTSHWPEVIED 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  217 ISDRITVIRDGQKIgtwpAEGLTTRKITELMTGldiVHERKPPNNAEDRRTVLEIKNLSR------AGQYR---DINLNL 287
Cdd:TIGR03269 235 LSDKAIWLENGEIK----EEGTPDEVVAVFMEG---VSEVEKECEVEVGEPIIKVRNVSKryisvdRGVVKavdNVSLEV 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  288 KRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFiegkpVKLKNN-TDAIKRGIGYVSEDRLTLGAILQQ-------SI 359
Cdd:TIGR03269 308 KEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVN-----VRVGDEwVDMTKPGPDGRGRAKRYIGILHQEydlyphrTV 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  360 ADNMVISI-------LDRLKTPWHL----IDEKQCQDIVQewiadldiKVTDpnnalsTLSGGNQQKVVLAKWILTRPKV 428
Cdd:TIGR03269 383 LDNLTEAIglelpdeLARMKAVITLkmvgFDEEKAEEILD--------KYPD------ELSEGERHRVALAQVLIKEPRI 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  429 LILDSPTvgvdiGAKDSIYKLihrlsGVGISILLITDEASEAYY-----------NCDRILHMKQGSIVK-----EIVTD 492
Cdd:TIGR03269 449 VILDEPT-----GTMDPITKV-----DVTHSILKAREEMEQTFIivshdmdfvldVCDRAALMRDGKIVKigdpeEIVEE 518
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
14-247 9.28e-26

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 108.25  E-value: 9.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLtpdKARELGVQV 93
Cdd:PRK10851   3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSG-HIRFHGTDVSRL---HARDRKVGF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENIAFELNLKGyfgwfRKKQ-----LREKALEILNELAFT-IDPDTPVQfLPIAQRQQVAICRALV 167
Cdd:PRK10851  79 VFQHYALFRHMTVFDNIAFGLTVLP-----RRERpnaaaIKAKVTQLLEMVQLAhLADRYPAQ-LSGGQKQRVALARALA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 168 ADARLVIMDEPTASL---TRTEVNQLLSTV-NYLKdkgITVVFVSHRLEEVKEISDRITVIRDG--QKIGT----W--PA 235
Cdd:PRK10851 153 VEPQILLLDEPFGALdaqVRKELRRWLRQLhEELK---FTSVFVTHDQEEAMEVADRVVVMSQGniEQAGTpdqvWrePA 229
                        250
                 ....*....|..
gi 491046221 236 egltTRKITELM 247
Cdd:PRK10851 230 ----TRFVLEFM 237
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
14-230 4.86e-25

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: 103.07  E-value: 4.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELgVQ 92
Cdd:cd03254    3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKG-QILIDGIDIRDISRKSLRSM-IG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  93 VIYQDLSLFPNlTVAENIAFELNLKgyfgwfrKKQLREKALEILNELAFTI----DPDTPV----QFLPIAQRQQVAICR 164
Cdd:cd03254   81 VVLQDTFLFSG-TIMENIRLGRPNA-------TDEEVIEAAKEAGAHDFIMklpnGYDTVLgengGNLSQGERQLLAIAR 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 165 ALVADARLVIMDEPTASL-TRTE--VNQLLSTVNylkdKGITVVFVSHRLEEVKEiSDRITVIRDGQKI 230
Cdd:cd03254  153 AMLRDPKILILDEATSNIdTETEklIQEALEKLM----KGRTSIIIAHRLSTIKN-ADKILVLDDGKII 216
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
14-227 4.94e-25

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 106.27  E-value: 4.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKArelGVQV 93
Cdd:PRK11000   4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSG-DLFIGEKRMNDVPPAER---GVGM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLR---EKALEILnELAFTID--PDTpvqfLPIAQRQQVAICRALVA 168
Cdd:PRK11000  80 VFQSYALYPHLSVAENMSFGLKLAG----AKKEEINqrvNQVAEVL-QLAHLLDrkPKA----LSGGQRQRVAIGRTLVA 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 169 DARLVIMDEPTASL-------TRTEVNQLlstvnyLKDKGITVVFVSHRLEEVKEISDRITVIRDG 227
Cdd:PRK11000 151 EPSVFLLDEPLSNLdaalrvqMRIEISRL------HKRLGRTMIYVTHDQVEAMTLADKIVVLDAG 210
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
14-228 6.81e-25

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: 102.28  E-value: 6.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARElGV 91
Cdd:cd03245    3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGS-VLLDGTDIRQLDPADLRR-NI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIYQDLSLFpNLTVAENIAFelnlkgyFGWFRKKQLREKALEILNELAFT-IDP---DTPV----QFLPIAQRQQVAIC 163
Cdd:cd03245   81 GYVPQDVTLF-YGTLRDNITL-------GAPLADDERILRAAELAGVTDFVnKHPnglDLQIgergRGLSGGQRQAVALA 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 164 RALVADARLVIMDEPTASLTRTEVNQLLSTV-NYLKDKgiTVVFVSHRLeEVKEISDRITVIRDGQ 228
Cdd:cd03245  153 RALLNDPPILLLDEPTSAMDMNSEERLKERLrQLLGDK--TLIIITHRP-SLLDLVDRIIVMDSGR 215
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
14-228 7.37e-25

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: 102.19  E-value: 7.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGgHRALRnIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDkarELGVQV 93
Cdd:cd03298    1 VRLDKIRFSYG-EQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGR-VLINGVDVTAAPPA---DRPVSM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENIAFELN--LKgyfgwfRKKQLREKALEILNELAFT-IDPDTPVQfLPIAQRQQVAICRALVADA 170
Cdd:cd03298   75 LFQENNLFAHLTVEQNVGLGLSpgLK------LTAEDRQAIEVALARVGLAgLEKRLPGE-LSGGERQRVALARVLVRDK 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 171 RLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03298  148 PVLLLDEPFAALdpaLRAEMLDLVLDLH--AETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
12-241 9.24e-25

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 103.08  E-value: 9.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKS------YHRLTPDK 85
Cdd:PRK11701   5 PLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGE-VHYRMRDgqlrdlYALSEAER 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  86 AR----ELGvqVIYQDL--SLFPNLTVAENIAFELNLkgyFGWFRKKQLREKALEILNELafTIDP----DTPVQFL-PI 154
Cdd:PRK11701  84 RRllrtEWG--FVHQHPrdGLRMQVSAGGNIGERLMA---VGARHYGDIRATAGDWLERV--EIDAaridDLPTTFSgGM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 155 AQRQQVAicRALVADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTw 233
Cdd:PRK11701 157 QQRLQIA--RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES- 233

                 ....*...
gi 491046221 234 paeGLTTR 241
Cdd:PRK11701 234 ---GLTDQ 238
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
12-240 9.46e-25

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 106.08  E-value: 9.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTpdkARELGV 91
Cdd:PRK09536   2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGT-VLVAGDDVEALS---ARAASR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QV--IYQDLSLFPNLTVAENIafELNLKGYFGWFRK-----KQLREKALEILNELAFTidpDTPVQFLPIAQRQQVAICR 164
Cdd:PRK09536  78 RVasVPQDTSLSFEFDVRQVV--EMGRTPHRSRFDTwtetdRAAVERAMERTGVAQFA---DRPVTSLSGGERQRVLLAR 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 165 ALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDG--QKIGTwPAEGLTT 240
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGrvRAAGP-PADVLTA 229
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
13-228 1.84e-24

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 101.58  E-value: 1.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFGgHRALRnIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSyHRLTPDKARElgVQ 92
Cdd:PRK10771   1 MLKLTDITWLYH-HLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGS-LTLNGQD-HTTTPPSRRP--VS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  93 VIYQDLSLFPNLTVAENIAFELN----LKGYfgwfRKKQLREKA-----LEILNELaftidpdtPVQfLPIAQRQQVAIC 163
Cdd:PRK10771  75 MLFQENNLFSHLTVAQNIGLGLNpglkLNAA----QREKLHAIArqmgiEDLLARL--------PGQ-LSGGQRQRVALA 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 164 RALVADARLVIMDEPTASLT---RTEVNQLLSTVnyLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK10771 142 RCLVREQPILLLDEPFSALDpalRQEMLTLVSQV--CQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
14-228 3.17e-24

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: 99.21  E-value: 3.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRA--LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDkarELGV 91
Cdd:cd03246    1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSG-RVRLDGADISQWDPN---ELGD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIY--QDLSLFPNlTVAENIafelnLKGyfgwfrkkqlrekaleilnelaftidpdtpvqflpiAQRQQVAICRALVAD 169
Cdd:cd03246   77 HVGYlpQDDELFSG-SIAENI-----LSG------------------------------------GQRQRLGLARALYGN 114
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLeEVKEISDRITVIRDGQ 228
Cdd:cd03246  115 PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGR 172
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
24-228 4.29e-24

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


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 105.51  E-value: 4.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   24 GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKareLGVQVIY--QDLSLF 101
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGS-VRLDGADLKQWDRET---FGKHIGYlpQDVELF 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  102 PNlTVAENIA-FELNlkgyfgwFRKKQLREKA-LEILNEL--AFTIDPDTPV----QFLPIAQRQQVAICRALVADARLV 173
Cdd:TIGR01842 405 PG-TVAENIArFGEN-------ADPEKIIEAAkLAGVHELilRLPDGYDTVIgpggATLSGGQRQRIALARALYGDPKLV 476
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 491046221  174 IMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLeEVKEISDRITVIRDGQ 228
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRP-SLLGCVDKILVLQDGR 530
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
16-247 4.66e-24

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 103.26  E-value: 4.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  16 LRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSyhrLTPDKARELGVQVIY 95
Cdd:PRK11432   9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEG-QIFIDGED---VTHRSIQQRDICMVF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  96 QDLSLFPNLTVAENIAFELNLKGYFGWFRKKQLREkALEILNELAFTidpDTPVQFLPIAQRQQVAICRALVADARLVIM 175
Cdd:PRK11432  85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKE-ALELVDLAGFE---DRYVDQISGGQQQRVALARALILKPKVLLF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 176 DEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELM 247
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFM 233
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
12-228 7.09e-24

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 100.10  E-value: 7.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDK-AReLG 90
Cdd:COG1137    2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSG-RIFLDGEDITHLPMHKrAR-LG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  91 VQVIYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNElaFTIDP--DTPVQFLPIAQRQQVAICRALVA 168
Cdd:COG1137   80 IGYLPQEASIFRKLTVEDNILAVLELRKL----SKKEREERLEELLEE--FGITHlrKSKAYSLSGGERRRVEIARALAT 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 169 DARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:COG1137  154 NPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGK 213
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
14-228 7.87e-24

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: 100.00  E-value: 7.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELgV 91
Cdd:cd03251    1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGR-ILIDGHDVRDYTLASLRRQ-I 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIYQDLSLFpNLTVAENIAFelnlkGYFGWFRKKQlrEKALEILNELAFTID-P---DTPVQ----FLPIAQRQQVAIC 163
Cdd:cd03251   79 GLVSQDVFLF-NDTVAENIAY-----GRPGATREEV--EEAARAANAHEFIMElPegyDTVIGergvKLSGGQRQRIAIA 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 164 RALVADARLVIMDEPTASL-TRTE--VNQLLStvNYLKDKgiTVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:cd03251  151 RALLKDPPILILDEATSALdTESErlVQAALE--RLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGK 213
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
11-211 7.96e-24

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: 104.75  E-value: 7.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   11 DPLITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:TIGR02868 332 KPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGE-VTLDGVPVSSLDQDEVRRR 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   90 gVQVIYQDLSLFpNLTVAENIAFElnlkgyfgwfRKKQLREKALEILNELAFTIDP-------DTPV----QFLPIAQRQ 158
Cdd:TIGR02868 411 -VSVCAQDAHLF-DTTVRENLRLA----------RPDATDEELWAALERVGLADWLralpdglDTVLgeggARLSGGERQ 478
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 491046221  159 QVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYlKDKGITVVFVSHRL 211
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
12-241 1.01e-23

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 101.91  E-value: 1.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSF----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVyaPDDGSKIEID-----GKSYHRLT 82
Cdd:COG4170    2 PLLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI--TKDNWHVTADrfrwnGIDLLKLS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  83 PDKAREL---GVQVIYQD--LSLFPNLTVAENIAFEL---NLKGYFgWFRKKQLREKALEILNELAFTIDPDT----PVQ 150
Cdd:COG4170   80 PRERRKIigrEIAMIFQEpsSCLDPSAKIGDQLIEAIpswTFKGKW-WQRFKWRKKRAIELLHRVGIKDHKDImnsyPHE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 151 fLPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDG 227
Cdd:COG4170  159 -LTEGECQKVMIAMAIANQPRLLIADEPTNAMestTQAQIFRLLARLN--QLQGTSILLISHDLESISQWADTITVLYCG 235
                        250
                 ....*....|....
gi 491046221 228 QKIGTWPAEGLTTR 241
Cdd:COG4170  236 QTVESGPTEQILKS 249
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
33-228 1.43e-23

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


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 98.39  E-value: 1.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   33 DLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPdkaRELGVQVIYQDLSLFPNLTVAENIAF 112
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGS-IKVNDQSHTGLAP---YQRPVSMLFQENNLFAHLTVRQNIGL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  113 ELNLKGYFGWFRKKQLREKALE--ILNELAftidpDTPVQfLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQL 190
Cdd:TIGR01277  94 GLHPGLKLNAEQQEKVVDAAQQvgIADYLD-----RLPEQ-LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM 167
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 491046221  191 LSTVNYLKD-KGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:TIGR01277 168 LALVKQLCSeRQRTLLMVTHHLSDARAIASQIAVVSQGK 206
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
14-228 1.78e-23

type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274550 [Multi-domain]  Cd Length: 694  Bit Score: 104.18  E-value: 1.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   14 ITLRDLSKSFGG--HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARElGV 91
Cdd:TIGR03375 464 IEFRNVSFAYPGqeTPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGS-VLLDGVDIRQIDPADLRR-NI 541
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   92 QVIYQDLSLFpNLTVAENIAFELNLkgyfgwFRKKQLREkALEILNELAFT-IDP---DTPV----QFLPIAQRQQVAIC 163
Cdd:TIGR03375 542 GYVPQDPRLF-YGTLRDNIALGAPY------ADDEEILR-AAELAGVTEFVrRHPdglDMQIgergRSLSGGQRQAVALA 613
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221  164 RALVADARLVIMDEPTASL-TRTEvNQLLSTVN-YLKDKgiTVVFVSHRLeEVKEISDRITVIRDGQ 228
Cdd:TIGR03375 614 RALLRDPPILLLDEPTSAMdNRSE-ERFKDRLKrWLAGK--TLVLVTHRT-SLLDLVDRIIVMDNGR 676
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
11-236 1.85e-23

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: 103.34  E-value: 1.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   11 DPLITLRDLSKSF-----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEIDGKSYHRLTPDK 85
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPG 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   86 ARELG-----VQVIYQDLSLFPNLTVAENIAFELNLKGYFGWFRKKQL---------REKALEILNELaftidPDTpvqf 151
Cdd:TIGR03269 357 PDGRGrakryIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVitlkmvgfdEEKAEEILDKY-----PDE---- 427
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  152 LPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQllSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMdpiTKVDVTH--SILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGK 505

                  ....*...
gi 491046221  229 KIGTWPAE 236
Cdd:TIGR03269 506 IVKIGDPE 513
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
10-253 2.08e-23

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 100.26  E-value: 2.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSyhrlTPDKARE- 88
Cdd:PRK13537   4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGS-ISLCGEP----VPSRARHa 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  89 -LGVQVIYQDLSLFPNLTVAENIafeLNLKGYFGwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALV 167
Cdd:PRK13537  79 rQRVGVVPQFDNLDPDFTVRENL---LVFGRYFG-LSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 168 ADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIgtwpAEGlTTRKITELM 247
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKI----AEG-APHALIESE 229

                 ....*.
gi 491046221 248 TGLDIV 253
Cdd:PRK13537 230 IGCDVI 235
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
269-486 2.80e-23

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: 97.74  E-value: 2.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRA-GQY---RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklknnTDAIKRGIGYV 344
Cdd:cd03269    1 LEVENVTKRfGRVtalDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-----DIAARNRIGYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 345 SEDRltlGAILQQSIADNMVisILDRLKTpwhlIDEKQCQDIVQEWIADLDIKvTDPNNALSTLSGGNQQKVVLAKWILT 424
Cdd:cd03269   76 PEER---GLYPKMKVIDQLV--YLAQLKG----LKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIH 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 425 RPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:cd03269  146 DPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
10-222 5.55e-23

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 97.09  E-value: 5.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKAREl 89
Cdd:PRK10247   4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSG-TLLFEGEDISTLKPEIYRQ- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 gvQVIY--QDLSLFPNlTVAENIAFELNLkgyfgwfRKKQLREKALeiLNELAFTIDPDT----PVQFLPIAQRQQVAIC 163
Cdd:PRK10247  82 --QVSYcaQTPTLFGD-TVYDNLIFPWQI-------RNQQPDPAIF--LDDLERFALPDTiltkNIAELSGGEKQRISLI 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 164 RALVADARLVIMDEPTASL---TRTEVNQLLStvNYLKDKGITVVFVSHRLEEVKEISDRIT 222
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALdesNKHNVNEIIH--RYVREQNIAVLWVTHDKDEINHADKVIT 209
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
10-247 6.46e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 98.14  E-value: 6.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKAR 87
Cdd:PRK13632   4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSG-EIKIDGITISKENLKEIR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  88 ElGVQVIYQDL-SLFPNLTVAENIAFELNlkgyfgwfRKKQLREKALEILNELAFTIDP----DTPVQFLPIAQRQQVAI 162
Cdd:PRK13632  83 K-KIGIIFQNPdNQFIGATVEDDIAFGLE--------NKKVPPKKMKDIIDDLAKKVGMedylDKEPQNLSGGQKQRVAI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 163 CRALVADARLVIMDEPTASLT---RTEVNQLLSTVNYLKDKgiTVVFVSHRLEEVKeISDRITVIRDGQ--KIGTwPAEG 237
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDpkgKREIKKIMVDLRKTRKK--TLISITHDMDEAI-LADKVIVFSEGKliAQGK-PKEI 229
                        250
                 ....*....|
gi 491046221 238 LTTRKITELM 247
Cdd:PRK13632 230 LNNKEILEKA 239
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
7-228 8.08e-23

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 101.71  E-value: 8.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   7 ADKSDPLITLRDLSKSF-----------GGHRALRNIDLTLNKGEVHCLAGTNGCGKST----LIKTIsgvyaPDDGSkI 71
Cdd:PRK15134 269 PEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGE-I 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  72 EIDGKSYHRLT-----PDKARelgVQVIYQD--LSLFPNLTVAENIAFELNLkgYFGWFRKKQLREKALEILNELAftID 144
Cdd:PRK15134 343 WFDGQPLHNLNrrqllPVRHR---IQVVFQDpnSSLNPRLNVLQIIEEGLRV--HQPTLSAAQREQQVIAVMEEVG--LD 415
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 145 PDT----PVQFlPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISD 219
Cdd:PRK15134 416 PETrhryPAEF-SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCH 494

                 ....*....
gi 491046221 220 RITVIRDGQ 228
Cdd:PRK15134 495 QVIVLRQGE 503
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
267-485 1.01e-22

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 97.08  E-value: 1.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 267 TVLEIKNLSRAgqY------RDINLNLKRGEVlglcgllgsgrteLAL---------SLF----GITHPDSGELFIEGKP 327
Cdd:COG1121    5 PAIELENLTVS--YggrpvlEDVSLTIPPGEF-------------VAIvgpngagksTLLkailGLLPPTSGTVRLFGKP 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 328 VKLKnntdaiKRGIGYVSedrltlgailQQSIAD-NMVISILD------RLKTPWHLIDEKQCQDIVQEWIADLDIkvTD 400
Cdd:COG1121   70 PRRA------RRRIGYVP----------QRAEVDwDFPITVRDvvlmgrYGRRGLFRRPSRADREAVDEALERVGL--ED 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 401 -PNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILH 479
Cdd:COG1121  132 lADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLL 211

                 ....*.
gi 491046221 480 MKQGSI 485
Cdd:COG1121  212 LNRGLV 217
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
9-237 1.20e-22

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 98.75  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   9 KSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSyhrlTPDKAR- 87
Cdd:PRK13536  37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG-KITVLGVP----VPARARl 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  88 -ELGVQVIYQDLSLFPNLTVAENIafeLNLKGYFGWFRKKQlrEKALEILNELA-FTIDPDTPVQFLPIAQRQQVAICRA 165
Cdd:PRK13536 112 aRARIGVVPQFDNLDLEFTVRENL---LVFGRYFGMSTREI--EAVIPSLLEFArLESKADARVSDLSGGMKRRLTLARA 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 166 LVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIgtwpAEG 237
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKI----AEG 254
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
3-224 1.27e-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: 100.82  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221    3 STSKADKSDPLITLRDLSKSFGGHR-ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRL 81
Cdd:TIGR02857 311 KAPVTAAPASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS-IAVNGVPLADA 389
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   82 TPDKARElgvQVIY--QDLSLFPNlTVAENIAF--------ELnlkgyfgwfRKKQLREKALEILNELAFTIDpdTPV-- 149
Cdd:TIGR02857 390 DADSWRD---QIAWvpQHPFLFAG-TIAENIRLarpdasdaEI---------REALERAGLDEFVAALPQGLD--TPIge 454
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221  150 --QFLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKdKGITVVFVSHRLeEVKEISDRITVI 224
Cdd:TIGR02857 455 ggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRL-ALAALADRIVVL 529
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
13-232 1.51e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 97.07  E-value: 1.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGK--SYHRLTPDKAREl 89
Cdd:PRK13639   1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSG-EVLIKGEpiKYDKKSLLEVRK- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 GVQVIYQ--DLSLFPNlTVAENIAF-ELNLKgyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRAL 166
Cdd:PRK13639  79 TVGIVFQnpDDQLFAP-TVEEDVAFgPLNLG-----LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 167 VADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGT 232
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
12-228 2.33e-22

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 95.65  E-value: 2.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGGHR----ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIeIDGKSYHRLTP-DKA 86
Cdd:PRK11629   4 ILLQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVI-FNGQPMSKLSSaAKA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  87 ----RELGVqvIYQDLSLFPNLTVAENIAFELnlkgYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAI 162
Cdd:PRK11629  83 elrnQKLGF--IYQFHHLLPDFTALENVAMPL----LIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAI 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 163 CRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISdRITVIRDGQ 228
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLdarNADSIFQLLGELN--RLQGTAFLVVTHDLQLAKRMS-RQLEMRDGR 222
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
13-249 2.45e-22

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 95.73  E-value: 2.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVyAPDDGSKIEIDGKSYhRLTPDKAREL-GV 91
Cdd:PRK10895   3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGI-VPRDAGNIIIDDEDI-SLLPLHARARrGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIYQDLSLFPNLTVAENIAFELNLKGYFgwfRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADAR 171
Cdd:PRK10895  81 GYLPQEASIFRRLSVYDNLMAVLQIRDDL---SAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI--GTwPAEGLTTRKITELMTG 249
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIahGT-PTEILQDEHVKRVYLG 236
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
14-228 3.15e-22

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: 93.53  E-value: 3.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLtpDKARELGV 91
Cdd:cd03247    1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGE-ITLDGVPVSDL--EKALSSLI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIYQDLSLFpNLTVAENIAfeLNLKGyfgwfrkkqlrekaleilnelaftidpdtpvqflpiAQRQQVAICRALVADAR 171
Cdd:cd03247   78 SVLNQRPYLF-DTTLRNNLG--RRFSG------------------------------------GERQRLALARILLQDAP 118
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTV-NYLKDKgiTVVFVSHRLEEVKEIsDRITVIRDGQ 228
Cdd:cd03247  119 IVLLDEPTVGLDPITERQLLSLIfEVLKDK--TLIWITHHLTGIEHM-DKILFLENGK 173
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
14-232 4.07e-22

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: 94.91  E-value: 4.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSF---GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELg 90
Cdd:cd03249    1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGE-ILLDGVDIRDLNLRWLRSQ- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  91 VQVIYQDLSLFPNlTVAENIAFELNlkgyfgwFRKKQLREKALEILNELAFTID-P---DTPVQF----LPIAQRQQVAI 162
Cdd:cd03249   79 IGLVSQEPVLFDG-TIAENIRYGKP-------DATDEEVEEAAKKANIHDFIMSlPdgyDTLVGErgsqLSGGQKQRIAI 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 163 CRALVADARLVIMDEPTASL-TRTE--VNQLLSTVNylkdKGITVVFVSHRLEEVKEiSDRITVIRDGQKI--GT 232
Cdd:cd03249  151 ARALLRNPKILLLDEATSALdAESEklVQEALDRAM----KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVeqGT 220
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
269-485 4.60e-22

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: 92.85  E-value: 4.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS-RAGQY---RDINLNLKRGEVlglcgllgsgrteLAL-------------SLFGITHPDSGELFIEGKPVKlk 331
Cdd:cd03230    1 IEVRNLSkRYGKKtalDDISLTVEKGEI-------------YGLlgpngagkttlikIILGLLKPDSGEIKVLGKDIK-- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 332 NNTDAIKRGIGYVSEDrltlgailqqsiadnmvISILDRLkTPWHLIDekqcqdivqewiadldikvtdpnnalstLSGG 411
Cdd:cd03230   66 KEPEEVKRRIGYLPEE-----------------PSLYENL-TVRENLK----------------------------LSGG 99
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 412 NQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSI 485
Cdd:cd03230  100 MKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
22-222 5.63e-22

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 93.45  E-value: 5.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  22 SFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKieidgksyhrltpdkARELGVQVIY--QDLS 99
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYvpQRSE 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 100 L---FPnLTVAEniAFELNLKGYFGWFRK-----KQLREKALEI--LNELAftidpDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:NF040873  66 VpdsLP-LTVRD--LVAMGRWARRGLWRRltrddRAAVDDALERvgLADLA-----GRQLGELSGGQRQRALLAQGLAQE 137
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRIT 222
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
14-228 6.46e-22

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 94.76  E-value: 6.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSF----------------------GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkI 71
Cdd:COG1134    5 IEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR-V 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  72 EIDGksyhRLTPdkarELGVQVIYQdlslfPNLTVAENIAFELNLKGyfgwFRKKQLREKALEIlneLAFT-IDP--DTP 148
Cdd:COG1134   84 EVNG----RVSA----LLELGAGFH-----PELTGRENIYLNGRLLG----LSRKEIDEKFDEI---VEFAeLGDfiDQP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 149 VQFLPIAQRQQVAICRALVADARLVIMDEPTA---------SLTRtevnqllstVNYLKDKGITVVFVSHRLEEVKEISD 219
Cdd:COG1134  144 VKTYSSGMRARLAFAVATAVDPDILLVDEVLAvgdaafqkkCLAR---------IRELRESGRTVIFVSHSMGAVRRLCD 214

                 ....*....
gi 491046221 220 RITVIRDGQ 228
Cdd:COG1134  215 RAIWLEKGR 223
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
18-227 2.97e-21

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 93.11  E-value: 2.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  18 DLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKsYHRLTPDKARELGV------ 91
Cdd:PRK10619  10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGS-IVVNGQ-TINLVRDKDGQLKVadknql 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 -------QVIYQDLSLFPNLTVAENI-AFELNLKGyfgwFRKKQLREKALEILNELAftIDPDTPVQF---LPIAQRQQV 160
Cdd:PRK10619  88 rllrtrlTMVFQHFNLWSHMTVLENVmEAPIQVLG----LSKQEARERAVKYLAKVG--IDERAQGKYpvhLSGGQQQRV 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 161 AICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDG 227
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
14-246 5.35e-21

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 92.28  E-value: 5.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIE----IDGKSYHRLTPDKAREL 89
Cdd:PRK14247   4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSgevyLDGQDIFKMDVIELRRR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 gVQVIYQDLSLFPNLTVAENIAFELNLKGYFGwfRKKQLREKALEILnELAFTIDP-----DTPVQFLPIAQRQQVAICR 164
Cdd:PRK14247  84 -VQMVFQIPNPIPNLSIFENVALGLKLNRLVK--SKKELQERVRWAL-EKAQLWDEvkdrlDAPAGKLSGGQQQRLCIAR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 165 ALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKdKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKIT 244
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELK-KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238

                 ..
gi 491046221 245 EL 246
Cdd:PRK14247 239 EL 240
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
15-228 6.67e-21

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: 90.78  E-value: 6.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  15 TLRDLSKSFG-GHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRltpdKARELGVQV 93
Cdd:cd03226    1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSG-SILLNGKPIKA----KERRKSIGY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLS--LFPNlTVAENIAfeLNLKGYfgwfrkkqlrEKALEILNELAFTIDPDTPVQFLPIA----QRQQVAICRALV 167
Cdd:cd03226   76 VMQDVDyqLFTD-SVREELL--LGLKEL----------DAGNEQAETVLKDLDLYALKERHPLSlsggQKQRLAIAAALL 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 168 ADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03226  143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
10-230 7.00e-21

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 91.76  E-value: 7.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTIS--GVYAPDDGSKIEIDGKSYHRLTP---- 83
Cdd:PRK14239   2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVTITGSIVYNGHNIYSPrtdt 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  84 -DKARELGvqVIYQDLSLFPnLTVAENIAFELNLKGyfgwFRKKQLREKALE-------ILNELAFTIDpDTPVQfLPIA 155
Cdd:PRK14239  82 vDLRKEIG--MVFQQPNPFP-MSIYENVVYGLRLKG----IKDKQVLDEAVEkslkgasIWDEVKDRLH-DSALG-LSGG 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 156 QRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKgITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLI 226
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
270-483 8.12e-21

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 90.67  E-value: 8.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 270 EIKNLS-RAGQY---RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNntdaikRGIGYVS 345
Cdd:cd03235    1 EVEDLTvSYGGHpvlEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER------KRIGYVP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 346 edrltlgailQQSIAD-NMVISILD------RLKTPWHLIDEKQCQDIVQEWIADLDIkvTD-PNNALSTLSGGNQQKVV 417
Cdd:cd03235   75 ----------QRRSIDrDFPISVRDvvlmglYGHKGLFRRLSKADKAKVDEALERVGL--SElADRQIGELSGGQQQRVL 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 418 LAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:cd03235  143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
10-459 9.10e-21

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 95.16  E-value: 9.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSF--GGH--RALRNIDLTLNKGEVHCLAGTNGCGKST-------LIKTISGVYAPDDgskIEIDGKSY 78
Cdd:PRK15134   2 TQPLLAIENLSVAFrqQQTvrTVVNDVSLQIEAGETLALVGESGSGKSVtalsilrLLPSPPVVYPSGD---IRFHGESL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  79 hrLTPDKARELGVQ-----VIYQD--LSLFPNLTVAENIAFELNL-KGyfgwFRKKQLREKALEILNEL----AFTIDPD 146
Cdd:PRK15134  79 --LHASEQTLRGVRgnkiaMIFQEpmVSLNPLHTLEKQLYEVLSLhRG----MRREAARGEILNCLDRVgirqAAKRLTD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 147 TPVQfLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIR 225
Cdd:PRK15134 153 YPHQ-LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQ 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 226 DGQKIGTWPAEGL-------TTRKItelmtgLDIVHERKPPNNAEDRRTVLEIKNLS-----RAGQYR----------DI 283
Cdd:PRK15134 232 NGRCVEQNRAATLfsapthpYTQKL------LNSEPSGDPVPLPEPASPLLDVEQLQvafpiRKGILKrtvdhnvvvkNI 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 284 NLNLKRGEVLGLCGLLGSGRTELALSLFGIThPDSGELFIEGKPVKLKNNTD--AIKRGIGYVSED-------RLTlgai 354
Cdd:PRK15134 306 SFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQllPVRHRIQVVFQDpnsslnpRLN---- 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 355 LQQSIADNM-----VISILDRlktpwhlidEKQCQDIVQEWIADLDIKVTDPnnalSTLSGGNQQKVVLAKWILTRPKVL 429
Cdd:PRK15134 381 VLQIIEEGLrvhqpTLSAAQR---------EQQVIAVMEEVGLDPETRHRYP----AEFSGGQRQRIAIARALILKPSLI 447
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 491046221 430 ILDSPTVGVDIGAKDSIYKLI------HRLSGVGIS 459
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLkslqqkHQLAYLFIS 483
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
28-252 1.04e-20

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 92.00  E-value: 1.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  28 ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSyhrLTPDKARELGVQV--IYQDL-SLFPNL 104
Cdd:PRK13635  22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGT-ITVGGMV---LSEETVWDVRRQVgmVFQNPdNQFVGA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 105 TVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASLT- 183
Cdd:PRK13635  98 TVQDDVAFGLENIG----VPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDp 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 184 --RTEVnqlLSTVNYLKD-KGITVVFVSHRLEEVKEiSDRITVIRDGQKIgtwpAEGlTTRKITELMT-----GLDI 252
Cdd:PRK13635 174 rgRREV---LETVRQLKEqKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL----EEG-TPEEIFKSGHmlqeiGLDV 241
cbiO PRK13646
energy-coupling factor transporter ATPase;
26-228 1.30e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 91.76  E-value: 1.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  26 HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKA-----RELGVQVIYQDLSL 100
Cdd:PRK13646  20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGT-VTVDDITITHKTKDKYirpvrKRIGMVFQFPESQL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 101 FPNlTVAENIA-----FELNLkgyfgwfrkKQLREKALEILNELAFTID--PDTPVQfLPIAQRQQVAICRALVADARLV 173
Cdd:PRK13646  99 FED-TVEREIIfgpknFKMNL---------DEVKNYAHRLLMDLGFSRDvmSQSPFQ-MSGGQMRKIAIVSILAMNPDII 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 174 IMDEPTASLTRTEVNQLLSTVNYLK-DKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGS 223
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
11-230 1.45e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 91.83  E-value: 1.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  11 DPLITLRDLSKSFG-GHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGK--SYHRLTPDKAR 87
Cdd:PRK13636   3 DYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSG-RILFDGKpiDYSRKGLMKLR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  88 ElGVQVIYQ--DLSLFpNLTVAENIAF-ELNLKgyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICR 164
Cdd:PRK13636  82 E-SVGMVFQdpDNQLF-SASVYQDVSFgAVNLK-----LPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAG 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 165 ALVADARLVIMDEPTASLTRTEVNQLLS-TVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKlLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
11-228 2.28e-20

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 93.98  E-value: 2.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  11 DPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIdGKsyhrltpdkarelG 90
Cdd:COG0488  313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG-TVKL-GE-------------T 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  91 VQVIY--QDLSLF-PNLTVAENI------AFELNLKGYFGWFRkkqlrekaleilnelaFT-IDPDTPVQFLPIAQRQQV 160
Cdd:COG0488  378 VKIGYfdQHQEELdPDKTVLDELrdgapgGTEQEVRGYLGRFL----------------FSgDDAFKPVGVLSGGEKARL 441
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 161 AICRALVADARLVIMDEPTASL---TRTEVNQLLStvNYlkdKGiTVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:COG0488  442 ALAKLLLSPPNVLLLDEPTNHLdieTLEALEEALD--DF---PG-TVLLVSHDRYFLDRVATRILEFEDGG 506
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
14-228 2.43e-20

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: 89.98  E-value: 2.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHR-ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARElGVQ 92
Cdd:cd03253    1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGS-ILIDGQDIREVTLDSLRR-AIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  93 VIYQDLSLFpNLTVAENIAFElNLKGyfgwfRKKQLRE--KALEILNE-LAFTIDPDTPVQ----FLPIAQRQQVAICRA 165
Cdd:cd03253   79 VVPQDTVLF-NDTIGYNIRYG-RPDA-----TDEEVIEaaKAAQIHDKiMRFPDGYDTIVGerglKLSGGEKQRVAIARA 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 166 LVADARLVIMDEPTASL-TRTEvNQLLSTVNYLKdKGITVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:cd03253  152 ILKNPPILLLDEATSALdTHTE-REIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGR 212
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
14-230 3.23e-20

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: 89.70  E-value: 3.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHR---------------------ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIE 72
Cdd:cd03267    1 IEVSNLSKSYRVYSkepgligslkslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGE-VR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  73 IDGKSYHRLTPDKARELGVqVIYQDLSLFPNLTVAEniAFELNLKGY-FGWFRKKQLREKALEILNELAFTidpDTPVQF 151
Cdd:cd03267   80 VAGLVPWKRRKKFLRRIGV-VFGQKTQLWWDLPVID--SFYLLAAIYdLPPARFKKRLDELSELLDLEELL---DTPVRQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 152 LPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03267  154 LSLGQRMRAEIAAALLHEPEILFLDEPTIGLdvvAQENIRNFLKEYN--RERGTTVLLTSHYMKDIEALARRVLVIDKGR 231

                 ..
gi 491046221 229 KI 230
Cdd:cd03267  232 LL 233
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
12-228 5.02e-20

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 89.17  E-value: 5.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGV 91
Cdd:PRK11614   4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGR-IVFDGKDITDWQTAKIMREAV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIYQDLSLFPNLTVAENIAFElnlkgyfGWFRKKQLREKALEILNELaftidpdTPVQFLPIAQR---------QQVAI 162
Cdd:PRK11614  83 AIVPEGRRVFSRMTVEENLAMG-------GFFAERDQFQERIKWVYEL-------FPRLHERRIQRagtmsggeqQMLAI 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 163 CRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
27-224 5.05e-20

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 90.92  E-value: 5.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL--GVQVIYQD--LSLFP 102
Cdd:PRK15079  35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGE-VAWLGKDLLGMKDDEWRAVrsDIQMIFQDplASLNP 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 103 NLTVAENIAFElnLKGYFGWFRKKQLREKALEILnelaftidpdTPVQFLP--I---------AQRQQVAICRALVADAR 171
Cdd:PRK15079 114 RMTIGEIIAEP--LRTYHPKLSRQEVKDRVKAMM----------LKVGLLPnlInryphefsgGQCQRIGIARALILEPK 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 172 LVIMDEPTASLtrtEVNQLLSTVNYLKD----KGITVVFVSHRLEEVKEISDRITVI 224
Cdd:PRK15079 182 LIICDEPVSAL---DVSIQAQVVNLLQQlqreMGLSLIFIAHDLAVVKHISDRVLVM 235
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
12-245 5.34e-20

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 89.45  E-value: 5.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDK-ARELG 90
Cdd:PRK13548   1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSG-EVRLNGRPLADWSPAElARRRA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  91 vqVIYQDLSL-FPnLTVAENIAFELnLKGYFGWFRKKQLREKALEI--LNELAftidpDTPVQFLPIAQRQQVAICRALV 167
Cdd:PRK13548  80 --VLPQHSSLsFP-FTVEEVVAMGR-APHGLSRAEDDALVAAALAQvdLAHLA-----GRDYPQLSGGEQQRVQLARVLA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 168 ------ADARLVIMDEPTASLTRTEVNQLLSTV-NYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI--GTwPAEGL 238
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAHQHHVLRLArQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVadGT-PAEVL 229

                 ....*..
gi 491046221 239 TTRKITE 245
Cdd:PRK13548 230 TPETLRR 236
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
14-236 6.34e-20

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 91.06  E-value: 6.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPdkaRELGVQ 92
Cdd:PRK11650   4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE-IWIGGRVVNELEP---ADRDIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  93 VIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLR---EKALEILnELAftidpdtpvQFL---PIA----QRQQVAI 162
Cdd:PRK11650  80 MVFQNYALYPHMSVRENMAYGLKIRG----MPKAEIEervAEAARIL-ELE---------PLLdrkPRElsggQRQRVAM 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 163 CRALVADARLVIMDEPTASL-------TRTEVNQL---LSTvnylkdkgiTVVFVSHRLEEVKEISDRITVIRDGQ--KI 230
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLdaklrvqMRLEIQRLhrrLKT---------TSLYVTHDQVEAMTLADRVVVMNGGVaeQI 216

                 ....*.
gi 491046221 231 GTwPAE 236
Cdd:PRK11650 217 GT-PVE 221
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
268-486 1.09e-19

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: 87.95  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 268 VLEIKNLS-----RAGQYR---DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKR 339
Cdd:cd03257    1 LLEVKNLSvsfptGGGSVKaldDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 340 G--IGYVSED-------RLTLGailqQSIADNMVIsildrlktpwHLIDEKQCQDivQEWIADLDIKVTDPNNAL----S 406
Cdd:cd03257   81 RkeIQMVFQDpmsslnpRMTIG----EQIAEPLRI----------HGKLSKKEAR--KEAVLLLLVGVGLPEEVLnrypH 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 407 TLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSI 485
Cdd:cd03257  145 ELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224

                 .
gi 491046221 486 V 486
Cdd:cd03257  225 V 225
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
14-228 1.17e-19

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: 87.59  E-value: 1.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSF----------------------GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKI 71
Cdd:cd03220    1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG-TV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  72 EIDGKSYHRLtpdkarELGVqviyqdlSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEIL--NELAFTIdpDTPV 149
Cdd:cd03220   80 TVRGRVSSLL------GLGG-------GFNPELTGRENIYLNGRLLG----LSRKEIDEKIDEIIefSELGDFI--DLPV 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 150 QFLPIAQRQQVAICRALVADARLVIMDEPTA---SLTRTEVNQLLSTvnyLKDKGITVVFVSHRLEEVKEISDRITVIRD 226
Cdd:cd03220  141 KTYSSGMKARLAFAIATALEPDILLIDEVLAvgdAAFQEKCQRRLRE---LLKQGKTVILVSHDPSSIKRLCDRALVLEK 217

                 ..
gi 491046221 227 GQ 228
Cdd:cd03220  218 GK 219
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
28-228 1.42e-19

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: 87.93  E-value: 1.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  28 ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGksYHRLTPDKA---RELGvqVIYQDLSLFpNL 104
Cdd:cd03252   17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENG-RVLVDG--HDLALADPAwlrRQVG--VVLQENVLF-NR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 105 TVAENIAFE------------LNLKGYFGWFRkkQLREKALEILNELAFTidpdtpvqfLPIAQRQQVAICRALVADARL 172
Cdd:cd03252   91 SIRDNIALAdpgmsmervieaAKLAGAHDFIS--ELPEGYDTIVGEQGAG---------LSGGQRQRIAIARALIHNPRI 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 173 VIMDEPTASLTRTEVNQLLSTVNYLKDkGITVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:cd03252  160 LIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGR 213
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
28-232 1.43e-19

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 90.86  E-value: 1.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  28 ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKAREL---GVQVIYQDLSLFPNL 104
Cdd:PRK10070  43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG-QVLIDGVDIAKISDAELREVrrkKIAMVFQSFALMPHM 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 105 TVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASL-- 182
Cdd:PRK10070 122 TVLDNTAFGMELAG----INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALdp 197
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491046221 183 -TRTEVNQLLSTVNYLKDKgiTVVFVSHRLEEVKEISDRITVIRDGQ--KIGT 232
Cdd:PRK10070 198 lIRTEMQDELVKLQAKHQR--TIVFISHDLDEAMRIGDRIAIMQNGEvvQVGT 248
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
12-228 1.43e-19

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: 87.49  E-value: 1.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSF-----GGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS--------KIEIDGK 76
Cdd:COG4778    3 TLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilvrhdggWVDLAQA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  77 SYHRLTPDKARELGvqviY--QDLSLFPNLT----VAENiAFELNlkgyfgwFRKKQLREKALEILNELA-----FTIDP 145
Cdd:COG4778   83 SPREILALRRRTIG----YvsQFLRVIPRVSaldvVAEP-LLERG-------VDREEARARARELLARLNlperlWDLPP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 146 DTpvqFlPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTvnyLKDKGITVVFVSHRLEEVKEISDRIT 222
Cdd:COG4778  151 AT---F-SGGEQQRVNIARGFIADPPLLLLDEPTASLdaaNRAVVVELIEE---AKARGTAIIGIFHDEEVREAVADRVV 223

                 ....*.
gi 491046221 223 VIRDGQ 228
Cdd:COG4778  224 DVTPFS 229
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
13-228 1.58e-19

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 92.09  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   13 LITLRDLSKSFGGH---RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPD------DGSKI-EIDGKSYHRlt 82
Cdd:TIGR00958 478 LIEFQDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTggqvllDGVPLvQYDHHYLHR-- 555
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   83 pdkarelGVQVIYQDLSLFpNLTVAENIAFELNLKgyfgwfRKKQLREKALE------ILNelaFTIDPDTPV----QFL 152
Cdd:TIGR00958 556 -------QVALVGQEPVLF-SGSVRENIAYGLTDT------PDEEIMAAAKAanahdfIME---FPNGYDTEVgekgSQL 618
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221  153 PIAQRQQVAICRALVADARLVIMDEPTASLTrTEVNQLLSTVNYLKDKgiTVVFVSHRLEEVkEISDRITVIRDGQ 228
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALD-AECEQLLQESRSRASR--TVLLIAHRLSTV-ERADQILVLKKGS 690
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
12-240 2.60e-19

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 87.82  E-value: 2.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGGH---------RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLT 82
Cdd:PRK10419   2 TLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQG-NVSWRGEPLAKLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  83 PDKAREL--GVQVIYQD-LSLF-PNLTVAENIAFEL----NLKgyfgwfrKKQLREKALEILN--ELAFTIDPDTPVQfL 152
Cdd:PRK10419  81 RAQRKAFrrDIQMVFQDsISAVnPRKTVREIIREPLrhllSLD-------KAERLARASEMLRavDLDDSVLDKRPPQ-L 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 153 PIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDGQKIG 231
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232

                 ....*....
gi 491046221 232 TWPAEGLTT 240
Cdd:PRK10419 233 TQPVGDKLT 241
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
269-501 2.69e-19

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: 86.62  E-value: 2.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS--RAGQY---RDINLNLKRGEvlglcgllgsgR-----------TELALSLFGITHPDSGELFIEGKPVKlKN 332
Cdd:COG1122    1 IELENLSfsYPGGTpalDDVSLSIEKGE-----------FvaiigpngsgkSTLLRLLNGLLKPTSGEVLVDGKDIT-KK 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 333 NTDAIKRGIGYVsedrltlgaiLQQsiADNMVIS--ILD-------RLKtpwhlIDEKQCQDIVQEWIADLDI-----KV 398
Cdd:COG1122   69 NLRELRRKVGLV----------FQN--PDDQLFAptVEEdvafgpeNLG-----LPREEIRERVEEALELVGLehladRP 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 399 TdpnnalSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRIL 478
Cdd:COG1122  132 P------HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVI 205
                        250       260
                 ....*....|....*....|....*
gi 491046221 479 HMKQGSIVKEIVTDSI--NEQQLEE 501
Cdd:COG1122  206 VLDDGRIVADGTPREVfsDYELLEE 230
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
13-231 3.24e-19

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 86.47  E-value: 3.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRL----TPDKAR 87
Cdd:PRK10908   1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAG-KIWFSGHDITRLknreVPFLRR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  88 ELGvqVIYQDLSLFPNLTVAENIAFELNLKGYFGwfrkKQLREKALEILNELAFtIDP--DTPVQfLPIAQRQQVAICRA 165
Cdd:PRK10908  80 QIG--MIFQDHHLLMDRTVYDNVAIPLIIAGASG----DDIRRRVSAALDKVGL-LDKakNFPIQ-LSGGEQQRVGIARA 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 166 LVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIG 231
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
11-245 1.23e-18

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 85.94  E-value: 1.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  11 DPLITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:PRK13647   2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGR-VKVMGREVNAENEKWVRSK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 gVQVIYQDL--SLFPNlTVAENIAF-ELNLKgyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRAL 166
Cdd:PRK13647  81 -VGLVFQDPddQVFSS-TVWDDVAFgPVNMG-----LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 167 VADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITE 245
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVE 232
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
13-228 1.28e-18

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 85.83  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKS--YHRLTPDKARElG 90
Cdd:PRK13638   1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGA-VLWQGKPldYSKRGLLALRQ-Q 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  91 VQVIYQD--LSLFPNlTVAENIAFEL-NLkgyfGWFRKKQLR--EKALEILNELAFTidpDTPVQFLPIAQRQQVAICRA 165
Cdd:PRK13638  79 VATVFQDpeQQIFYT-DIDSDIAFSLrNL----GVPEAEITRrvDEALTLVDAQHFR---HQPIQCLSHGQKKRVAIAGA 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 166 LVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQ 213
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
14-230 1.47e-18

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 86.68  E-value: 1.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSF---------GG------HR------ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIE 72
Cdd:COG4586    2 IEVENLSKTYrvyekepglKGalkglfRReyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGE-VR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  73 IDGKSYHRLTPDKARELGVqVIYQDLSLFPNLTVAENiaFELNlkgyfgwfRK-----KQLREKALEILNELaFTIDP-- 145
Cdd:COG4586   81 VLGYVPFKRRKEFARRIGV-VFGQRSQLWWDLPAIDS--FRLL--------KAiyripDAEYKKRLDELVEL-LDLGEll 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 146 DTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRIT 222
Cdd:COG4586  149 DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLdvvSKEAIREFLKEYN--RERGTTILLTSHDMDDIEALCDRVI 226

                 ....*...
gi 491046221 223 VIRDGQKI 230
Cdd:COG4586  227 VIDHGRII 234
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
281-486 1.89e-18

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: 83.85  E-value: 1.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTdaikRGIGYVSEDrltLGAIL-QQSI 359
Cdd:cd03226   17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR----KSIGYVMQD---VDYQLfTDSV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 360 ADNMVISILDrlktpwhlIDEKQCQdiVQEWIADLDIKVTDPNNALStLSGGNQQKVVLAKWILTRPKVLILDSPTVGVD 439
Cdd:cd03226   90 REELLLGLKE--------LDAGNEQ--AETVLKDLDLYALKERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491046221 440 IGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:cd03226  159 YKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
cbiO PRK13640
energy-coupling factor transporter ATPase;
10-228 2.61e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 85.24  E-value: 2.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDG--SKIEIDGKSYHRLTPDK 85
Cdd:PRK13640   2 KDNIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNpnSKITVDGITLTAKTVWD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  86 ARElGVQVIYQDL-SLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICR 164
Cdd:PRK13640  82 IRE-KVGIVFQNPdNQFVGATVGDDVAFGLENRA----VPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAG 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 165 ALVADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVkEISDRITVIRDGQ 228
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDGK 220
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
20-230 2.71e-18

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: 82.98  E-value: 2.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  20 SKSFGGHRA-LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISG--VYAPDDGSkIEIDGKsyhrltPDKARELGVQVIY- 95
Cdd:cd03213   15 SSPSKSGKQlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGE-VLINGR------PLDKRSFRKIIGYv 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  96 -QDLSLFPNLTVAENIAFELNLKGyfgwfrkkqlrekaleilnelaftidpdtpvqfLPIAQRQQVAICRALVADARLVI 174
Cdd:cd03213   88 pQDDILHPTLTVRETLMFAAKLRG---------------------------------LSGGERKRVSIALELVSNPSLLF 134
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 175 MDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRL-EEVKEISDRITVIRDGQKI 230
Cdd:cd03213  135 LDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
12-240 3.27e-18

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 85.62  E-value: 3.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSF----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVyaPDDGSKIEIDGKSYH-----RLT 82
Cdd:PRK15093   2 PLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV--TKDNWRVTADRMRFDdidllRLS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  83 PDKAREL---GVQVIYQDlslfPN--LTVAENIAFEL--NLKG--YFG--WFRKKQLREKALEILNELAFTIDPDTPVQF 151
Cdd:PRK15093  80 PRERRKLvghNVSMIFQE----PQscLDPSERVGRQLmqNIPGwtYKGrwWQRFGWRKRRAIELLHRVGIKDHKDAMRSF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 152 ---LPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIR 225
Cdd:PRK15093 156 pyeLTEGECQKVMIAIALANQPRLLIADEPTNAMeptTQAQIFRLLTRLN--QNNNTTILLISHDLQMLSQWADKINVLY 233
                        250
                 ....*....|....*
gi 491046221 226 DGQKIGTWPAEGLTT 240
Cdd:PRK15093 234 CGQTVETAPSKELVT 248
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
11-228 3.38e-18

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 84.46  E-value: 3.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  11 DPLITLRDLSKSF----GGHR-----ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGksyHRL 81
Cdd:PRK15112   2 ETLLEVRNLSKTFryrtGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG-ELLIDD---HPL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  82 T-PDKA-RELGVQVIYQD--LSLFPNLTVAENIAFELNLKGYFgwfrKKQLREKAL-EILNELAFTIDPDT--PVQFLPi 154
Cdd:PRK15112  78 HfGDYSyRSQRIRMIFQDpsTSLNPRQRISQILDFPLRLNTDL----EPEQREKQIiETLRQVGLLPDHASyyPHMLAP- 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 155 AQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGE 227
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
269-488 4.99e-18

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: 82.80  E-value: 4.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRA-GQY---RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKlkNNTDAIKRGIGYV 344
Cdd:cd03265    1 IEVENLVKKyGDFeavRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV--REPREVRRRIGIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 345 SEDrLTLGAILqqSIADNMVIsiLDRLK-TPWHLIDEKQcqDIVQEWIADLDIKvtdpNNALSTLSGGNQQKVVLAKWIL 423
Cdd:cd03265   79 FQD-LSVDDEL--TGWENLYI--HARLYgVPGAERRERI--DELLDFVGLLEAA----DRLVKTYSGGMRRRLEIARSLV 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 424 TRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:cd03265  148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
4-228 9.49e-18

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 86.05  E-value: 9.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   4 TSKADKSDPL-ITLRDLS-KSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGvYAPDDGSkIEIDGKSYHRL 81
Cdd:PRK11174 339 EKELASNDPVtIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGS-LKINGIELREL 416
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  82 TPDKARE----LGvqviyQDLSLFPNlTVAENIAF--------ELNlkgyfgwfrkkQLREKA--LEILNELAFTIDpdT 147
Cdd:PRK11174 417 DPESWRKhlswVG-----QNPQLPHG-TLRDNVLLgnpdasdeQLQ-----------QALENAwvSEFLPLLPQGLD--T 477
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 148 PVQ----FLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKdKGITVVFVSHRLEEVKEIsDRITV 223
Cdd:PRK11174 478 PIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDLAQW-DQIWV 555

                 ....*
gi 491046221 224 IRDGQ 228
Cdd:PRK11174 556 MQDGQ 560
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
12-236 1.31e-17

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 85.93  E-value: 1.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSF----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLI-------KTISGVYAPDDGSKIEIDGKSYHR 80
Cdd:PRK10535   3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMnilgcldKPTSGTYRVAGQDVATLDADALAQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  81 LtpdkaRELGVQVIYQDLSLFPNLTVAENIafelNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQV 160
Cdd:PRK10535  83 L-----RREHFGFIFQRYHLLSHLTAAQNV----EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRV 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 161 AICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRlEEVKEISDRITVIRDGQKIGTWPAE 236
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPPAQ 228
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
2-228 1.42e-17

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 85.46  E-value: 1.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   2 TSTSKADKSDPLITLRDLSKSFGG--HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYH 79
Cdd:PRK11176 330 EGKRVIERAKGDIEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGE-ILLDGHDLR 408
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  80 RLTPDKARElGVQVIYQDLSLFpNLTVAENIAFELNLKgyfgwFRKKQLrEKALEILNELAFtIDP-----DTPV----Q 150
Cdd:PRK11176 409 DYTLASLRN-QVALVSQNVHLF-NDTIANNIAYARTEQ-----YSREQI-EEAARMAYAMDF-INKmdnglDTVIgengV 479
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 151 FLPIAQRQQVAICRALVADARLVIMDEPTASL-TRTEvNQLLSTVNYLKdKGITVVFVSHRLEEVkEISDRITVIRDGQ 228
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALdTESE-RAIQAALDELQ-KNRTSLVIAHRLSTI-EKADEILVVEDGE 555
cbiO PRK13637
energy-coupling factor transporter ATPase;
27-273 1.51e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 82.79  E-value: 1.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSyhrLTPDKA------RELGVQVIYQDLSL 100
Cdd:PRK13637  21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSG-KIIIDGVD---ITDKKVklsdirKKVGLVFQYPEYQL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 101 FPNlTVAENIAFELNLKGYFGWFRKKQLREkALEILNELAFTIDPDTPVQfLPIAQRQQVAICRALVADARLVIMDEPTA 180
Cdd:PRK13637  97 FEE-TIEKDIAFGPINLGLSEEEIENRVKR-AMNIVGLDYEDYKDKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTA 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 181 SLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDGQKI--GTwPAE-----------GLTTRKITEL 246
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCElqGT-PREvfkevetlesiGLAVPQVTYL 252
                        250       260
                 ....*....|....*....|....*..
gi 491046221 247 MTGLdivhERKPPNNAEDRRTVLEIKN 273
Cdd:PRK13637 253 VRKL----RKKGFNIPDDIFTIEEAKE 275
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
281-483 1.57e-17

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


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 80.97  E-value: 1.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKlKNNTDAIKRGIGYV---SEDRLtlgaiLQQ 357
Cdd:cd03225   18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT-KLSLKELRRKVGLVfqnPDDQF-----FGP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 358 SIADNMVISiLDRLKTPWHLIDEKqcqdiVQEWIADLDIKvTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVG 437
Cdd:cd03225   92 TVEEEVAFG-LENLGLPEEEIEER-----VEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 491046221 438 VDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:cd03225  165 LDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
4-220 1.98e-17

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 82.01  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   4 TSKADKSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKT-------ISGVYApdDGsKIEIDGK 76
Cdd:COG1117    2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGARV--EG-EILLDGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  77 S-YHRLTPdkARELGVQV--IYQDLSLFPnLTVAENIAFELNLKGYfgwFRKKQLR---EKALEI----------LNELA 140
Cdd:COG1117   79 DiYDPDVD--VVELRRRVgmVFQKPNPFP-KSIYDNVAYGLRLHGI---KSKSELDeivEESLRKaalwdevkdrLKKSA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 141 FTidpdtpvqfLPIAQRQQVAICRALVADARLVIMDEPTASL----TRTeVNQLLSTvnyLKDKgITVVFVSHRLEEVKE 216
Cdd:COG1117  153 LG---------LSGGQQQRLCIARALAVEPEVLLMDEPTSALdpisTAK-IEELILE---LKKD-YTIVIVTHNMQQAAR 218

                 ....
gi 491046221 217 ISDR 220
Cdd:COG1117  219 VSDY 222
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
14-236 2.02e-17

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: 80.65  E-value: 2.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGV--YAPDDGsKIEIDGKSYHRLTPDKARELGV 91
Cdd:cd03217    1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEG-EILFKGEDITDLPPEERARLGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIYQDLSLFPNLTVAENIAFeLNlKGYFGWFRKKqlrekaleilNElaftidpdtpvqflpiaqrqqvaICRALVADAR 171
Cdd:cd03217   80 FLAFQYPPEIPGVKNADFLRY-VN-EGFSGGEKKR----------NE-----------------------ILQLLLLEPD 124
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHR---LEEVKeiSDRITVIRDGQKIGTWPAE 236
Cdd:cd03217  125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIK--PDRVHVLYDGRIVKSGDKE 190
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
26-228 2.02e-17

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: 81.36  E-value: 2.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  26 HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKS--------YHRLtpdkarelgVQVIYQD 97
Cdd:cd03248   27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGG-QVLLDGKPisqyehkyLHSK---------VSLVGQE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  98 LSLFPNlTVAENIAFELNLKGyFGWFRKKQLREKALEILNELAFTIDPDTPVQ--FLPIAQRQQVAICRALVADARLVIM 175
Cdd:cd03248   97 PVLFAR-SLQDNIAYGLQSCS-FECVKEAAQKAHAHSFISELASGYDTEVGEKgsQLSGGQKQRVAIARALIRNPQVLIL 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 176 DEPTASL---TRTEVNQLLSTVNYLKdkgiTVVFVSHRLEEVkEISDRITVIRDGQ 228
Cdd:cd03248  175 DEATSALdaeSEQQVQQALYDWPERR----TVLVIAHRLSTV-ERADQILVLDGGR 225
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
14-245 5.10e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 80.66  E-value: 5.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIE----IDGKSYH--RLTPDKAR 87
Cdd:PRK14267   5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEgevrLFGRNIYspDVDPIEVR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  88 ElGVQVIYQDLSLFPNLTVAENIAFELNLKGYFGwfRKKQLREKALEILNELAFTID-----PDTPVQfLPIAQRQQVAI 162
Cdd:PRK14267  85 R-EVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVK--SKKELDERVEWALKKAALWDEvkdrlNDYPSN-LSGGQRQRLVI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 163 CRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKgITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPaegltTRK 242
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP-----TRK 234

                 ...
gi 491046221 243 ITE 245
Cdd:PRK14267 235 VFE 237
cbiO PRK13650
energy-coupling factor transporter ATPase;
29-252 6.94e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 80.93  E-value: 6.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGksyHRLTPDKARELGVQV--IYQDL-SLFPNLT 105
Cdd:PRK13650  23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQ-IIIDG---DLLTEENVWDIRHKIgmVFQNPdNQFVGAT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 106 VAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASLTRT 185
Cdd:PRK13650  99 VEDDVAFGLENKG----IPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 186 EVNQLLSTVNYLKDK-GITVVFVSHRLEEVKeISDRITVIRDGQKIGTWPAEGLTTRKITELMTGLDI 252
Cdd:PRK13650 175 GRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNDLLQLGLDI 241
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
17-229 8.75e-17

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: 78.69  E-value: 8.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  17 RDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELgVQVIYQ 96
Cdd:cd03231    4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG-RVLLNGGPLDFQRDSIARGL-LYLGHA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  97 DlSLFPNLTVAENIAFelnlkgyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMD 176
Cdd:cd03231   82 P-GIKTTLSVLENLRF----------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491046221 177 EPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEisDRITVIRDGQK 229
Cdd:cd03231  151 EPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSE--AGARELDLGFK 201
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
281-488 1.01e-16

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: 77.47  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVlglcgllgsgrteLAL--------S-----LFGITHPDSGELFIEGKPVKLKNNTDAIKRGIGYVSEd 347
Cdd:cd03216   17 DGVSLSVRRGEV-------------HALlgengagkStlmkiLSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMVYQ- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 348 rltlgailqqsiadnmvisildrlktpwhlidekqcqdivqewiadldikvtdpnnalstLSGGNQQKVVLAKWILTRPK 427
Cdd:cd03216   83 ------------------------------------------------------------LSVGERQMVEIARALARNAR 102
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 428 VLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:cd03216  103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
12-217 1.07e-16

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 78.76  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRltpDKARELGV 91
Cdd:PRK13539   1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGT-IKLDGGDIDD---PDVAEACH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIYQDlSLFPNLTVAENIAFELNLKGyfgwfrkkQLREKALEILNelAFTIDP--DTPVQFLPIAQRQQVAICRALVAD 169
Cdd:PRK13539  77 YLGHRN-AMKPALTVAENLEFWAAFLG--------GEELDIAAALE--AVGLAPlaHLPFGYLSAGQKRRVALARLLVSN 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHR---LEEVKEI 217
Cdd:PRK13539 146 RPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIplgLPGAREL 196
cbiO PRK13645
energy-coupling factor transporter ATPase;
27-259 2.02e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 79.67  E-value: 2.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEID-----GKSYHRLTPDKARELGVQVIYQDLSLF 101
Cdd:PRK13645  25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipaNLKKIKEVKRLRKEIGLVFQFPEYQLF 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 102 PNlTVAENIAF-ELNLKGyfgwfRKKQLREKALEILNELAFTID--PDTPVQfLPIAQRQQVAICRALVADARLVIMDEP 178
Cdd:PRK13645 105 QE-TIEKDIAFgPVNLGE-----NKQEAYKKVPELLKLVQLPEDyvKRSPFE-LSGGQKRRVALAGIIAMDGNTLVLDEP 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 179 TASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTW-PAEGLTTRkitELMTGLDIvher 256
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGsPFEIFSNQ---ELLTKIEI---- 250

                 ...
gi 491046221 257 KPP 259
Cdd:PRK13645 251 DPP 253
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
266-502 2.13e-16

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: 81.87  E-value: 2.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 266 RTVLEIKNLS---RAGQY---RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPD---SGELFIEGKPVkLKNNTDA 336
Cdd:COG1123    2 TPLLEVRDLSvryPGGDVpavDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL-LELSEAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 337 IKRGIGYVSEDRLTlgAILQQSIADNMVISILDRLKTPwhlideKQCQDIVQEWIADLDIKvTDPNNALSTLSGGNQQKV 416
Cdd:COG1123   81 RGRRIGMVFQDPMT--QLNPVTVGDQIAEALENLGLSR------AEARARVLELLEAVGLE-RRLDRYPHQLSGGQRQRV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 417 VLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG-VGISILLITDEASEAYYNCDRILHMKQGSIVKEIVTDSI- 494
Cdd:COG1123  152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIl 231

                 ....*....
gi 491046221 495 -NEQQLEEI 502
Cdd:COG1123  232 aAPQALAAV 240
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
269-486 2.15e-16

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: 78.53  E-value: 2.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRAG---QYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklkNNTDAIKRGIGYVS 345
Cdd:cd03299    1 LKVENLSKDWkefKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI---TNLPPEKRDISYVP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 346 EDR-LTLGAILQQSIADNMVISILDRLKtpwhlIDEKqcqdiVQEWIADLDIK-VTDPNNAlsTLSGGNQQKVVLAKWIL 423
Cdd:cd03299   78 QNYaLFPHMTVYKNIAYGLKKRKVDKKE-----IERK-----VLEIAEMLGIDhLLNRKPE--TLSGGEQQRVAIARALV 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 424 TRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:cd03299  146 VNPKILLLDEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
28-228 2.27e-16

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: 77.92  E-value: 2.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  28 ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELgVQVIYQDLSLFPNlTVA 107
Cdd:cd03244   19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGS-ILIDGVDISKIGLHDLRSR-ISIIPQDPVLFSG-TIR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 108 ENIAFelnlkgyFGWFRKKQLREkALEI--LNELAFTIDP--DTPVQ----FLPIAQRQQVAICRALVADARLVIMDEPT 179
Cdd:cd03244   96 SNLDP-------FGEYSDEELWQ-ALERvgLKEFVESLPGglDTVVEeggeNLSVGQRQLLCLARALLRKSKILVLDEAT 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491046221 180 ASL---TRTEVNQLLSTvnylKDKGITVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:cd03244  168 ASVdpeTDALIQKTIRE----AFKDCTVLTIAHRLDTIID-SDRILVLDKGR 214
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
280-436 3.33e-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: 75.76  E-value: 3.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  280 YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVkLKNNTDAIKRGIGYVSEDrltLGAILQQSI 359
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL-TDDERKSLRKEIGYVFQD---PQLFPRLTV 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221  360 ADNMVISIldRLKTPWHLIDEKQCQDIvQEWIADLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTV 436
Cdd:pfam00005  77 RENLRLGL--LLKGLSKREKDARAEEA-LEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
29-228 3.55e-16

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 77.51  E-value: 3.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVyapDDGSKIEID--GKSYHRLTPDKAREL---GVQVIYQDLSLFPN 103
Cdd:PRK10584  26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGL---DDGSSGEVSlvGQPLHQMDEEARAKLrakHVGFVFQSFMLIPT 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 104 LTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPD-TPVQfLPIAQRQQVAICRALVADARLVIMDEPTASL 182
Cdd:PRK10584 103 LNALENVELPALLRGE----SSRQSRNGAKALLEQLGLGKRLDhLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 491046221 183 TRT---EVNQLLSTVNylKDKGITVVFVSHRlEEVKEISDRITVIRDGQ 228
Cdd:PRK10584 178 DRQtgdKIADLLFSLN--REHGTTLILVTHD-LQLAARCDRRLRLVNGQ 223
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
12-249 3.67e-16

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 80.87  E-value: 3.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKsfgghRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGV 91
Cdd:PRK15439 267 PVLTVEDLTG-----EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGR-IMLNGKEINALSTAQRLARGL 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 qvIY-----QDLSLFPNLTVAENI-AFELNLKGYfgWFRKKqlREKA-LE----ILNeLAFTiDPDTPVQFLPIAQRQQV 160
Cdd:PRK15439 341 --VYlpedrQSSGLYLDAPLAWNVcALTHNRRGF--WIKPA--RENAvLEryrrALN-IKFN-HAEQAARTLSGGNQQKV 412
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 161 AICRALVADARLVIMDEPTASL---TRTEVNQLLSTVnylKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEG 237
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVdvsARNDIYQLIRSI---AAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAA 489
                        250
                 ....*....|..
gi 491046221 238 LTTRKITELMTG 249
Cdd:PRK15439 490 INVDTIMRLAFG 501
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
29-228 4.24e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 78.17  E-value: 4.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDgSKIEIDGKSYH------RLTPDKARElGVQVIYQDLSLFP 102
Cdd:PRK14246  26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYD-SKIKVDGKVLYfgkdifQIDAIKLRK-EVGMVFQQPNPFP 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 103 NLTVAENIAFELNLKGYFGWFRKKQLREKALEILNELAFTIDP-DTPVQFLPIAQRQQVAICRALVADARLVIMDEPTAS 181
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491046221 182 LTRTEVNQLLSTVNYLKDKgITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGE 229
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
27-246 4.61e-16

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 80.73  E-value: 4.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  27 RALRN-IDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELGVQVIYQD---LSLFP 102
Cdd:PRK11288 266 PGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAG-QVYLDGKPIDIRSPRDAIRAGIMLCPEDrkaEGIIP 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 103 NLTVAENI---AFELNLKgyFGWF-RKKQLREKALEILNELAF-TIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDE 177
Cdd:PRK11288 345 VHSVADNInisARRHHLR--AGCLiNNRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDE 422
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 178 PTASL---TRTEVNQLLstvnY-LKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITEL 246
Cdd:PRK11288 423 PTRGIdvgAKHEIYNVI----YeLAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQATERQALSL 491
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
31-249 5.29e-16

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 80.36  E-value: 5.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  31 NIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEIDGKSYHRLTPDKARELGVQVIYQDLS---LFPNLTVA 107
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKrdgIVPVMGVG 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 108 ENIAFElNLKGYFGWFRKKQLREK--ALEILNELAFTidpdTPVQFLPIAQ-----RQQVAICRALVADARLVIMDEPTA 180
Cdd:PRK13549 360 KNITLA-ALDRFTGGSRIDDAAELktILESIQRLKVK----TASPELAIARlsggnQQKAVLAKCLLLNPKILILDEPTR 434
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 181 SL---TRTEVNQLlstVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMTG 249
Cdd:PRK13549 435 GIdvgAKYEIYKL---INQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNLTQEQVMEAALR 503
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
3-230 5.98e-16

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 80.64  E-value: 5.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   3 STSKADKSDPLITLRDLSKSF--GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHR 80
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGE-ILLNGQPIAD 406
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  81 LTPDKARElGVQVIYQDLSLFpNLTVAENIAFELNLKGyfgwfrkkqlREKALEILN--ELAFTIDPDTPV--------- 149
Cdd:PRK11160 407 YSEAALRQ-AISVVSQRVHLF-SATLRDNLLLAAPNAS----------DEALIEVLQqvGLEKLLEDDKGLnawlgeggr 474
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 150 QfLPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLstVNYLKDKgiTVVFVSHRLEEVKEIsDRITVIRD 226
Cdd:PRK11160 475 Q-LSGGEQRRLGIARALLHDAPLLLLDEPTEGLdaeTERQILELL--AEHAQNK--TVLMITHRLTGLEQF-DRICVMDN 548

                 ....
gi 491046221 227 GQKI 230
Cdd:PRK11160 549 GQII 552
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
269-488 6.80e-16

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 76.70  E-value: 6.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSrAGqY------RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKRGIG 342
Cdd:cd03224    1 LEVENLN-AG-YgksqilFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 343 YVSEDRLTLGailQQSIADN--MVISILDRLKTPWHLidekqcqdivqEWIADL-DIKVTDPNNALSTLSGGNQQKVVLA 419
Cdd:cd03224   79 YVPEGRRIFP---ELTVEENllLGAYARRRAKRKARL-----------ERVYELfPRLKERRKQLAGTLSGGEQQMLAIA 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 420 KWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:cd03224  145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLE 213
cbiO PRK13641
energy-coupling factor transporter ATPase;
27-230 8.00e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 77.95  E-value: 8.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKA-----RELGVQVIYQDLSLF 101
Cdd:PRK13641  21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSG-TITIAGYHITPETGNKNlkklrKKVSLVFQFPEAQLF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 102 PNlTVAENIAF-ELNlkgyFGwFRKKQLREKALEILNELAFTIDPDTPVQF-LPIAQRQQVAICRALVADARLVIMDEPT 179
Cdd:PRK13641 100 EN-TVLKDVEFgPKN----FG-FSEDEAKEKALKWLKKVGLSEDLISKSPFeLSGGQMRRVAIAGVMAYEPEILCLDEPA 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491046221 180 ASL---TRTEVNQLLstVNYLKdKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:PRK13641 174 AGLdpeGRKEMMQLF--KDYQK-AGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
13-234 8.06e-16

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 80.38  E-value: 8.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGK-SYHRLTPDKAREL-- 89
Cdd:PRK11147   3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDG-RIIYEQDlIVARLQQDPPRNVeg 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 --------GVQVI------YQDLSLF-------PNLTVAENIAFELNLKGyfGWfrkkQLREKALEILNELAftIDPDTP 148
Cdd:PRK11147  82 tvydfvaeGIEEQaeylkrYHDISHLvetdpseKNLNELAKLQEQLDHHN--LW----QLENRINEVLAQLG--LDPDAA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 149 VQFLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLlstVNYLKDKGITVVFVSHRLEEVKEISDRItVIRDGQ 228
Cdd:PRK11147 154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWL---EGFLKTFQGSIIFISHDRSFIRNMATRI-VDLDRG 229

                 ....*.
gi 491046221 229 KIGTWP 234
Cdd:PRK11147 230 KLVSYP 235
cbiO PRK13644
energy-coupling factor transporter ATPase;
13-228 9.48e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 77.33  E-value: 9.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKI--EIDGKSYHRLtpDKAREL 89
Cdd:PRK13644   1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsGIDTGDFSKL--QGIRKL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 gVQVIYQD-LSLFPNLTVAENIAF-ELNLkgyfgWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALV 167
Cdd:PRK13644  79 -VGIVFQNpETQFVGRTVEEDLAFgPENL-----CLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 168 ADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVkEISDRITVIRDGQ 228
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGK 212
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
12-243 1.07e-15

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 77.00  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDdgSKIEIDGKS-------YHRLTPD 84
Cdd:PRK14258   6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE--SEVRVEGRVeffnqniYERRVNL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  85 KARELGVQVIYQDLSLFPnLTVAENIAFELNLkgyFGWFRKKQLRE------KALEILNELAFTIDPDTpvQFLPIAQRQ 158
Cdd:PRK14258  84 NRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKI---VGWRPKLEIDDivesalKDADLWDEIKHKIHKSA--LDLSGGQQQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 159 QVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKG-ITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEG 237
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEF 237

                 ....*.
gi 491046221 238 LTTRKI 243
Cdd:PRK14258 238 GLTKKI 243
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
10-223 1.18e-15

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 78.08  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKS-------FGGHR---ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYh 79
Cdd:PRK11308   2 QQPLLQAIDLKKHypvkrglFKPERlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGE-LYYQGQDL- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  80 rLTPD----KARELGVQVIYQD--LSLFPNLTV----AENIAFELNLKgyfgwfrKKQLREKALEILNELAftIDPD--- 146
Cdd:PRK11308  80 -LKADpeaqKLLRQKIQIVFQNpyGSLNPRKKVgqilEEPLLINTSLS-------AAERREKALAMMAKVG--LRPEhyd 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 147 -TPVQFlPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRIT 222
Cdd:PRK11308 150 rYPHMF-SGGQRQRIAIARALMLDPDVVVADEPVSALdvsVQAQVLNLMMDLQ--QELGLSYVFISHDLSVVEHIADEVM 226

                 .
gi 491046221 223 V 223
Cdd:PRK11308 227 V 227
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
14-228 1.48e-15

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 79.60  E-value: 1.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   14 ITLRDLSksFGGHRA----LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKAREl 89
Cdd:TIGR03796 478 VELRNIT--FGYSPLepplIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSG-EILFDGIPREEIPREVLAN- 553
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   90 GVQVIYQDLSLFPNlTVAENIAFelnlkgyfgWFRkkQLREKALE-------ILNE-LAFTIDPDTPV----QFLPIAQR 157
Cdd:TIGR03796 554 SVAMVDQDIFLFEG-TVRDNLTL---------WDP--TIPDADLVrackdaaIHDViTSRPGGYDAELaeggANLSGGQR 621
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221  158 QQVAICRALVADARLVIMDEPTASL-TRTEvnqlLSTVNYLKDKGITVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:TIGR03796 622 QRLEIARALVRNPSILILDEATSALdPETE----KIIDDNLRRRGCTCIIVAHRLSTIRD-CDEIIVLERGK 688
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
29-210 1.61e-15

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 74.99  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYhrltpDKARelgvqVIYQDLSLF------- 101
Cdd:PRK13540  17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKG-EILFERQSI-----KKDL-----CTYQKQLCFvghrsgi 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 102 -PNLTVAENIAFELNlkgyfgwFRKKQLREKALEILNELAFTIDpdTPVQFLPIAQRQQVAICRALVADARLVIMDEPTA 180
Cdd:PRK13540  86 nPYLTLRENCLYDIH-------FSPGAVGITELCRLFSLEHLID--YPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
                        170       180       190
                 ....*....|....*....|....*....|
gi 491046221 181 SLTRTEVNQLLSTVNYLKDKGITVVFVSHR 210
Cdd:PRK13540 157 ALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
28-252 1.63e-15

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 76.66  E-value: 1.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  28 ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKsyhrltpDKARELGVQVIYQDLSL-FPN--- 103
Cdd:PRK13633  25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEG-KVYVDGL-------DTSDEENLWDIRNKAGMvFQNpdn 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 104 ----LTVAENIAF-ELNLKgyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEP 178
Cdd:PRK13633  97 qivaTIVEEDVAFgPENLG-----IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEP 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 179 TASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEiSDRITVIRDGQKIgtwpAEGlTTRKI---TELMT--GLDI 252
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVV----MEG-TPKEIfkeVEMMKkiGLDV 245
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
9-238 1.68e-15

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 76.73  E-value: 1.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   9 KSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGK-----SYHRLTP 83
Cdd:PRK11831   3 SVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHG-EILFDGEnipamSRSRLYT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  84 DKARelgVQVIYQDLSLFPNLTVAENIAFELNlkgyfgwfRKKQLREKALE--ILNELAfTIDPDTPVQFLP------IA 155
Cdd:PRK11831  82 VRKR---MSMLFQSGALFTDMNVFDNVAYPLR--------EHTQLPAPLLHstVMMKLE-AVGLRGAAKLMPselsggMA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 156 QRqqVAICRALVADARLVIMDEPTAS---LTRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGT 232
Cdd:PRK11831 150 RR--AALARAIALEPDLIMFDEPFVGqdpITMGVLVKLISELN--SALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAH 225

                 ....*.
gi 491046221 233 WPAEGL 238
Cdd:PRK11831 226 GSAQAL 231
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
13-230 1.83e-15

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 78.85  E-value: 1.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFGGHR-ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARElGV 91
Cdd:PRK13657 334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGR-ILIDGTDIRTVTRASLRR-NI 411
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIYQDLSLFpNLTVAENI------AFELNLkgyfgwfRKKQLREKALEIL--NELAFtidpDTPV----QFLPIAQRQQ 159
Cdd:PRK13657 412 AVVFQDAGLF-NRSIEDNIrvgrpdATDEEM-------RAAAERAQAHDFIerKPDGY----DTVVgergRQLSGGERQR 479
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 160 VAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylkdKGITVVFVSHRLEEVKEiSDRITVIRDGQKI 230
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALdveTEAKVKAALDELM----KGRTTFIIAHRLSTVRN-ADRILVFDNGRVV 548
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
34-227 3.33e-15

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


Pssm-ID: 163483 [Multi-domain]  Cd Length: 223  Bit Score: 74.89  E-value: 3.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   34 LTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSyhrlTPDKARELGVQVIYQDLSL-FPnLTVAENIaf 112
Cdd:TIGR03771   1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGT-VKVAGAS----PGKGWRHIGYVPQRHEFAWdFP-ISVAHTV-- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  113 eLNLK-GYFGWFRKKQLRE-----KALEI--LNELAftidpDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASLTR 184
Cdd:TIGR03771  73 -MSGRtGHIGWLRRPCVADfaavrDALRRvgLTELA-----DRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDM 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 491046221  185 TEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRI-----TVIRDG 227
Cdd:TIGR03771 147 PTQELLTELFIELAGAGTAILMTTHDLAQAMATCDRVvllngRVIADG 194
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
14-228 4.32e-15

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 77.84  E-value: 4.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARElGVQ 92
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEG-EIRLDGRPLSSLSHSVLRQ-GVA 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  93 VIYQDL-----SLFPNLTVAENIAFELNlkgyfgWfrkkqlreKALEI--LNELAFTIdPD---TPV----QFLPIAQRQ 158
Cdd:PRK10790 419 MVQQDPvvladTFLANVTLGRDISEEQV------W--------QALETvqLAELARSL-PDglyTPLgeqgNNLSVGQKQ 483
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 159 QVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylkdKGITVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIdsgTEQAIQQALAAVR----EHTTLVVIAHRLSTIVE-ADTILVLHRGQ 551
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
13-231 4.70e-15

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 75.22  E-value: 4.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFGGHR-ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSyhrLTPDKARELG- 90
Cdd:PRK13652   3 LIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSG-SVLIRGEP---ITKENIREVRk 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  91 -VQVIYQ--DLSLFpNLTVAENIAF-ELNLKgyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRAL 166
Cdd:PRK13652  79 fVGLVFQnpDDQIF-SPTVEQDIAFgPINLG-----LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVI 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 167 VADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIG 231
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
12-228 4.83e-15

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: 78.52  E-value: 4.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221    12 PLITLRDLSKSF--GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYhrltpdkarEL 89
Cdd:TIGR01257  927 PGVCVKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGT-VLVGGKDI---------ET 996
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221    90 GVQVIYQDLS-------LFPNLTVAENIAFELNLKGYfGWfRKKQLREKALeiLNELAFTIDPDTPVQFLPIAQRQQVAI 162
Cdd:TIGR01257  997 NLDAVRQSLGmcpqhniLFHHLTVAEHILFYAQLKGR-SW-EEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSV 1072
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   163 CRALVADARLVIMDEPTASL---TRTEVNQLLstvnyLKDK-GITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:TIGR01257 1073 AIAFVGDAKVVVLDEPTSGVdpySRRSIWDLL-----LKYRsGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
10-205 7.74e-15

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 73.34  E-value: 7.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKsyHRLTPDKAREl 89
Cdd:PRK13543   8 APPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESG-QIQIDGK--TATRGDRSRF- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 gVQVIYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEIlneLAFTIDPDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:PRK13543  84 -MAYLGHLPGLKADLSTLENLHFLCGLHGR----RAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSP 155
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491046221 170 ARLVIMDEPTASLTR---TEVNQLLSTvnYLKDKGITVV 205
Cdd:PRK13543 156 APLWLLDEPYANLDLegiTLVNRMISA--HLRGGGAALV 192
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
14-228 9.51e-15

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: 71.33  E-value: 9.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkieidgksyhrltpdkarelgvqv 93
Cdd:cd03221    1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI------------------------ 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 iyqdLSLFPNLTVaeniafelnlkGYFgwfrkKQLR--EKAleilnelaftidpdtpvqflpiaqrqQVAICRALVADAR 171
Cdd:cd03221   57 ----VTWGSTVKI-----------GYF-----EQLSggEKM--------------------------RLALAKLLLENPN 90
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 172 LVIMDEPTASLTRTEVNQLlstVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03221   91 LLLLDEPTNHLDLESIEAL---EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
cbiO PRK13643
energy-coupling factor transporter ATPase;
27-230 1.05e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 74.77  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS----KIEIDGKSYHRLTPDKARELGVQVIYQDLSLFP 102
Cdd:PRK13643  20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKvtvgDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 103 NlTVAENIAFElnlKGYFGwFRKKQLREKALEILNELAFTID--PDTPVQfLPIAQRQQVAICRALVADARLVIMDEPTA 180
Cdd:PRK13643 100 E-TVLKDVAFG---PQNFG-IPKEKAEKIAAEKLEMVGLADEfwEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491046221 181 SL---TRTEVNQLLSTVNylkDKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:PRK13643 174 GLdpkARIEMMQLFESIH---QSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
281-488 1.31e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 74.11  E-value: 1.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPV--------KLKNNTdaikrGIGYVSEDRLTLG 352
Cdd:PRK13636  23 KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrkglmKLRESV-----GMVFQDPDNQLFS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 353 AILQQSIADNMVisildRLKTPWHLIDEKQCQDIVQEWIADLDIKVTdpnnalSTLSGGNQQKVVLAKWILTRPKVLILD 432
Cdd:PRK13636  98 ASVYQDVSFGAV-----NLKLPEDEVRKRVDNALKRTGIEHLKDKPT------HCLSFGQKKRVAIAGVLVMEPKVLVLD 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 433 SPTVGVDIGAKDSIYKLIHRLS-GVGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:PRK13636 167 EPTAGLDPMGVSEIMKLLVEMQkELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
269-488 1.53e-14

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: 72.92  E-value: 1.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNL--SRAGQ--YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPV-KLKNNTD-AIKRGIG 342
Cdd:cd03261    1 IELRGLtkSFGGRtvLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsGLSEAELyRLRRRMG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 343 YVSEDrltlGAILQQ-SIADNMVISILDRLKTPwhlidEKQCQDIVQEWIADLDIKVTD---PnnalSTLSGGNQQKVVL 418
Cdd:cd03261   81 MLFQS----GALFDSlTVFENVAFPLREHTRLS-----EEEIREIVLEKLEAVGLRGAEdlyP----AELSGGMKKRVAL 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 419 AKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGV-GISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:cd03261  148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
19-250 1.64e-14

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 73.48  E-value: 1.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  19 LSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRL-TPDKARELGvqVIYQD 97
Cdd:PRK10253  13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGH-VWLDGEHIQHYaSKEVARRIG--LLAQN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  98 LSLFPNLTVAENIAF-ELNLKGYFGWFRKKQlREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMD 176
Cdd:PRK10253  90 ATTPGDITVQELVARgRYPHQPLFTRWRKED-EEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 177 EPTASLT---RTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMTGL 250
Cdd:PRK10253 169 EPTTWLDishQIDLLELLSELN--REKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGL 243
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
1-487 1.67e-14

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 76.05  E-value: 1.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   1 MTSTSKADKSDPLiTLRDLSKSFGGHR----ALRNIDLTLNKGEVHCLAGTNGCGKST-------LIKTISGVYAPD--- 66
Cdd:PRK10261   1 MPHSDELDARDVL-AVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDkml 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  67 ----DGSKIEIDGKSYHRLTpdKARELGVQVIYQD--LSLFPNLTVAENIAFELNLKGYFGwfRKKQLREkALEILNEL- 139
Cdd:PRK10261  80 lrrrSRQVIELSEQSAAQMR--HVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGAS--REEAMVE-AKRMLDQVr 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 140 ---AFTIDPDTPVQfLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVK 215
Cdd:PRK10261 155 ipeAQTILSRYPHQ-LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 216 EISDRITVIRDGQKIGTWPAEGL-------TTRKITEL------MTGLDIVH----------ERKPPNNAEDR----RTV 268
Cdd:PRK10261 234 EIADRVLVMYQGEAVETGSVEQIfhapqhpYTRALLAAvpqlgaMKGLDYPRrfplislehpAKQEPPIEQDTvvdgEPI 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS-----RAGQY----------RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNN 333
Cdd:PRK10261 314 LQVRNLVtrfplRSGLLnrvtrevhavEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 334 T--DAIKRGIGYVSED-------RLTLGailqqsiadnmvISILDRLKTpwH-LIDEKQCQDIVQEWIADLDIKvtdPNN 403
Cdd:PRK10261 394 GklQALRRDIQFIFQDpyasldpRQTVG------------DSIMEPLRV--HgLLPGKAAAARVAWLLERVGLL---PEH 456
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 404 ALS---TLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS-GVGISILLITDEASEAYYNCDRILH 479
Cdd:PRK10261 457 AWRyphEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAV 536

                 ....*...
gi 491046221 480 MKQGSIVK 487
Cdd:PRK10261 537 MYLGQIVE 544
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
408-483 1.80e-14

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: 70.74  E-value: 1.80e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:cd00267   81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
8-227 2.66e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 72.86  E-value: 2.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   8 DKSDPLITLRDLSKSFGGHRA--LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEIDgksyHRLTPDK 85
Cdd:PRK13648   2 EDKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN----QAITDDN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  86 AREL--GVQVIYQDL-SLFPNLTVAENIAFEL--NLKGYfgwfrkKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQV 160
Cdd:PRK13648  78 FEKLrkHIGIVFQNPdNQFVGSIVKYDVAFGLenHAVPY------DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRV 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 161 AICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLK-DKGITVVFVSHRLEEVKEiSDRITVIRDG 227
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKG 218
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
14-230 3.26e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 73.20  E-value: 3.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGH-----RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS------------------- 69
Cdd:PRK13651   3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewifkdeknkkktkekek 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  70 ---KIEIDGKSYHRLTPDKA--RELGVQVIYQDLSLFPNlTVAENIAFELNLKGyfgwFRKKQLREKALEILnELAftid 144
Cdd:PRK13651  83 vleKLVIQKTRFKKIKKIKEirRRVGVVFQFAEYQLFEQ-TIEKDIIFGPVSMG----VSKEEAKKRAAKYI-ELV---- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 145 pDTPVQFLPIA-------QRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEI 217
Cdd:PRK13651 153 -GLDESYLQRSpfelsggQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEW 231
                        250
                 ....*....|...
gi 491046221 218 SDRITVIRDGQKI 230
Cdd:PRK13651 232 TKRTIFFKDGKII 244
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
269-486 4.13e-14

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


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 71.88  E-value: 4.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRA-GQYR---DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklkNNTDAIKRGIGYV 344
Cdd:cd03300    1 IELENVSKFyGGFValdGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI---TNLPPHKRPVNTV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 345 SEDRltlgAILQQ-SIADNMVISiLDRLKTPWHLIDEK--QCQDIVQ-EWIADLDIkvtdpnnalSTLSGGNQQKVVLAK 420
Cdd:cd03300   78 FQNY----ALFPHlTVFENIAFG-LRLKKLPKAEIKERvaEALDLVQlEGYANRKP---------SQLSGGQQQRVAIAR 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 421 WILTRPKVLILDSPTVGVDIGAKDSI---YKLIHRlsGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:cd03300  144 ALVNEPKVLLLDEPLGALDLKLRKDMqleLKRLQK--ELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
268-486 4.71e-14

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 72.83  E-value: 4.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 268 VLEIKNLSRagQY------RDINLNLKRGEVlglcgllgsgrteLAL---------SLF----GITHPDSGELFIEGKPV 328
Cdd:COG4152    1 MLELKGLTK--RFgdktavDDVSFTVPKGEI-------------FGLlgpngagktTTIriilGILAPDSGEVLWDGEPL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 329 klknnTDAIKRGIGYVSEDRltlGAILQQSIADNMVisILDRLktpwHLIDEKQCQDIVQEWIADLDIKvtD-PNNALST 407
Cdd:COG4152   66 -----DPEDRRRIGYLPEER---GLYPKMKVGEQLV--YLARL----KGLSKAEAKRRADEWLERLGLG--DrANKKVEE 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLIT---DEASEAyynCDRILHMKQGS 484
Cdd:COG4152  130 LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSShqmELVEEL---CDRIVIINKGR 206

                 ..
gi 491046221 485 IV 486
Cdd:COG4152  207 KV 208
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
13-236 5.71e-14

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 72.85  E-value: 5.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFGGH----RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISG-------VYApddgSKIEIDGKSYHRL 81
Cdd:PRK11022   3 LLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidypgrVMA----EKLEFNGQDLQRI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  82 TPDKAREL---GVQVIYQD--LSLFPNLTVAENI--AFELNLKGyfgwfRKKQLREKALEILNELAFTiDPDTPVQFLP- 153
Cdd:PRK11022  79 SEKERRNLvgaEVAMIFQDpmTSLNPCYTVGFQImeAIKVHQGG-----NKKTRRQRAIDLLNQVGIP-DPASRLDVYPh 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 154 -----IAQRqqVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDG 227
Cdd:PRK11022 153 qlsggMSQR--VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAG 230

                 ....*....
gi 491046221 228 QKIGTWPAE 236
Cdd:PRK11022 231 QVVETGKAH 239
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
18-228 6.57e-14

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 72.98  E-value: 6.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  18 DLSKSFGGHRAlrNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDG-----SKIEIDGKSYHRLTPDKARelgVQ 92
Cdd:PRK11144   5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGrivlnGRVLFDAEKGICLPPEKRR---IG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  93 VIYQDLSLFPNLTVAENIAFELnlkgyfgwfrKKQLREKALEILNELAftIDPdtPVQFLPIA----QRQQVAICRALVA 168
Cdd:PRK11144  80 YVFQDARLFPHYKVRGNLRYGM----------AKSMVAQFDKIVALLG--IEP--LLDRYPGSlsggEKQRVAIGRALLT 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 169 DARLVIMDEPTASLTRTEVNQLLstvNYL----KDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK11144 146 APELLLMDEPLASLDLPRKRELL---PYLerlaREINIPILYVSHSLDEILRLADRVVVLEQGK 206
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
4-219 6.92e-14

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 71.74  E-value: 6.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   4 TSKADKSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKT-------ISGVYApdDGsKIEIDGK 76
Cdd:PRK14243   1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGFRV--EG-KVTFHGK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  77 SYH--RLTPDKARELgVQVIYQDLSLFPNlTVAENIAFELNLKGYFG---WFRKKQLREKAL--EILNELaftidpDTPV 149
Cdd:PRK14243  78 NLYapDVDPVEVRRR-IGMVFQKPNPFPK-SIYDNIAYGARINGYKGdmdELVERSLRQAALwdEVKDKL------KQSG 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 150 QFLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKgITVVFVSHRLEEVKEISD 219
Cdd:PRK14243 150 LSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
ycf16 CHL00131
sulfate ABC transporter protein; Validated
8-236 7.00e-14

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 71.60  E-value: 7.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   8 DKSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISG--VYAPDDGsKIEIDGKSYHRLTPDK 85
Cdd:CHL00131   2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEG-DILFKGESILDLEPEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  86 ARELGVQVIYQDLSLFPNLTVAENIAFELNLKgyfgwfRKKQLREKA-----LEILNELAFTIDPDTpvQFLPI------ 154
Cdd:CHL00131  81 RAHLGIFLAFQYPIEIPGVSNADFLRLAYNSK------RKFQGLPELdplefLEIINEKLKLVGMDP--SFLSRnvnegf 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 155 --AQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSH--RLEEVKeISDRITVIRDGQKI 230
Cdd:CHL00131 153 sgGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqRLLDYI-KPDYVHVMQNGKII 231

                 ....*.
gi 491046221 231 GTWPAE 236
Cdd:CHL00131 232 KTGDAE 237
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
269-483 8.31e-14

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: 69.52  E-value: 8.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS-RAGQY---RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPV-KLKNNTDAIKRGIGY 343
Cdd:cd03229    1 LELKNVSkRYGQKtvlNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtDLEDELPPLRRRIGM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 344 VsedrltlgailqqsIADNMVISILDRLktpwhlidekqcqdivqewiadldikvtdpNNALSTLSGGNQQKVVLAKWIL 423
Cdd:cd03229   81 V--------------FQDFALFPHLTVL------------------------------ENIALGLSGGQQQRVALARALA 116
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 424 TRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:cd03229  117 MDPDVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
cbiO PRK13642
energy-coupling factor transporter ATPase;
29-252 1.08e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 71.28  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKsyhRLTPDKAREL--GVQVIYQDL-SLFPNLT 105
Cdd:PRK13642  23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGK-VKIDGE---LLTAENVWNLrrKIGMVFQNPdNQFVGAT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 106 VAENIAFELNLKGYFgwfRKKQLR--EKALEILNELAF-TIDPDTpvqfLPIAQRQQVAICRALVADARLVIMDEPTASL 182
Cdd:PRK13642  99 VEDDVAFGMENQGIP---REEMIKrvDEALLAVNMLDFkTREPAR----LSGGQKQRVAVAGIIALRPEIIILDESTSML 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 183 TRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEiSDRITVIRDGQKIGTWPAEGLTTRKITELMTGLDI 252
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDV 241
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
27-232 1.35e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 71.20  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEI------DGKSYHRLTPDKARelgVQVIYQdlsl 100
Cdd:PRK13634  21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSG-TVTIgervitAGKKNKKLKPLRKK---VGIVFQ---- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 101 FPNL-----TVAENIAF-ELNlkgyFGwFRKKQLREKALEILNELAFTIDPDTPVQF-LPIAQRQQVAICRALVADARLV 173
Cdd:PRK13634  93 FPEHqlfeeTVEKDICFgPMN----FG-VSEEDAKQKAREMIELVGLPEELLARSPFeLSGGQMRRVAIAGVLAMEPEVL 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 174 IMDEPTASLT---RTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ--KIGT 232
Cdd:PRK13634 168 VLDEPTAGLDpkgRKEMMEMFYKLH--KEKGLTTVLVTHSMEDAARYADQIVVMHKGTvfLQGT 229
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
269-486 1.60e-13

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: 69.84  E-value: 1.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS----RAGQY--RDINLNLKRGEVlglcgllgsgrteLAL---------SLF----GITHPDSGELFIEGKPVK 329
Cdd:cd03263    1 LQIRNLTktykKGTKPavDDLSLNVYKGEI-------------FGLlghngagktTTLkmltGELRPTSGTAYINGYSIR 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 330 lkNNTDAIKRGIGYVSEDRltlgailqqsiadnmvisILDRLKTPW-HL--------IDEKQCQDIVQEWIADLDIkvTD 400
Cdd:cd03263   68 --TDRKAARQSLGYCPQFD------------------ALFDELTVReHLrfyarlkgLPKSEIKEEVELLLRVLGL--TD 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 401 PNNAL-STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGvGISILLITDEASEAYYNCDRILH 479
Cdd:cd03263  126 KANKRaRTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAI 204

                 ....*..
gi 491046221 480 MKQGSIV 486
Cdd:cd03263  205 MSDGKLR 211
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
16-228 1.65e-13

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 70.10  E-value: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  16 LRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISG--VYAPDDGSkIEIDGKSYHRLTPDK-AReLGVQ 92
Cdd:COG0396    3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGS-ILLDGEDILELSPDErAR-AGIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  93 VIYQDLSLFPNLTV------AENIAFELNLKGYFgwFRKKqLREKaLEILNelaftIDPDtpvqFL-------------- 152
Cdd:COG0396   81 LAFQYPVEIPGVSVsnflrtALNARRGEELSARE--FLKL-LKEK-MKELG-----LDED----FLdryvnegfsggekk 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 153 --PIAQrqqvaicrALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSH--R-LEEVKeiSDRITVIRDG 227
Cdd:COG0396  148 rnEILQ--------MLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHyqRiLDYIK--PDFVHVLVDG 217

                 .
gi 491046221 228 Q 228
Cdd:COG0396  218 R 218
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
14-228 1.78e-13

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 72.70  E-value: 1.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHR-ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELgVQ 92
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSG-EILLDGKPVTAEQPEDYRKL-FS 400
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  93 VIYQDLSLFPNLTVAENiaFELNLKGYFGWFRKKQLREKaLEILNELAFTIDpdtpvqfLPIAQRQQVAICRALVADARL 172
Cdd:PRK10522 401 AVFTDFHLFDQLLGPEG--KPANPALVEKWLERLKMAHK-LELEDGRISNLK-------LSKGQKKRLALLLALAEERDI 470
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 173 VIMDEPTASLT---RTEVNQLLstVNYLKDKGITVVFVSHRlEEVKEISDRITVIRDGQ 228
Cdd:PRK10522 471 LLLDEWAADQDphfRREFYQVL--LPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
12-221 1.81e-13

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 70.14  E-value: 1.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKarelgv 91
Cdd:PRK09544   3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-VIKRNGKLRIGYVPQK------ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 qvIYQDLSLfpNLTVAENIAFELNLKgyfgwfrkkqlREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADAR 171
Cdd:PRK09544  76 --LYLDTTL--PLTVNRFLRLRPGTK-----------KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491046221 172 LVIMDEPTASLtrtEVN---QLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRI 221
Cdd:PRK09544 141 LLVLDEPTQGV---DVNgqvALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
316-494 2.11e-13

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: 69.52  E-value: 2.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 316 PDSGELFIEGKPVKLKNNTdaikrgigyVSEDRLTLGAILQQ------SIADNmvISILDRLktpwHLIDEKQCQDIVQE 389
Cdd:cd03260   57 PDEGEVLLDGKDIYDLDVD---------VLELRRRVGMVFQKpnpfpgSIYDN--VAYGLRL----HGIKLKEELDERVE 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 390 W---IADLDIKVTDPNNALStLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVgISILLITDE 466
Cdd:cd03260  122 EalrKAALWDEVKDRLHALG-LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHN 199
                        170       180
                 ....*....|....*....|....*...
gi 491046221 467 ASEAYYNCDRILHMKQGSIVKEIVTDSI 494
Cdd:cd03260  200 MQQAARVADRTAFLLNGRLVEFGPTEQI 227
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
269-485 2.42e-13

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: 69.68  E-value: 2.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS-RAGQYR---DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklkNNTDAIKRGIGYV 344
Cdd:cd03296    3 IEVRNVSkRFGDFValdDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQERNVGFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 345 SEDRltlgAILQQ-SIADNMVISILDR---LKTPWHLIDEK--QCQDIVQ-EWIADldikvTDPNNalstLSGGNQQKVV 417
Cdd:cd03296   80 FQHY----ALFRHmTVFDNVAFGLRVKprsERPPEAEIRAKvhELLKLVQlDWLAD-----RYPAQ----LSGGQRQRVA 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 418 LAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSI 485
Cdd:cd03296  147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
281-494 3.48e-13

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: 69.11  E-value: 3.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKRGIGYVSED-----RLTlgail 355
Cdd:cd03218   17 NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQEasifrKLT----- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 356 qqsIADNmVISILDRLKtpwhlIDEKQCQDIVQEWIADLDIKVTDPNNAlSTLSGGNQQKVVLAKWILTRPKVLILDSPT 435
Cdd:cd03218   92 ---VEEN-ILAVLEIRG-----LSKKEREEKLEELLEEFHITHLRKSKA-SSLSGGERRRVEIARALATNPKFLLLDEPF 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 436 VGVDIGAKDSIYKLIHRLSGVGISIlLITDE-ASEAYYNCDRILHMKQGSIVKEIVTDSI 494
Cdd:cd03218  162 AGVDPIAVQDIQKIIKILKDRGIGV-LITDHnVRETLSITDRAYIIYEGKVLAEGTPEEI 220
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
13-228 5.09e-13

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 67.91  E-value: 5.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL--- 89
Cdd:PRK13538   1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGE-VLWQGEPIRRQRDEYHQDLlyl 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 ----GVQviyqdlslfPNLTVAENIAFELNLKGYFGwfrkkqlREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRA 165
Cdd:PRK13538  80 ghqpGIK---------TELTALENLRFYQRLHGPGD-------DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARL 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 166 LVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRleEVKEISDRITVIRDGQ 228
Cdd:PRK13538 144 WLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQ--DLPVASDKVRKLRLGQ 204
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
14-228 5.43e-13

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: 67.82  E-value: 5.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGH--RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARElGV 91
Cdd:cd03369    7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEG-KIEIDGIDISTIPLEDLRS-SL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIYQDLSLFPNlTVAENIafelnlkGYFGWFRKKQLREkALEI----LNelaftidpdtpvqfLPIAQRQQVAICRALV 167
Cdd:cd03369   85 TIIPQDPTLFSG-TIRSNL-------DPFDEYSDEEIYG-ALRVseggLN--------------LSQGQRQLLCLARALL 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 168 ADARLVIMDEPTASLTrTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEIsDRITVIRDGQ 228
Cdd:cd03369  142 KRPRVLVLDEATASID-YATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGE 200
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
268-497 5.58e-13

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 68.77  E-value: 5.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 268 VLEIKNLSRAGQYR----DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKRGIGY 343
Cdd:PRK10895   3 TLTAKNLAKAYKGRrvveDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 344 VSEDrltlGAILQQ-SIADNM--VISILDRLKTpwhlideKQCQDIVQEWIADLDIKVTDpNNALSTLSGGNQQKVVLAK 420
Cdd:PRK10895  83 LPQE----ASIFRRlSVYDNLmaVLQIRDDLSA-------EQREDRANELMEEFHIEHLR-DSMGQSLSGGERRRVEIAR 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 421 WILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKEIVTDSI--NEQ 497
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIlqDEH 229
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
28-228 5.73e-13

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 69.07  E-value: 5.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  28 ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKsyhrltpdkarelgVQVIYQDLSLFPNLTVA 107
Cdd:PRK13546  39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG-KVDRNGE--------------VSVIAISAGLSGQLTGI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 108 ENIAFELNLKGyfgwFRKKQLREKALEIL--NELAFTIdpDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASLTRT 185
Cdd:PRK13546 104 ENIEFKMLCMG----FKRKEIKAMTPKIIefSELGEFI--YQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 491046221 186 EVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGK 220
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
2-238 7.95e-13

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 68.97  E-value: 7.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   2 TSTSKADKSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEID----GKS 77
Cdd:PRK14271  10 SGAADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDvllgGRS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  78 Y--HRLTPDKARELGVqvIYQDLSLFPnLTVAENI-----AFELNLKGYFGWFRKKQLREKAL--EILNELAftidpDTP 148
Cdd:PRK14271  90 IfnYRDVLEFRRRVGM--LFQRPNPFP-MSIMDNVlagvrAHKLVPRKEFRGVAQARLTEVGLwdAVKDRLS-----DSP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 149 VQfLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKgITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK14271 162 FR-LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGR 239
                        250
                 ....*....|
gi 491046221 229 KIGTWPAEGL 238
Cdd:PRK14271 240 LVEEGPTEQL 249
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
10-250 9.35e-13

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 68.28  E-value: 9.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTIsGVYAPDDGSKIEIDGKSyhrLTPDKAREL 89
Cdd:PRK10575   8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAQP---LESWSSKAF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 GVQVIY--QDLSLFPNLTVAENIAF-ELNLKGYFGWFRKKQlREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRAL 166
Cdd:PRK10575  84 ARKVAYlpQQLPAAEGMTVRELVAIgRYPWHGALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 167 VADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITE 245
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLE 242

                 ....*
gi 491046221 246 LMTGL 250
Cdd:PRK10575 243 QIYGI 247
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
26-439 1.03e-12

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 70.04  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  26 HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKiEIDGKSYHRLTPDKARELgVQVIYQD-----LSL 100
Cdd:PRK10938  16 TKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER-QSQFSHITRLSFEQLQKL-VSDEWQRnntdmLSP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 101 FPN---LTVAENIafelnlkgyfgwfrkkQLREKALEILNELA--FTIDP--DTPVQFLPIAQRQQVAICRALVADARLV 173
Cdd:PRK10938  94 GEDdtgRTTAEII----------------QDEVKDPARCEQLAqqFGITAllDRRFKYLSTGETRKTLLCQALMSEPDLL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 174 IMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKI------TELM 247
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALvaqlahSEQL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 248 TGLDI-------VHERKPPNNAedrRTVLeiknlsRAG--QYRD------INLNLKRGEVLGLCGLLGSGRTELaLSLFG 312
Cdd:PRK10938 238 EGVQLpepdepsARHALPANEP---RIVL------NNGvvSYNDrpilhnLSWQVNPGEHWQIVGPNGAGKSTL-LSLIT 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 313 ITHPD--SGELFIEGKPVKLKNNTDAIKRGIGYVSeDRLTLGAILQQSIADNMVISILDRLKTpWHLIDEKQcQDIVQEW 390
Cdd:PRK10938 308 GDHPQgySNDLTLFGRRRGSGETIWDIKKHIGYVS-SSLHLDYRVSTSVRNVILSGFFDSIGI-YQAVSDRQ-QKLAQQW 384
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 491046221 391 IADLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVD 439
Cdd:PRK10938 385 LDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
270-488 1.24e-12

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: 66.30  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 270 EIKNLS-RAGQY---RDINLNLKRGEVlglcgllgsgrteLAL-------------SLFGITHPDSGELFIEGKPVKLKN 332
Cdd:cd03214    1 EVENLSvGYGGRtvlDDLSLSIEAGEI-------------VGIlgpngagkstllkTLAGLLKPSSGEILLDGKDLASLS 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 333 NTDAIKRgIGYVSEdrltlgailqqsiadnmvisILDRLKTpWHLIDEKqcqdivqewiadldikvtdpnnaLSTLSGGN 412
Cdd:cd03214   68 PKELARK-IAYVPQ--------------------ALELLGL-AHLADRP-----------------------FNELSGGE 102
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 413 QQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG-VGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:cd03214  103 RQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
268-488 1.36e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 68.18  E-value: 1.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 268 VLEIKNLSRAgqYRD-------INLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTdaikrg 340
Cdd:PRK13639   1 ILETRDLKYS--YPDgtealkgINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKS------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 341 igyVSEDRLTLGAILQQSiaDNMVISIL---DRLKTPWHL-IDEKQCQDIVQEWIADLDIKVTDpNNALSTLSGGNQQKV 416
Cdd:PRK13639  73 ---LLEVRKTVGIVFQNP--DDQLFAPTveeDVAFGPLNLgLSKEEVEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRV 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 417 VLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
281-488 1.56e-12

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: 67.01  E-value: 1.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGkpVKLKNNTDAIKRGIGYVSE-----DRLTLGAIL 355
Cdd:cd03266   22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARRRLGFVSDstglyDRLTARENL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 356 QqsiadnmvisILDRLktpwHLIDEKQCQDIVQEWIADLDIKVTdPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPT 435
Cdd:cd03266  100 E----------YFAGL----YGLKGDELTARLEELADRLGMEEL-LDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491046221 436 VGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:cd03266  165 TGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
27-230 1.82e-12

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: 66.91  E-value: 1.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVyAPDDGSK---IEIDGKSyhrLTPDKARELgVQVIYQDLSLFPN 103
Cdd:cd03234   21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEGGGTTsgqILFNGQP---RKPDQFQKC-VAYVRQDDILLPG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 104 LTVAENIAFELNLKGYFGwFRKKQLREK-ALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASL 182
Cdd:cd03234   96 LTVRETLTYTAILRLPRK-SSDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 491046221 183 TRTEVNQLLSTVNYLKDKGITVVFVSHR-LEEVKEISDRITVIRDGQKI 230
Cdd:cd03234  175 DSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
269-485 2.03e-12

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: 66.36  E-value: 2.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRagQY----------RDINLNLKRGEVLGLCGLLGSGRTELaLSLF-GITHPDSGELFIEGKPV-KLKNNTDA 336
Cdd:cd03255    1 IELKNLSK--TYggggekvqalKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILgGLDRPTSGEVRVDGTDIsKLSEKELA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 337 IKRgigyvsedRLTLGAILQQSiadNMV--ISILDRLKTPWHL--IDEKQCQDIVQEWIADLDIKvtdpnNAL----STL 408
Cdd:cd03255   78 AFR--------RRHIGFVFQSF---NLLpdLTALENVELPLLLagVPKKERRERAEELLERVGLG-----DRLnhypSEL 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 409 SGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS-GVGISILLITDEASEAYYnCDRILHMKQGSI 485
Cdd:cd03255  142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
264-486 2.23e-12

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: 66.93  E-value: 2.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 264 DRRTVLEIKNL--SRAGQ--YRDINLNLKRGEVlglcgllgsgrteLAL-------------SLFGITHPDSGELFIEGK 326
Cdd:COG1127    1 MSEPMIEVRNLtkSFGDRvvLDGVSLDVPRGEI-------------LAIiggsgsgksvllkLIIGLLRPDSGEILVDGQ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 327 PV-KLKNNT-DAIKRGIGYVsedrltlgaiLQQ-------SIADNMVISILDRLKtpwhlIDEKQCQDIVQEWIADLDIK 397
Cdd:COG1127   68 DItGLSEKElYELRRRIGML----------FQGgalfdslTVFENVAFPLREHTD-----LSEAEIRELVLEKLELVGLP 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 398 vtdpnNAL----STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGV-GISILLITDEASEAYY 472
Cdd:COG1127  133 -----GAAdkmpSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFA 207
                        250
                 ....*....|....
gi 491046221 473 NCDRILHMKQGSIV 486
Cdd:COG1127  208 IADRVAVLADGKII 221
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
281-486 2.59e-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: 66.56  E-value: 2.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKlknNTDAIK--RGIGYVSEDrltLGAILQQS 358
Cdd:cd03295   18 NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR---EQDPVElrRKIGYVIQQ---IGLFPHMT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 359 IADNmvISILDRLKTpWhliDEKQCQDIVQEWIADLDIkvtDPNNAL----STLSGGNQQKVVLAKWILTRPKVLILDSP 434
Cdd:cd03295   92 VEEN--IALVPKLLK-W---PKEKIRERADELLALVGL---DPAEFAdrypHELSGGQQQRVGVARALAADPPLLLMDEP 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491046221 435 TVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:cd03295  163 FGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
312-487 2.63e-12

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: 66.16  E-value: 2.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 312 GITHPDSGELFIEGKPV---KLKNNTDAIKRGIGYVsedrltlgaiLQQ-------SIADNMVISIldRLKTPwhlideK 381
Cdd:cd03297   45 GLEKPDGGTIVLNGTVLfdsRKKINLPPQQRKIGLV----------FQQyalfphlNVRENLAFGL--KRKRN------R 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 382 QCQDIVQEWIADLDIkvtDP--NNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG-VGI 458
Cdd:cd03297  107 EDRISVDELLDLLGL---DHllNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKnLNI 183
                        170       180
                 ....*....|....*....|....*....
gi 491046221 459 SILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:cd03297  184 PVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
20-230 2.69e-12

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: 65.75  E-value: 2.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  20 SKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYapddGSKIEIDGK-SYHRLTPDKARE-LGVQVIY-- 95
Cdd:cd03233   14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT----EGNVSVEGDiHYNGIPYKEFAEkYPGEIIYvs 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  96 QDLSLFPNLTVAENIAFELNLKGyfgwfrkkqlrekaleilNELaftidpdtpVQFLPIAQRQQVAICRALVADARLVIM 175
Cdd:cd03233   90 EEDVHFPTLTVRETLDFALRCKG------------------NEF---------VRGISGGERKRVSIAEALVSRASVLCW 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 176 DEPTASLTRTEVNQLLSTVNYLKD--KGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:cd03233  143 DNSTRGLDSSTALEILKCIRTMADvlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
28-248 3.11e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 67.57  E-value: 3.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  28 ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS----------KIEIDGKSYHRLTP-----DKARELgVQ 92
Cdd:PRK13631  41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTiqvgdiyigdKKNNHELITNPYSKkiknfKELRRR-VS 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  93 VIYQ--DLSLFPNlTVAENIAF-ELNLKgyfgwFRKKQLREKALEILNELAFTID--PDTPVQfLPIAQRQQVAICRALV 167
Cdd:PRK13631 120 MVFQfpEYQLFKD-TIEKDIMFgPVALG-----VKKSEAKKLAKFYLNKMGLDDSylERSPFG-LSGGQKRRVAIAGILA 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 168 ADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ--KIGTwPAEGLTTRKITE 245
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKilKTGT-PYEIFTDQHIIN 271

                 ...
gi 491046221 246 LMT 248
Cdd:PRK13631 272 STS 274
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
2-228 3.42e-12

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 67.44  E-value: 3.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   2 TSTSKADKSDPLITLRDLSKSF----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPD---DGSKI--- 71
Cdd:PRK09473   1 TVPLAQQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATfng 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  72 -EIDGKSYHRLTPDKARElgVQVIYQD--LSLFPNLTVAENIAFELNL-KGYfgwfRKKQLREKALEILNELAFtidPDT 147
Cdd:PRK09473  81 rEILNLPEKELNKLRAEQ--ISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGM----SKAEAFEESVRMLDAVKM---PEA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 148 -------PVQFlPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISD 219
Cdd:PRK09473 152 rkrmkmyPHEF-SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICD 230

                 ....*....
gi 491046221 220 RITVIRDGQ 228
Cdd:PRK09473 231 KVLVMYAGR 239
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
282-501 4.16e-12

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 66.19  E-value: 4.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 282 DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKrgigyVSEDRLTLGAILQQ---- 357
Cdd:PRK11124  20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKA-----IRELRRNVGMVFQQynlw 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 358 ---SIADNMV---ISILDrlktpwhlIDEKQCQDIVQEWIADLdiKVTDPNNALST-LSGGNQQKVVLAKWILTRPKVLI 430
Cdd:PRK11124  95 phlTVQQNLIeapCRVLG--------LSKDQALARAEKLLERL--RLKPYADRFPLhLSGGQQQRVAIARALMMEPQVLL 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 431 LDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKEIVTDSINEQQLEE 501
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQPQTEA 235
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
10-236 4.54e-12

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 66.44  E-value: 4.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  10 SDPLITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARE 88
Cdd:PRK15056   3 QQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG-KISILGQPTRQALQKNLVA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  89 LGVQVIYQDLSlFPNLTvaENIAFeLNLKGYFGWFRK-----KQLREKALEILNELAFTidpDTPVQFLPIAQRQQVAIC 163
Cdd:PRK15056  82 YVPQSEEVDWS-FPVLV--EDVVM-MGRYGHMGWLRRakkrdRQIVTAALARVDMVEFR---HRQIGELSGGQKKRVFLA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 164 RALVADARLVIMDEP-TASLTRTEVnQLLSTVNYLKDKGITVVFVSHRLEEVKEISDrITVIRDGQKIGTWPAE 236
Cdd:PRK15056 155 RAIAQQGQVILLDEPfTGVDVKTEA-RIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTE 226
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
281-488 5.12e-12

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: 65.59  E-value: 5.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTdAIKRGIGYVSEDRLtlgaILQQSIA 360
Cdd:cd03252   19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPA-WLRRQVGVVLQENV----LFNRSIR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 361 DNMVisiLDRLKTPWHLIDEKQCQDIVQEWIADL----DIKVTDPNnalSTLSGGNQQKVVLAKWILTRPKVLILDSPTV 436
Cdd:cd03252   94 DNIA---LADPGMSMERVIEAAKLAGAHDFISELpegyDTIVGEQG---AGLSGGQRQRIAIARALIHNPRILIFDEATS 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491046221 437 GVDIGAKDSIYKLIHRLSGvGISILLITDEASeAYYNCDRILHMKQGSIVKE 488
Cdd:cd03252  168 ALDYESEHAIMRNMHDICA-GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQ 217
cbiO PRK13649
energy-coupling factor transporter ATPase;
27-228 5.51e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 66.31  E-value: 5.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS----KIEIDGKSYHRLTPDKARELGVQVIYQDLSLFP 102
Cdd:PRK13649  21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSvrvdDTLITSTSKNKDIKQIRKKVGLVFQFPESQLFE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 103 NlTVAENIAFELNLKGYFGWFRKKQLREK-ALEILNELAFTIDPdtpvqF-LPIAQRQQVAICRALVADARLVIMDEPTA 180
Cdd:PRK13649 101 E-TVLKDVAFGPQNFGVSQEEAEALAREKlALVGISESLFEKNP-----FeLSGGQMRRVAIAGILAMEPKILVLDEPTA 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 491046221 181 SLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
303-505 6.52e-12

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 66.78  E-value: 6.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 303 RTELALSLFGITHPDSGELFIEGKPVKLKnnTDAIKRGIGYVSE-DRLTLGAILQQSIadnMVISILDRLKTpwhlideK 381
Cdd:PRK13536  80 KSTIARMILGMTSPDAGKITVLGVPVPAR--ARLARARIGVVPQfDNLDLEFTVRENL---LVFGRYFGMST-------R 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 382 QCQDIVQEWI--ADLDIKVtdpNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGIS 459
Cdd:PRK13536 148 EIEAVIPSLLefARLESKA---DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKT 224
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 491046221 460 ILLITDEASEAYYNCDRILHMKQG-SIVKEIVTDSINEQ---QLEEIING 505
Cdd:PRK13536 225 ILLTTHFMEEAERLCDRLCVLEAGrKIAEGRPHALIDEHigcQVIEIYGG 274
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
269-489 7.11e-12

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 64.55  E-value: 7.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRA-GQYR---DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKpvKLKNNTDAIKRgigyv 344
Cdd:cd03268    1 LKTNDLTKTyGKKRvldDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRR----- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 345 sedrltLGAILQ-QSIADNMV----ISILDRLktpwHLIDEKQCQDIVQEW----IADLDIKvtdpnnalsTLSGGNQQK 415
Cdd:cd03268   74 ------IGALIEaPGFYPNLTarenLRLLARL----LGIRKKRIDEVLDVVglkdSAKKKVK---------GFSLGMKQR 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 416 VVLAKWILTRPKVLILDSPTVGVD-IGAKDsIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKEI 489
Cdd:cd03268  135 LGIALALLGNPDLLILDEPTNGLDpDGIKE-LRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
12-228 9.85e-12

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 67.22  E-value: 9.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGG---HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSyhrltpdkare 88
Cdd:PRK13545  20 PFDKLKDLFFRSKDgeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKG-TVDIKGSA----------- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  89 lgvQVIYQDLSLFPNLTVAENIafelNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVA 168
Cdd:PRK13545  88 ---ALIAISSGLNGQLTGIENI----ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHI 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 169 DARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK13545 161 NPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQ 220
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
281-486 1.39e-11

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: 63.81  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklkNNTDAIKRGIGYVsedrltlgaiLQQ--- 357
Cdd:cd03301   17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV---TDLPPKDRDIAMV----------FQNyal 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 358 ----SIADNMVISiLDRLKTPWHLIDEKqcqdiVQEWIADLDIKvTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDS 433
Cdd:cd03301   84 yphmTVYDNIAFG-LKLRKVPKDEIDER-----VREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 434 PTVGVD----IGAKDSIYKLIHRLsgvGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:cd03301  157 PLSNLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
283-486 1.86e-11

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 63.74  E-value: 1.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 283 INLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPV-KLKNN-TDAIKRGIGYVSEDRLTLgaiLQQSIA 360
Cdd:PRK10908  21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItRLKNReVPFLRRQIGMIFQDHHLL---MDRTVY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 361 DNMVISILdrlktpwhlIDEKQCQDIVQEWIADLDiKVTDPNNALS---TLSGGNQQKVVLAKWILTRPKVLILDSPTVG 437
Cdd:PRK10908  98 DNVAIPLI---------IAGASGDDIRRRVSAALD-KVGLLDKAKNfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 491046221 438 VDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:PRK10908 168 LDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
14-483 2.52e-11

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 66.30  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDG----KSYHRltpdkaREL 89
Cdd:NF033858   2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGR-VEVLGgdmaDARHR------RAV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 GVQVIY--QDL--SLFPNLTVAENIAFELNLkgyFGwFRKKQLREKALEILNE---LAFtidPDTPVQFLPIAQRQQVAI 162
Cdd:NF033858  75 CPRIAYmpQGLgkNLYPTLSVFENLDFFGRL---FG-QDAAERRRRIDELLRAtglAPF---ADRPAGKLSGGMKQKLGL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 163 CRALVADARLVIMDEPTAS---LTRtevNQLLSTVNYLKDK--GITVVFVSHRLEEVkEISDRITVIRDGQKIGTWPAEG 237
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGvdpLSR---RQFWELIDRIRAErpGMSVLVATAYMEEA-ERFDWLVAMDAGRVLATGTPAE 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 238 LTTRkitelmTG---LD--IVH----ERK---------PPNNAEDRRTVLEIKNLS-RAGQY---RDINLNLKRGEVlgl 295
Cdd:NF033858 224 LLAR------TGadtLEaaFIAllpeEKRrghqpvvipPRPADDDDEPAIEARGLTmRFGDFtavDHVSFRIRRGEI--- 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 296 cgllgsgrtelalslFG---------------IT---HPDSGE--LFieGKPVKLKNNtdAIKRGIGYVSE--------- 346
Cdd:NF033858 295 ---------------FGflgsngcgksttmkmLTgllPASEGEawLF--GQPVDAGDI--ATRRRVGYMSQafslygelt 355
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 347 --DRLTLGAilqqsiadnmvisildRLktpWHLiDEKQCQDIVQEWIADLDIK-VTDpnnAL-STLSGGNQQKVVLAKWI 422
Cdd:NF033858 356 vrQNLELHA----------------RL---FHL-PAAEIAARVAEMLERFDLAdVAD---ALpDSLPLGIRQRLSLAVAV 412
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 423 LTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS---GVGISIllitdeaSEAYYN----CDRILHMKQG 483
Cdd:NF033858 413 IHKPELLILDEPTSGVDPVARDMFWRLLIELSredGVTIFI-------STHFMNeaerCDRISLMHAG 473
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
273-494 2.54e-11

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 63.94  E-value: 2.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 273 NLSRAGQY----RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPV-KLKN-NTDAIKRGIGYVSE 346
Cdd:PRK10419  17 GLSGKHQHqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaKLNRaQRKAFRRDIQMVFQ 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 347 D-------RLTLGAILQQSIAdnmvisildrlktpwHL--IDEKQCQDIVQEWIADLDIKVTDPNNALSTLSGGNQQKVV 417
Cdd:PRK10419  97 DsisavnpRKTVREIIREPLR---------------HLlsLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVC 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 418 LAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG-VGISILLITDEASEAYYNCDRILHMKQGSIVKEI-VTDSI 494
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQpVGDKL 240
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
269-492 2.77e-11

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: 63.26  E-value: 2.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRAgqYR----------DINLNLKRGEVlglcgllgsgrteLAL---------SLF----GITHPDSGELFIEG 325
Cdd:cd03293    1 LEVRNVSKT--YGggggavtaleDISLSVEEGEF-------------VALvgpsgcgksTLLriiaGLERPTSGEVLVDG 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 326 KPVKlknntdAIKRGIGYVsedrltlgaiLQQ-------SIADNmvISILDRLKtpwhLIDEKQCQDIVQEWIADLDIKv 398
Cdd:cd03293   66 EPVT------GPGPDRGYV----------FQQdallpwlTVLDN--VALGLELQ----GVPKAEARERAEELLELVGLS- 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 399 tDPNNAL-STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDR 476
Cdd:cd03293  123 -GFENAYpHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADR 201
                        250
                 ....*....|....*...
gi 491046221 477 ILHMKQ--GSIVKEIVTD 492
Cdd:cd03293  202 VVVLSArpGRIVAEVEVD 219
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
269-485 4.80e-11

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 62.16  E-value: 4.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRA-GQY---RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKL-KNNTDAIKRGIGY 343
Cdd:cd03262    1 IEIKNLHKSfGDFhvlKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdKKNINELRQKVGM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 344 VsedrltlgaiLQQ-------SIADNMVISILDRLKtpwhlIDEKQCQDIVQEWIAdlDIKVTDPNNAL-STLSGGNQQK 415
Cdd:cd03262   81 V----------FQQfnlfphlTVLENITLAPIKVKG-----MSKAEAEERALELLE--KVGLADKADAYpAQLSGGQQQR 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 416 VVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSI 485
Cdd:cd03262  144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
PLN03211 PLN03211
ABC transporter G-25; Provisional
15-228 5.10e-11

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 65.29  E-value: 5.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  15 TLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISG-VYAPDDGSKIEIDGKsyhRLTPDKARELGVqv 93
Cdd:PLN03211  70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNFTGTILANNR---KPTKQILKRTGF-- 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IYQDLSLFPNLTVAENIAFELNLKGYFGWFRKKQLReKALEILNELAF-----TIDPDTPVQFLPIAQRQQVAICRALVA 168
Cdd:PLN03211 145 VTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKIL-VAESVISELGLtkcenTIIGNSFIRGISGGERKRVSIAHEMLI 223
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 169 DARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHR-LEEVKEISDRITVIRDGQ 228
Cdd:PLN03211 224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
310-488 5.43e-11

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 62.21  E-value: 5.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 310 LFGITHPDSGELFIEGKPVKlkNNTDAIKRGIGYVSEDrltlgailqQSIADNM-VISILD---RLKTpwhlIDEKQCQD 385
Cdd:cd03264   45 LATLTPPSSGTIRIDGQDVL--KQPQKLRRRIGYLPQE---------FGVYPNFtVREFLDyiaWLKG----IPSKEVKA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 386 IVQEWIADLDikVTDPNN-ALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLsGVGISILLIT 464
Cdd:cd03264  110 RVDEVLELVN--LGDRAKkKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILST 186
                        170       180
                 ....*....|....*....|....
gi 491046221 465 DEASEAYYNCDRILHMKQGSIVKE 488
Cdd:cd03264  187 HIVEDVESLCNQVAVLNKGKLVFE 210
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
263-502 6.13e-11

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 62.85  E-value: 6.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 263 EDRRTVLEIKNLSRagQYR--------DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNT 334
Cdd:PRK13648   2 EDKNSIIVFKNVSF--QYQsdasftlkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 335 DaIKRGIGYV--SEDRLTLGAILQQSIA---DNmvisildrlktpwHLIDEKQCQDIVQEWIADLDIkVTDPNNALSTLS 409
Cdd:PRK13648  80 K-LRKHIGIVfqNPDNQFVGSIVKYDVAfglEN-------------HAVPYDEMHRRVSEALKQVDM-LERADYEPNALS 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 410 GGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAyYNCDRILHMKQGSIVKE 488
Cdd:PRK13648 145 GGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKE 223
                        250
                 ....*....|....*.
gi 491046221 489 IVTDSI--NEQQLEEI 502
Cdd:PRK13648 224 GTPTEIfdHAEELTRI 239
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
30-215 7.10e-11

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 65.05  E-value: 7.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   30 RNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEIDGKSYHRLTPDKARElGVQVIYQDLSLFPNlTVAEN 109
Cdd:PTZ00265  402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRS-KIGVVSQDPLLFSN-SIKNN 479
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  110 IAFEL-NLK---------------GYFGWFRKKQLREKALEILNELAFTIDPDTPVQF---------------------- 151
Cdd:PTZ00265  480 IKYSLySLKdlealsnyynedgndSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMrknyqtikdsevvdvskkvlih 559
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  152 --------------------LPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLK--DKGITVVfVSH 209
Cdd:PTZ00265  560 dfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITII-IAH 638

                  ....*.
gi 491046221  210 RLEEVK 215
Cdd:PTZ00265  639 RLSTIR 644
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
14-104 7.61e-11

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: 64.43  E-value: 7.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRN-----IDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARE 88
Cdd:COG4615  328 LELRGVTYRYPGEDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGE-ILLDGQPVTADNREAYRQ 406
                         90
                 ....*....|....*.
gi 491046221  89 LgVQVIYQDLSLFPNL 104
Cdd:COG4615  407 L-FSAVFSDFHLFDRL 421
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
3-223 1.16e-10

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 63.67  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   3 STSKADKSDPLITLRDLSKSFGGHRaLRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGK-SY--H 79
Cdd:PRK13409 330 PPRDESERETLVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE-VDPELKiSYkpQ 407
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  80 RLTPDkarelgvqviyqdlslfPNLTVAENIAfelNLKGYFG--WFRkkqlrekaLEILNELAftIDP--DTPVQFLPIA 155
Cdd:PRK13409 408 YIKPD-----------------YDGTVEDLLR---SITDDLGssYYK--------SEIIKPLQ--LERllDKNVKDLSGG 457
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 156 QRQQVAICRALVADARLVIMDEPTASLtrtEVNQLLSTV----NYLKDKGITVVFVSHRLEEVKEISDRITV 223
Cdd:PRK13409 458 ELQRVAIAACLSRDADLYLLDEPSAHL---DVEQRLAVAkairRIAEEREATALVVDHDIYMIDYISDRLMV 526
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
307-486 1.24e-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: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 307 ALSLFGITHPDSGELFIEGKPVKLKNntdaIKRGIGYVSEDRLTLGailQQSIADNMVISIldrlktpwhlidekqcqdi 386
Cdd:cd03213   54 ALAGRRTGLGVSGEVLINGRPLDKRS----FRKIIGYVPQDDILHP---TLTVRETLMFAA------------------- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 387 vqewiadldikvtdpnnALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDE 466
Cdd:cd03213  108 -----------------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQ 170
                        170       180
                 ....*....|....*....|.
gi 491046221 467 AS-EAYYNCDRILHMKQGSIV 486
Cdd:cd03213  171 PSsEIFELFDKLLLLSQGRVI 191
cbiO PRK13642
energy-coupling factor transporter ATPase;
268-488 1.38e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 62.03  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 268 VLEIKNL-------SRAGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDaIKRG 340
Cdd:PRK13642   4 ILEVENLvfkyekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-LRRK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 341 IGYVSE--DRLTLGAILQQSIADNMVISILDRlktpwhlidEKQCQDIVQEWIA--DLDIKVTDPnnalSTLSGGNQQKV 416
Cdd:PRK13642  83 IGMVFQnpDNQFVGATVEDDVAFGMENQGIPR---------EEMIKRVDEALLAvnMLDFKTREP----ARLSGGQKQRV 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 417 VLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG-VGISILLITDEASEAyYNCDRILHMKQGSIVKE 488
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKE 221
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
247-486 1.39e-10

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: 63.70  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 247 MTGLDIVHErKPPNNAEDRRTV--------LEIKNLS----RAGQY--RDINLNLKRGEVlglcgllgsgrteLALS--- 309
Cdd:COG2274  445 LERLDDILD-LPPEREEGRSKLslprlkgdIELENVSfrypGDSPPvlDNISLTIKPGER-------------VAIVgrs 510
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 310 ----------LFGITHPDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDrltlGAILQQSIADNmvISI------LDRLkt 373
Cdd:COG2274  511 gsgkstllklLLGLYEPTSGRILIDGIDLR-QIDPASLRRQIGVVLQD----VFLFSGTIREN--ITLgdpdatDEEI-- 581
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 374 pWHLIDEKQCQDIVQEWIADLDIKVTDPNnalSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL 453
Cdd:COG2274  582 -IEAARLAGLHDFIEALPMGYDTVVGEGG---SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL 657
                        250       260       270
                 ....*....|....*....|....*....|...
gi 491046221 454 SGvGISILLITDEASeAYYNCDRILHMKQGSIV 486
Cdd:COG2274  658 LK-GRTVIIIAHRLS-TIRLADRIIVLDKGRIV 688
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
312-488 1.63e-10

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 61.20  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 312 GITHPDSGELFIEGKPVklknnTD------AiKRGIGYVSED-----RLTlgailqqsIADNmVISILDRLKtpwhlIDE 380
Cdd:COG1137   51 GLVKPDSGRIFLDGEDI-----THlpmhkrA-RLGIGYLPQEasifrKLT--------VEDN-ILAVLELRK-----LSK 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 381 KQCQDIVQEWIADLDI-KVTDpNNALStLSGGNQQKVVLAKWILTRPKVLILDSPTVGVD-IGAKDsIYKLIHRLSGVGI 458
Cdd:COG1137  111 KEREERLEELLEEFGItHLRK-SKAYS-LSGGERRRVEIARALATNPKFILLDEPFAGVDpIAVAD-IQKIIRHLKERGI 187
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491046221 459 SIlLITDeaseayYN-------CDR--ILHmkQGSIVKE 488
Cdd:COG1137  188 GV-LITD------HNvretlgiCDRayIIS--EGKVLAE 217
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
29-228 2.36e-10

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 62.76  E-value: 2.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPD--DGSKIEIDGksyHRLTPDKARELGVQVIYQDLsLFPNLTV 106
Cdd:TIGR00955  41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkGSGSVLLNG---MPIDAKEMRAISAYVQQDDL-FIPTLTV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  107 AENIAF--ELNLKGYFGwfrKKQLREKALEILNELAFTIDPDT------PVQFLPIAQRQQVAICRALVADARLVIMDEP 178
Cdd:TIGR00955 117 REHLMFqaHLRMPRRVT---KKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 491046221  179 TASLTRTEVNQLLSTVNYLKDKGITVVFVSHR-LEEVKEISDRITVIRDGQ 228
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGR 244
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
281-488 3.09e-10

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: 60.29  E-value: 3.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTD--AIKRGIGYVSEDrltLGAILQQS 358
Cdd:cd03258   22 KDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrKARRRIGMIFQH---FNLLSSRT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 359 IADNmVISILDRLKTPWHLIDEKqcqdiVQEWIADLDIkvTDPNNAL-STLSGGNQQKVVLAKWILTRPKVLILDSPTVG 437
Cdd:cd03258   99 VFEN-VALPLEIAGVPKAEIEER-----VLELLELVGL--EDKADAYpAQLSGGQKQRVGIARALANNPKVLLCDEATSA 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491046221 438 VDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:cd03258  171 LDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
20-228 4.60e-10

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: 59.41  E-value: 4.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  20 SKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGK-SYhrltpdkarelgvqviyqdL 98
Cdd:cd03250   12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGS-VSVPGSiAY-------------------V 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  99 SLFP---NLTVAENIAF--ELNlkgyfgwfrkKQLREKALEilnelAFTIDPDtpVQFLP-----------IA----QRQ 158
Cdd:cd03250   72 SQEPwiqNGTIRENILFgkPFD----------EERYEKVIK-----ACALEPD--LEILPdgdlteigekgINlsggQKQ 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 159 QVAICRALVADARLVIMDEPtasltrtevnqlLSTV-----NYLKDKGI--------TVVFVSHRLEEVKEiSDRITVIR 225
Cdd:cd03250  135 RISLARAVYSDADIYLLDDP------------LSAVdahvgRHIFENCIlglllnnkTRILVTHQLQLLPH-ADQIVVLD 201

                 ...
gi 491046221 226 DGQ 228
Cdd:cd03250  202 NGR 204
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
282-488 4.72e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 60.49  E-value: 4.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 282 DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKRGIGYVSE--DRLTLGAILQQSI 359
Cdd:PRK13633  28 DVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQnpDNQIVATIVEEDV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 360 A---DNMVI---SILDRlktpwhlIDEkqCQDIVQEWiadlDIKVTDPNnalsTLSGGNQQKVVLAKWILTRPKVLILDS 433
Cdd:PRK13633 108 AfgpENLGIppeEIRER-------VDE--SLKKVGMY----EYRRHAPH----LLSGGQKQRVAIAGILAMRPECIIFDE 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 434 PTVGVDIGAKDSIYKLIHRLSGV-GISILLIT---DEASEAyyncDRILHMKQGSIVKE 488
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKyGITIILIThymEEAVEA----DRIIVMDSGKVVME 225
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
2-223 6.58e-10

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: 61.34  E-value: 6.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   2 TSTSKADKSDPLITLRDLSKSFGGHRalrnidLTLNKGEVHC-----LAGTNGCGKSTLIKTISGVYAPDDGskiEIDGK 76
Cdd:COG1245  330 HAPRREKEEETLVEYPDLTKSYGGFS------LEVEGGEIREgevlgIVGPNGIGKTTFAKILAGVLKPDEG---EVDED 400
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  77 syhrltpdkarelgVQVIY--QDLSLFPNLTVAENIaFELNLKGYFG-WFRkkqlrekaLEILNELAftIDP--DTPVQF 151
Cdd:COG1245  401 --------------LKISYkpQYISPDYDGTVEEFL-RSANTDDFGSsYYK--------TEIIKPLG--LEKllDKNVKD 455
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 152 LPIAQRQQVAICRALVADARLVIMDEPTASLtrtEVNQLLSTV----NYLKDKGITVVFVSHRLEEVKEISDRITV 223
Cdd:COG1245  456 LSGGELQRVAIAACLSRDADLYLLDEPSAHL---DVEQRLAVAkairRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
14-210 7.11e-10

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: 57.93  E-value: 7.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLS-KSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYaPDDGSKIEIdgksyhrltPDKARELGV- 91
Cdd:cd03223    1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLW-PWGSGRIGM---------PEGEDLLFLp 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIYqdlslFPNLTVAENIAFElnlkgyfgWFRKkqlrekaleilnelaftidpdtpvqfLPIAQRQQVAICRALVADAR 171
Cdd:cd03223   71 QRPY-----LPLGTLREQLIYP--------WDDV--------------------------LSGGEQQRLAFARLLLHKPK 111
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTvnyLKDKGITVVFVSHR 210
Cdd:cd03223  112 FVFLDEATSALDEESEDRLYQL---LKELGITVISVGHR 147
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
269-488 9.45e-10

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: 58.99  E-value: 9.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRagQY------RDINLNLKRGEVlglcgllgsgrteLAL---------SLF----GITHPDSGELFIEGKPVK 329
Cdd:cd03219    1 LEVRGLTK--RFgglvalDDVSFSVRPGEI-------------HGLigpngagktTLFnlisGFLRPTSGSVLFDGEDIT 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 330 LKNNTDAIKRGIGyvsedR---LTlgAILQQ-SIADNMVISILDRLKTPWHLI----DEKQCQDIVQEWIADLDIkvTDP 401
Cdd:cd03219   66 GLPPHEIARLGIG-----RtfqIP--RLFPElTVLENVMVAAQARTGSGLLLArarrEEREARERAEELLERVGL--ADL 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 402 NNAL-STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLItdeasE-------AYyn 473
Cdd:cd03219  137 ADRPaGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLV-----EhdmdvvmSL-- 209
                        250
                 ....*....|....*
gi 491046221 474 CDRILHMKQGSIVKE 488
Cdd:cd03219  210 ADRVTVLDQGRVIAE 224
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
337-492 9.48e-10

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 58.94  E-value: 9.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 337 IKRGIGYVSEDrltlgaiLQQSI-----ADNMVIS----ILDRlktpWHLIDEKQcQDIVQEWIADLDIKvTDPNNALST 407
Cdd:COG1119   76 LRKRIGLVSPA-------LQLRFprdetVLDVVLSgffdSIGL----YREPTDEQ-RERARELLELLGLA-HLADRPFGT 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVG-ISILLIT---DEASEAYyncDRILHMKQG 483
Cdd:COG1119  143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVThhvEEIPPGI---THVLLLKDG 219
                        170
                 ....*....|....
gi 491046221 484 SIV-----KEIVTD 492
Cdd:COG1119  220 RVVaagpkEEVLTS 233
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
282-468 9.89e-10

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: 58.57  E-value: 9.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 282 DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPV-KLKNN-TDAIKRGIGYVSEDRLTLgaiLQQSI 359
Cdd:cd03292   19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRGRaIPYLRRKIGVVFQDFRLL---PDRNV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 360 ADNMVISILdrlktpwhlIDEKQCQDIVQEWIADLD-IKVTDPNNAL-STLSGGNQQKVVLAKWILTRPKVLILDSPTVG 437
Cdd:cd03292   96 YENVAFALE---------VTGVPPREIRKRVPAALElVGLSHKHRALpAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
                        170       180       190
                 ....*....|....*....|....*....|.
gi 491046221 438 VDIGAKDSIYKLIHRLSGVGISILLITDEAS 468
Cdd:cd03292  167 LDPDTTWEIMNLLKKINKAGTTVVVATHAKE 197
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
29-227 1.10e-09

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 58.50  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGK--SYHRLTPDKARELGVQVIYQDLSLFPNLTV 106
Cdd:cd03290   17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG-KVHWSNKneSEPSFEATRSRNRYSVAYAAQKPWLLNATV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 107 AENIAFElnlkGYFGWFRKKQLREkaleilnelAFTIDPDtpVQFLPI---------------AQRQQVAICRALVADAR 171
Cdd:cd03290   96 EENITFG----SPFNKQRYKAVTD---------ACSLQPD--IDLLPFgdqteigerginlsgGQRQRICVARALYQNTN 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 172 LVIMDEPTASLTRTEVNQLLST--VNYLKDKGITVVFVSHRLEEVKEiSDRITVIRDG 227
Cdd:cd03290  161 IVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
281-502 1.31e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 58.85  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKR-GIGYVSEDRLTLGAILQQSI 359
Cdd:PRK13632  26 KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKiGIIFQNPDNQFIGATVEDDI 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 360 AdnmvISILDRLktpwhlIDEKQCQDIVQEWIADLDIK---VTDPNNalstLSGGNQQKVVLAKWILTRPKVLILDSPTV 436
Cdd:PRK13632 106 A----FGLENKK------VPPKKMKDIIDDLAKKVGMEdylDKEPQN----LSGGQKQRVAIASVLALNPEIIIFDESTS 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 437 GVDIGAKDSIYKLIHRLSGVGISILL-ITDEASEAyYNCDRILHMKQGSIV-----KEIVTdsiNEQQLEEI 502
Cdd:PRK13632 172 MLDPKGKREIKKIMVDLRKTRKKTLIsITHDMDEA-ILADKVIVFSEGKLIaqgkpKEILN---NKEILEKA 239
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
312-503 1.90e-09

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 59.68  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 312 GITHPDSGELFIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGailQQSIADNmvisILDRLktPWHLIDEKQCQDIVQEWI 391
Cdd:PRK15439  59 GIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFP---NLSVKEN----ILFGL--PKRQASMQKMKQLLAALG 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 392 ADLDIKVtdpnnALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAY 471
Cdd:PRK15439 130 CQLDLDS-----SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIR 204
                        170       180       190
                 ....*....|....*....|....*....|..
gi 491046221 472 YNCDRILHMKQGSIVKEIVTDSINEqqlEEII 503
Cdd:PRK15439 205 QLADRISVMRDGTIALSGKTADLST---DDII 233
hmuV PRK13547
heme ABC transporter ATP-binding protein;
25-240 2.18e-09

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 58.30  E-value: 2.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  25 GHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSK-------IEIDGKSYHRLTPDK-ARELGVqviyq 96
Cdd:PRK13547  13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRgarvtgdVTLNGEPLAAIDAPRlARLRAV----- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  97 dlslfpnLTVAENIAF-----ELNLKGYFGWFRKK-QLREKALEILNELAFTIDPDT----PVQFLPIAQRQQVAICRAL 166
Cdd:PRK13547  88 -------LPQAAQPAFafsarEIVLLGRYPHARRAgALTHRDGEIAWQALALAGATAlvgrDVTTLSGGELARVQFARVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 167 ---------VADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAE 236
Cdd:PRK13547 161 aqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240

                 ....
gi 491046221 237 GLTT 240
Cdd:PRK13547 241 DVLT 244
cbiO PRK13644
energy-coupling factor transporter ATPase;
281-494 2.23e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 58.46  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKRGIGYVSEDRLT--LGAILQQS 358
Cdd:PRK13644  19 ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETqfVGRTVEED 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 359 IA---DNMVISILDRLKtpwhLIDEKQCQDIVQEWiadldikvtdPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPT 435
Cdd:PRK13644  99 LAfgpENLCLPPIEIRK----RVDRALAEIGLEKY----------RHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 436 VGVDIGAKDSIYKLIHRLSGVGISILLITDEASEaYYNCDRILHMKQGSIVKEIVTDSI 494
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENV 222
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
316-483 2.42e-09

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: 56.24  E-value: 2.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 316 PDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDrltlGAILQQSIADNMvisildrlktpwhlidekqcqdivqewiadld 395
Cdd:cd03228   54 PTSGEILIDGVDLR-DLDLESLRKNIAYVPQD----PFLFSGTIRENI-------------------------------- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 396 ikvtdpnnalstLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGvGISILLITDEASEAyYNCD 475
Cdd:cd03228   97 ------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTI-RDAD 162

                 ....*...
gi 491046221 476 RILHMKQG 483
Cdd:cd03228  163 RIIVLDDG 170
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
14-228 2.47e-09

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: 58.33  E-value: 2.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSF--GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDdgSKIEIDGKSYHRLTPDKARElGV 91
Cdd:cd03289    3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE--GDIQIDGVSWNSVPLQKWRK-AF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  92 QVIYQDLSLFPNltvaeniAFELNLKGYFGWFRKKQLR---EKALEILNE-----LAFTIDPDTPVqfLPIAQRQQVAIC 163
Cdd:cd03289   80 GVIPQKVFIFSG-------TFRKNLDPYGKWSDEEIWKvaeEVGLKSVIEqfpgqLDFVLVDGGCV--LSHGHKQLMCLA 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 164 RALVADARLVIMDEPTASLTRTEVNQLLSTVNYlKDKGITVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:cd03289  151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENK 213
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
35-228 2.73e-09

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 57.80  E-value: 2.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  35 TLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDG-SKIEIDGKSYhrlTPdkarelgvQVIYQDLSlfpnLTVAENIAFE 113
Cdd:cd03237   21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGdIEIELDTVSY---KP--------QYIKADYE----GTVRDLLSSI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 114 LNLKGYFGWFRKkqlrekalEILNELAftIDP--DTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASLtrtEVNQ-- 189
Cdd:cd03237   86 TKDFYTHPYFKT--------EIAKPLQ--IEQilDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL---DVEQrl 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 491046221 190 LLSTV--NYLKDKGITVVFVSHRLEEVKEISDRITVIrDGQ 228
Cdd:cd03237  153 MASKVirRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGE 192
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
29-230 3.14e-09

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 59.74  E-value: 3.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221    29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGvyaPDDGSKIEIDGK-SYHRLTPDK-ARELGVQVIY--QDLSLFPNL 104
Cdd:TIGR00956   77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS---NTDGFHIGVEGViTYDGITPEEiKKHYRGDVVYnaETDVHFPHL 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   105 TVAENIAFELNLKG----YFGWFRKKQLREKALEILNELAFTIDPDTPV-----QFLPIAQRQQVAICRALVADARLVIM 175
Cdd:TIGR00956  154 TVGETLDFAARCKTpqnrPDGVSREEYAKHIADVYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAKIQCW 233
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221   176 DEPTASL---TRTE-VNQLLSTVNYLKdkgiTVVFVS--HRLEEVKEISDRITVIRDGQKI 230
Cdd:TIGR00956  234 DNATRGLdsaTALEfIRALKTSANILD----TTPLVAiyQCSQDAYELFDKVIVLYEGYQI 290
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
267-453 3.67e-09

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 57.43  E-value: 3.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 267 TVLEIKNLSRA-GQYR---DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELfieGKPVKLKnntdaikrgIG 342
Cdd:PRK09544   3 SLVSLENVSVSfGQRRvlsDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---KRNGKLR---------IG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 343 YVSEdRLTLGAILQQSIADNM----------VISILDRLKTPwHLIDEkqcqdivqewiadldikvtdpnnALSTLSGGN 412
Cdd:PRK09544  71 YVPQ-KLYLDTTLPLTVNRFLrlrpgtkkedILPALKRVQAG-HLIDA-----------------------PMQKLSGGE 125
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 491046221 413 QQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL 453
Cdd:PRK09544 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQL 166
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
11-210 4.05e-09

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 59.05  E-value: 4.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  11 DPLITLRDLS-KSFGGHRALRNIDLTLNKGEvHCL-AGTNGCGKSTLIKTISG--------VYAPDDGSKIEIDGKSYhr 80
Cdd:COG4178  360 DGALALEDLTlRTPDGRPLLEDLSLSLKPGE-RLLiTGPSGSGKSTLLRAIAGlwpygsgrIARPAGARVLFLPQRPY-- 436
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  81 LTPDKARElgvQVIYqdlslfPNLtvAENIAFElnlkgyfgwfrkkQLREkALEILN--ELAFTIDPDTP-VQFLPIAQR 157
Cdd:COG4178  437 LPLGTLRE---ALLY------PAT--AEAFSDA-------------ELRE-ALEAVGlgHLAERLDEEADwDQVLSLGEQ 491
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 158 QQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTvnyLKD--KGITVVFVSHR 210
Cdd:COG4178  492 QRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL---LREelPGTTVISVGHR 543
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
283-488 4.58e-09

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 56.81  E-value: 4.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 283 INLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGailQQSIADN 362
Cdd:PRK11614  24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFS---RMTVEEN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 363 MVISILdrlktpwhLIDEKQCQDIVqEWIADLDIKVTDPNNALS-TLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIG 441
Cdd:PRK11614 101 LAMGGF--------FAERDQFQERI-KWVYELFPRLHERRIQRAgTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491046221 442 AKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:PRK11614 172 IIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
269-487 4.75e-09

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 58.19  E-value: 4.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS-RAGQYR---DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklknnTD-AIK-RGIG 342
Cdd:PRK11432   7 VVLKNITkRFGSNTvidNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-----THrSIQqRDIC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 343 YVSEdrlTLGAILQQSIADNmVISILDRLKTPWHLIDEKqcqdiVQEWIADLDIKVTDpNNALSTLSGGNQQKVVLAKWI 422
Cdd:PRK11432  82 MVFQ---SYALFPHMSLGEN-VGYGLKMLGVPKEERKQR-----VKEALELVDLAGFE-DRYVDQISGGQQQRVALARAL 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 423 LTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQ 217
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
310-488 5.22e-09

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 57.51  E-value: 5.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 310 LFGITHPDSGELFIEGKPVKlknntdaikrgiGYVSEDRLTLGAILQqsiADNM-----VISILdRLKTPWHLIDEKQCQ 384
Cdd:PRK13537  53 LLGLTHPDAGSISLCGEPVP------------SRARHARQRVGVVPQ---FDNLdpdftVRENL-LVFGRYFGLSAAAAR 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 385 DIVQEWI--ADLDIKVTDPnnaLSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILL 462
Cdd:PRK13537 117 ALVPPLLefAKLENKADAK---VGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILL 193
                        170       180
                 ....*....|....*....|....*.
gi 491046221 463 ITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:PRK13537 194 TTHFMEEAERLCDRLCVIEEGRKIAE 219
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
318-486 1.07e-08

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 57.75  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  318 SGELFIEGKPVklknNTDAIKRGIGYVSEDRLTLGAIlqqSIADNMVISIldRLKTPWHLiDEKQCQDIVQEWIADL--- 394
Cdd:TIGR00955  82 SGSVLLNGMPI----DAKEMRAISAYVQQDDLFIPTL---TVREHLMFQA--HLRMPRRV-TKKEKRERVDEVLQALglr 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  395 ---DIKVTDPNNaLSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVG-ISILLITDEASEA 470
Cdd:TIGR00955 152 kcaNTRIGVPGR-VKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGkTIICTIHQPSSEL 230
                         170
                  ....*....|....*.
gi 491046221  471 YYNCDRILHMKQGSIV 486
Cdd:TIGR00955 231 FELFDKIILMAEGRVA 246
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
281-486 1.13e-08

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: 55.80  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGK-PVKLKNNtdaIKRGIGYVSEDRLTL-------- 351
Cdd:cd03267   38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKRRKK---FLRRIGVVFGQKTQLwwdlpvid 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 352 GAILQQSIADNMVISILDRLKtpwHLIDEKQCQDIvqewiadLDIKVtdpnnalSTLSGGNQQKVVLAKWILTRPKVLIL 431
Cdd:cd03267  115 SFYLLAAIYDLPPARFKKRLD---ELSELLDLEEL-------LDTPV-------RQLSLGQRMRAEIAAALLHEPEILFL 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 432 DSPTVGVDIGAKDSIYKLIHRLSGV-GISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:cd03267  178 DEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
365-496 1.32e-08

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 55.82  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 365 ISILDRLKTPWH---LIDEKQCQDIVQEWIADLDI--KVTDP-NNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGV 438
Cdd:PRK14246 105 LSIYDNIAYPLKshgIKEKREIKKIVEECLRKVGLwkEVYDRlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 439 DIGAKDSIYKLIHRLSGvGISILLITDEASEAYYNCDRILHMKQGSIVK-----EIVTDSINE 496
Cdd:PRK14246 185 DIVNSQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGELVEwgssnEIFTSPKNE 246
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
35-228 1.40e-08

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 55.71  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  35 TLNKGEVHCLAGTNGCGKSTLIKTISGVYaPDDGSkIEIDGKSyhrLTPDKARELGVQVIYqdlslfpnLTVAENIAFEL 114
Cdd:PRK03695  18 EVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGS-IQFAGQP---LEAWSAAELARHRAY--------LSQQQTPPFAM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 115 NLKGYFGWFRKKQLREKALE-ILNELA--FTIDP--DTPVQFLPIAQRQQV---AIC----RALVADARLVIMDEPTASL 182
Cdd:PRK03695  85 PVFQYLTLHQPDKTRTEAVAsALNEVAeaLGLDDklGRSVNQLSGGEWQRVrlaAVVlqvwPDINPAGQLLLLDEPMNSL 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 491046221 183 TRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGK 210
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
256-487 1.81e-08

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 56.38  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 256 RKPPNNAEDRRTVLEIKNLSRA--GQY--RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEG------ 325
Cdd:PRK11607   7 RPQAKTRKALTPLLEIRNLTKSfdGQHavDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlshv 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 326 ----KPVKLKNNTDA------IKRGIGY-VSEDRLTLGailqqsiadnmviSILDRLKTPWHLIDekqcqdiVQEWIAdl 394
Cdd:PRK11607  87 ppyqRPINMMFQSYAlfphmtVEQNIAFgLKQDKLPKA-------------EIASRVNEMLGLVH-------MQEFAK-- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 395 dikvTDPNNalstLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSI-YKLIHRLSGVGISILLITDEASEAYYN 473
Cdd:PRK11607 145 ----RKPHQ----LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTM 216
                        250
                 ....*....|....
gi 491046221 474 CDRILHMKQGSIVK 487
Cdd:PRK11607 217 AGRIAIMNRGKFVQ 230
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
26-238 1.89e-08

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 55.48  E-value: 1.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  26 HRAL-RNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAP---DDGSKIEIDGKSYHrltPDKARELGVQVIYQD-LSL 100
Cdd:PRK10418  15 AQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrQTAGRVLLDGKPVA---PCALRGRKIATIMQNpRSA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 101 F-PNLTVAENIAFELNLKGyfgwfrKKQLREKALEILNELAFTiDPDTPVQFLP------IAQRQQVAIcrALVADARLV 173
Cdd:PRK10418  92 FnPLHTMHTHARETCLALG------KPADDATLTAALEAVGLE-NAARVLKLYPfemsggMLQRMMIAL--ALLCEAPFI 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 174 IMDEPTASL---TRTEVNQLLSTVnyLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGL 238
Cdd:PRK10418 163 IADEPTTDLdvvAQARILDLLESI--VQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
269-485 2.11e-08

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: 53.76  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS-RAGQ-----YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKlKNNTDAIKRGIG 342
Cdd:cd03246    1 LEVENVSfRYPGaeppvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS-QWDPNELGDHVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 343 YVSEDRLTLGAilqqSIADNMvisildrlktpwhlidekqcqdivqewiadldikvtdpnnalstLSGGNQQKVVLAKWI 422
Cdd:cd03246   80 YLPQDDELFSG----SIAENI--------------------------------------------LSGGQRQRLGLARAL 111
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 423 LTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEaSEAYYNCDRILHMKQGSI 485
Cdd:cd03246  112 YGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
11-209 2.32e-08

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 56.48  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   11 DPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIdGKSyhrltpdkarelg 90
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGT-IEI-GET------------- 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   91 VQVIYQDLS---LFPNLTVAENIA----------FELNLKGYFGWFR-KKQLREKaleilnelaftidpdtPVQFLPIAQ 156
Cdd:TIGR03719 385 VKLAYVDQSrdaLDPNKTVWEEISggldiiklgkREIPSRAYVGRFNfKGSDQQK----------------KVGQLSGGE 448
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 491046221  157 RQQVAICRALVADARLVIMDEPTASLtrtEVNQLLSTVNYLKDKGITVVFVSH 209
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDL---DVETLRALEEALLNFAGCAVVISH 498
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
264-502 2.35e-08

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 55.41  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 264 DRRTVLEIKNLS----RAGQY--RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDaI 337
Cdd:PRK13635   1 MKEEIIRVEHISfrypDAATYalKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-V 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 338 KRGIGYVSE--DRLTLGAILQQSIA----------DNMVISILDRLKtpwhlidEKQCQDIVQEwiadldikvtDPnnal 405
Cdd:PRK13635  80 RRQVGMVFQnpDNQFVGATVQDDVAfglenigvprEEMVERVDQALR-------QVGMEDFLNR----------EP---- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 406 STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG-VGISILLIT---DEASEAyyncDRILHMK 481
Cdd:PRK13635 139 HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqKGITVLSIThdlDEAAQA----DRVIVMN 214
                        250       260
                 ....*....|....*....|...
gi 491046221 482 QGSIVKEIVTDSINE--QQLEEI 502
Cdd:PRK13635 215 KGEILEEGTPEEIFKsgHMLQEI 237
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
406-485 2.72e-08

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 54.68  E-value: 2.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 406 STLSGGNQQKVVLAKWILTRPKVLILDSPtvgvdIGAKDSIYK-----LIHRL-SGVGISILLITDEASEAYYNCDRILH 479
Cdd:PRK11247 132 AALSGGQKQRVALARALIHRPGLLLLDEP-----LGALDALTRiemqdLIESLwQQHGFTVLLVTHDVSEAVAMADRVLL 206

                 ....*.
gi 491046221 480 MKQGSI 485
Cdd:PRK11247 207 IEEGKI 212
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
266-485 2.76e-08

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 55.02  E-value: 2.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 266 RTVLEIKNLSRAGQYRD----INLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSgelfIEGKPVKLKNNT-DAIKRG 340
Cdd:PRK09984   2 QTIIRVEKLAKTFNQHQalhaVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK----SAGSHIELLGRTvQREGRL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 341 IGYVSEDRLTLGAILQQ-------SIADNMVISILDrlKTP-------WHLIDEKQ--CQDIVQEWIADLdikvtdPNNA 404
Cdd:PRK09984  78 ARDIRKSRANTGYIFQQfnlvnrlSVLENVLIGALG--STPfwrtcfsWFTREQKQraLQALTRVGMVHF------AHQR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 405 LSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGV-GISILLITDEASEAYYNCDRILHMKQG 483
Cdd:PRK09984 150 VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQG 229

                 ..
gi 491046221 484 SI 485
Cdd:PRK09984 230 HV 231
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
281-488 2.85e-08

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: 54.54  E-value: 2.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDRLtlgaILQQSIA 360
Cdd:cd03254   20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR-DISRKSLRSMIGVVLQDTF----LFSGTIM 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 361 DNMvisildRLKTPwhLIDEKQCQDIVQEWIADLDIK------VTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSP 434
Cdd:cd03254   95 ENI------RLGRP--NATDEEVIEAAKEAGAHDFIMklpngyDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 435 TVGVDIGA----KDSIYKLI---------HRLSGVgisillitdeaseayYNCDRILHMKQGSIVKE 488
Cdd:cd03254  167 TSNIDTETekliQEALEKLMkgrtsiiiaHRLSTI---------------KNADKILVLDDGKIIEE 218
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
310-486 3.13e-08

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: 54.13  E-value: 3.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 310 LFGITHPDSGELFIEGKPVKLKNNTDaIKRGIGYVSED-RLTLGailqqSIADNMVISILdrlktpwhLIDEKQCQDIVQ 388
Cdd:cd03245   50 LAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYVPQDvTLFYG-----TLRDNITLGAP--------LADDERILRAAE 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 389 ewIADLDIKVTDPNNALST--------LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDsiyKLIHRLSGV--GI 458
Cdd:cd03245  116 --LAGVTDFVNKHPNGLDLqigergrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEE---RLKERLRQLlgDK 190
                        170       180
                 ....*....|....*....|....*...
gi 491046221 459 SILLITDEASeAYYNCDRILHMKQGSIV 486
Cdd:cd03245  191 TLIIITHRPS-LLDLVDRIIVMDSGRIV 217
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
29-227 3.57e-08

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: 56.46  E-value: 3.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221    29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGK-SYHRLTPdkarelgvqviyqdlSLFPNlTVA 107
Cdd:TIGR01271  442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG-KIKHSGRiSFSPQTS---------------WIMPG-TIK 504
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   108 ENIAFELNlkgyFGWFRKKQLReKALEILNELAFTIDPDTPVQF-----LPIAQRQQVAICRALVADARLVIMDEPTASL 182
Cdd:TIGR01271  505 DNIIFGLS----YDEYRYTSVI-KACQLEEDIALFPEKDKTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 491046221   183 TRTEVNQLLST--VNYLKDKgiTVVFVSHRLEEVKEiSDRITVIRDG 227
Cdd:TIGR01271  580 DVVTEKEIFESclCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEG 623
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
308-505 4.05e-08

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 54.41  E-value: 4.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 308 LSLFGITHPDS-GELFIEGKPVKlKNNTDAIKRGIGYVSEdrltlgailQQSIADNMVISILDRL-KTPWH-------LI 378
Cdd:PRK10575  54 LKMLGRHQPPSeGEILLDAQPLE-SWSSKAFARKVAYLPQ---------QLPAAEGMTVRELVAIgRYPWHgalgrfgAA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 379 DEKQcqdiVQEWIADLDIKvtdP--NNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGV 456
Cdd:PRK10575 124 DREK----VEEAISLVGLK---PlaHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQE 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 491046221 457 -GISILLITDEASEAYYNCDRILHMKQGSIVKEIVTDSINEQQLEEIING 505
Cdd:PRK10575 197 rGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYG 246
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
318-486 4.37e-08

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


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 53.81  E-value: 4.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 318 SGELFIEGKPVKlknnTDAIKRGIGYVSE-DRLTLGAILQQSIAdNMVISILDRLKTpwHLIDEKQCQDIVQEWIADLDI 396
Cdd:cd03234   64 SGQILFNGQPRK----PDQFQKCVAYVRQdDILLPGLTVRETLT-YTAILRLPRKSS--DAIRKKRVEDVLLRDLALTRI 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 397 KvtdpNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGakdSIYKLIHRLS--GVGISILLITDEA--SEAYY 472
Cdd:cd03234  137 G----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF---TALNLVSTLSqlARRNRIVILTIHQprSDLFR 209
                        170
                 ....*....|....
gi 491046221 473 NCDRILHMKQGSIV 486
Cdd:cd03234  210 LFDRILLLSSGEIV 223
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
389-494 4.61e-08

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 54.16  E-value: 4.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 389 EWIADLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEA 467
Cdd:PRK11701 133 DWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDL 212
                         90       100
                 ....*....|....*....|....*..
gi 491046221 468 SEAYYNCDRILHMKQGSIVKEIVTDSI 494
Cdd:PRK11701 213 AVARLLAHRLLVMKQGRVVESGLTDQV 239
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
269-485 6.62e-08

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 54.32  E-value: 6.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS----RAGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklkNNTDAIKRGIGYV 344
Cdd:PRK10851   3 IEIANIKksfgRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDRKVGFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 345 SEDRltlgAILQQ-SIADNMV--ISILDRLKTP-WHLIDEKQCQ--DIVQewIADLdikvtdPNNALSTLSGGNQQKVVL 418
Cdd:PRK10851  80 FQHY----ALFRHmTVFDNIAfgLTVLPRRERPnAAAIKAKVTQllEMVQ--LAHL------ADRYPAQLSGGQKQRVAL 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 419 AKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSI 485
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
26-228 6.90e-08

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 55.10  E-value: 6.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  26 HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELgVQVIYQDLSLFPNlT 105
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG-DIRFHDIPLTKLQLDSWRSR-LAVVSQTPFLFSD-T 404
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 106 VAENIAFElnlkgyfgwfrKKQLREKALEILNELAFTIDP--------DTPVQ----FLPIAQRQQVAICRALVADARLV 173
Cdd:PRK10789 405 VANNIALG-----------RPDATQQEIEHVARLASVHDDilrlpqgyDTEVGergvMLSGGQKQRISIARALLLNAEIL 473
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 174 IMDEP-TASLTRTEvNQLLSTVNYLKdKGITVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:PRK10789 474 ILDDAlSAVDGRTE-HQILHNLRQWG-EGRTVIISAHRLSALTE-ASEILVMQHGH 526
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
312-488 7.49e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 53.65  E-value: 7.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 312 GITHPDSGELFIEGKPVKlKNNTDAIKRGIGYV--SEDRLTLGAILQQSIADNMVISILDRlKTPWHLIDEKqcqdIVQE 389
Cdd:PRK13652  52 GILKPTSGSVLIRGEPIT-KENIREVRKFVGLVfqNPDDQIFSPTVEQDIAFGPINLGLDE-ETVAHRVSSA----LHML 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 390 WIADLDIKVtdPNNalstLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS-GVGISILLITDEAS 468
Cdd:PRK13652 126 GLEELRDRV--PHH----LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPeTYGMTVIFSTHQLD 199
                        170       180
                 ....*....|....*....|
gi 491046221 469 EAYYNCDRILHMKQGSIVKE 488
Cdd:PRK13652 200 LVPEMADYIYVMDKGRIVAY 219
cbiO PRK13637
energy-coupling factor transporter ATPase;
408-486 8.25e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 53.90  E-value: 8.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
29-243 9.65e-08

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 54.95  E-value: 9.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221    29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKAReLGVQVIYQDLSLFPNltvae 108
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEG-EIIIDGLNIAKIGLHDLR-FKITIIPQDPVLFSG----- 1374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   109 niAFELNLKGyFGWFRKKQLReKALEILNELAFTIDPDTPVQF--------LPIAQRQQVAICRALVADARLVIMDEPTA 180
Cdd:TIGR00957 1375 --SLRMNLDP-FSQYSDEEVW-WALELAHLKTFVSALPDKLDHecaeggenLSVGQRQLVCLARALLRKTKILVLDEATA 1450
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221   181 SLTRTEVNQLLSTVNYLKDKgITVVFVSHRLEEVKEISdRITVIRDG--QKIGTwPAEGLTTRKI 243
Cdd:TIGR00957 1451 AVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGevAEFGA-PSNLLQQRGI 1512
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
29-234 1.24e-07

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: 53.32  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKsyhrltpdkarelgVQVIYQDLSLFPNlTVAE 108
Cdd:cd03291   53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG-KIKHSGR--------------ISFSSQFSWIMPG-TIKE 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 109 NIAFELNLKGYfgwfRKKQLReKALEILNELAFTIDPDTPVQ-----FLPIAQRQQVAICRALVADARLVIMDEPTASL- 182
Cdd:cd03291  117 NIIFGVSYDEY----RYKSVV-KACQLEEDITKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLd 191
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491046221 183 TRTEVNQLLSTVNYLKDKGiTVVFVSHRLEEVKeISDRITVIRDGQKI--GTWP 234
Cdd:cd03291  192 VFTEKEIFESCVCKLMANK-TRILVTSKMEHLK-KADKILILHEGSSYfyGTFS 243
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
93-256 1.42e-07

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 54.26  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   93 VIYQDLSLFpNLTVAENIAFelnlkGYFGWFRKKQLREKALEILNELAFTIDP--DTPV----QFLPIAQRQQVAICRAL 166
Cdd:PTZ00265 1300 IVSQEPMLF-NMSIYENIKF-----GKEDATREDVKRACKFAAIDEFIESLPNkyDTNVgpygKSLSGGQKQRIAIARAL 1373
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  167 VADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKG-ITVVFVSHRLEEVKEiSDRITVIRDGQKIGTW-PAEGLTtrkiT 244
Cdd:PTZ00265 1374 LREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKR-SDKIVVFNNPDRTGSFvQAHGTH----E 1448
                         170
                  ....*....|..
gi 491046221  245 ELMTGLDIVHER 256
Cdd:PTZ00265 1449 ELLSVQDGVYKK 1460
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
408-488 1.43e-07

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 53.94  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG-VGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQeLNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236

                 ..
gi 491046221 487 KE 488
Cdd:PRK15134 237 EQ 238
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
15-209 1.46e-07

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: 53.79  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   15 TLRDLSKSFGGHRA-LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVyapDDgskiEIDGKSyhRLTPdkarelGVQV 93
Cdd:TIGR03719   6 TMNRVSKVVPPKKEiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DK----DFNGEA--RPQP------GIKV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   94 IY--QDLSLFPNLTVAENIAF-------------ELNLK-----GYFGWFRKKQ--LREK-----ALEILNELAFTID-- 144
Cdd:TIGR03719  71 GYlpQEPQLDPTKTVRENVEEgvaeikdaldrfnEISAKyaepdADFDKLAAEQaeLQEIidaadAWDLDSQLEIAMDal 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221  145 ----PDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLlstVNYLKDKGITVVFVSH 209
Cdd:TIGR03719 151 rcppWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWL---ERHLQEYPGTVVAVTH 216
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
28-246 1.55e-07

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 53.58  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  28 ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGVQVIYQD---LSLFPNL 104
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGT-ITLHGKKINNHNANEAINHGFALVTEErrsTGIYAYL 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 105 TVAEN--IAFELNLKGYFGWFRKKQLREKALEILNELAF-TIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTAS 181
Cdd:PRK10982 342 DIGFNslISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 182 L---TRTEVNQLLSTVNYlKDKGItvVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITEL 246
Cdd:PRK10982 422 IdvgAKFEIYQLIAELAK-KDKGI--IIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNEILRL 486
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
14-228 1.70e-07

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 53.74  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKieidgksyhrltpdKARElGVQV 93
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------------KWSE-NANI 384
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  94 IY--QDlslfpnltVAENIAFELNLKGYFGWFRKKQLREKALE-ILNELAFTIDpDT--PVQFLPIAQRQQVAICRALVA 168
Cdd:PRK15064 385 GYyaQD--------HAYDFENDLTLFDWMSQWRQEGDDEQAVRgTLGRLLFSQD-DIkkSVKVLSGGEKGRMLFGKLMMQ 455
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 169 DARLVIMDEPTASLTRTEVNQL-LSTVNYlkdKGiTVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLnMALEKY---EG-TLIFVSHDREFVSSLATRIIEITPDG 512
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
371-483 2.10e-07

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 52.30  E-value: 2.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 371 LKTPWHLIDEKQCQDIVQEWiadLD-IKVTD-PNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYK 448
Cdd:PRK11300 118 LKTPAFRRAESEALDRAATW---LErVGLLEhANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDE 194
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491046221 449 LIHRLSG-VGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:PRK11300 195 LIAELRNeHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
281-483 2.26e-07

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


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 51.70  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKnntdaikrgigyvSEDRLTlgaILQQ--- 357
Cdd:TIGR01184   2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEP-------------GPDRMV---VFQNysl 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  358 ----SIADNMVISIlDRLKtpwHLIDEKQCQDIVQEWIADLDIKVTdPNNALSTLSGGNQQKVVLAKWILTRPKVLILDS 433
Cdd:TIGR01184  66 lpwlTVRENIALAV-DRVL---PDLSKSERRAIVEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221  434 PtvgvdIGAKDSIYK--LIHRLSGV----GISILLITDEASEAYYNCDRILHMKQG 483
Cdd:TIGR01184 141 P-----FGALDALTRgnLQEELMQIweehRVTVLMVTHDVDEALLLSDRVVMLTNG 191
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
310-485 2.26e-07

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: 53.86  E-value: 2.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   310 LFGITHPDSGELFIEGKPVKlkNNTDAIKRGIGYVSEDRLTLGAIlqqSIADNMVISILDRLKTpWhliDEKQCQdiVQE 389
Cdd:TIGR01257  976 LTGLLPPTSGTVLVGGKDIE--TNLDAVRQSLGMCPQHNILFHHL---TVAEHILFYAQLKGRS-W---EEAQLE--MEA 1044
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   390 WIADLDIKvTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGvGISILLITDEASE 469
Cdd:TIGR01257 1045 MLEDTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDE 1122
                          170
                   ....*....|....*.
gi 491046221   470 AYYNCDRILHMKQGSI 485
Cdd:TIGR01257 1123 ADLLGDRIAIISQGRL 1138
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
16-209 2.54e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 53.42  E-value: 2.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  16 LRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS-----KIEIDGKSYHR--LTPDKare 88
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRihcgtKLEVAYFDQHRaeLDPEK--- 398
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  89 lgvqviyqdlslfpnlTVAENIA---FELNLKGyfgwfRKKQlrekALEILNELAFTidPD---TPVQFLPIAQRQQVAI 162
Cdd:PRK11147 399 ----------------TVMDNLAegkQEVMVNG-----RPRH----VLGYLQDFLFH--PKramTPVKALSGGERNRLLL 451
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491046221 163 CRALVADARLVIMDEPTASLTrTEVNQLLSTVnyLKDKGITVVFVSH 209
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLD-VETLELLEEL--LDSYQGTVLLVSH 495
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
268-485 2.79e-07

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 51.63  E-value: 2.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 268 VLEIKNLS-RAGQ---YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklkNNTDAIKRGIgy 343
Cdd:PRK09493   1 MIEFKNVSkHFGPtqvLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV---NDPKVDERLI-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 344 vsedRLTLGAILQQ-------SIADNMVISildrlktPWHL--IDEKQCQDIVQEWIAdldiKV---TDPNNALSTLSGG 411
Cdd:PRK09493  76 ----RQEAGMVFQQfylfphlTALENVMFG-------PLRVrgASKEEAEKQARELLA----KVglaERAHHYPSELSGG 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 412 NQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSI 485
Cdd:PRK09493 141 QQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
13-96 2.89e-07

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 51.72  E-value: 2.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGV--YAPDDGSkIEIDGKSYHRLTPDKARELG 90
Cdd:PRK09580   1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGT-VEFKGKDLLELSPEDRAGEG 79

                 ....*.
gi 491046221  91 VQVIYQ 96
Cdd:PRK09580  80 IFMAFQ 85
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
407-484 3.03e-07

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 52.89  E-value: 3.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 407 TLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLI-HRLSgvGISILLITDEAS-EAYYncDRILHMKQGS 484
Cdd:COG4178  485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLrEELP--GTTVISVGHRSTlAAFH--DRVLELTGDG 560
cbiO PRK13646
energy-coupling factor transporter ATPase;
385-488 3.16e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 52.09  E-value: 3.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 385 DIVQEWIADLDIKVTDPNNALST----LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS-GVGIS 459
Cdd:PRK13646 119 DEVKNYAHRLLMDLGFSRDVMSQspfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKT 198
                         90       100
                 ....*....|....*....|....*....
gi 491046221 460 ILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:PRK13646 199 IILVSHDMNEVARYADEVIVMKEGSIVSQ 227
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
5-232 3.25e-07

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: 53.48  E-value: 3.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221     5 SKADKSDpLITLRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIeIDGKSYhrLT 82
Cdd:TIGR01257 1930 SGGNKTD-ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDAT-VAGKSI--LT 2005
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221    83 pdkarelGVQVIYQDLSLFPN-------LTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIA 155
Cdd:TIGR01257 2006 -------NISDVHQNMGYCPQfdaiddlLTGREHLYLYARLRG----VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGG 2074
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221   156 QRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDG--QKIGT 232
Cdd:TIGR01257 2075 NKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGafQCLGT 2153
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
241-498 3.27e-07

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 53.19  E-value: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  241 RKITELMtgldivhERKP--PNNAEDR----RTVLEIKNLSRAGQYR-------DINLNLKRGEVLGLCGLLGSGRTELA 307
Cdd:TIGR00958 452 EKVFEYL-------DRKPniPLTGTLAplnlEGLIEFQDVSFSYPNRpdvpvlkGLTFTLHPGEVVALVGPSGSGKSTVA 524
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  308 LSLFGITHPDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDRLTLGAILQQSIA-------DNMVISIldrlktpwhlIDE 380
Cdd:TIGR00958 525 ALLQNLYQPTGGQVLLDGVPLV-QYDHHYLHRQVALVGQEPVLFSGSVRENIAygltdtpDEEIMAA----------AKA 593
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  381 KQCQDIVQEWIADLDikvTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLihrLSGVGISI 460
Cdd:TIGR00958 594 ANAHDFIMEFPNGYD---TEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES---RSRASRTV 667
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 491046221  461 LLITDEASEAyYNCDRILHMKQGSIVKEIVTDSINEQQ 498
Cdd:TIGR00958 668 LLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
407-480 3.30e-07

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: 50.23  E-value: 3.30e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 407 TLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLsgvGISILLITDEAS-EAYYncDRILHM 480
Cdd:cd03223   91 VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVGHRPSlWKFH--DRVLDL 160
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
14-216 3.61e-07

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: 52.99  E-value: 3.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221    14 ITLRDLSKSF--GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDdgSKIEIDGKSYHRLTPDKARElGV 91
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE--GEIQIDGVSWNSVTLQTWRK-AF 1294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221    92 QVIYQDLSLFPNltvaeniAFELNLKGYFGWFRKK--------QLREKALEILNELAFTIDPDTPVqfLPIAQRQQVAIC 163
Cdd:TIGR01271 1295 GVIPQKVFIFSG-------TFRKNLDPYEQWSDEEiwkvaeevGLKSVIEQFPDKLDFVLVDGGYV--LSNGHKQLMCLA 1365
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 491046221   164 RALVADARLVIMDEPTASLTRTEVNQLLSTvnyLKD--KGITVVFVSHRLEEVKE 216
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKT---LKQsfSNCTVILSEHRVEALLE 1417
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
269-464 3.68e-07

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: 50.57  E-value: 3.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNL--SRAGQ--YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPvkLKNNTDAIKRGIGYV 344
Cdd:cd03231    1 LEADELtcERDGRalFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP--LDFQRDSIARGLLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 345 SEdrltlgailqqsiADNM--VISILDRLkTPWHLIDEKqcqDIVQEWIADLDIKVTDpNNALSTLSGGNQQKVVLAKWI 422
Cdd:cd03231   79 GH-------------APGIktTLSVLENL-RFWHADHSD---EQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLL 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 491046221 423 LTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLIT 464
Cdd:cd03231  141 LSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTT 182
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
12-227 4.52e-07

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 52.32  E-value: 4.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISG----VYAPD-------DGSKIEI-DGKsyh 79
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqGYSNDltlfgrrRGSGETIwDIK--- 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  80 rltpdkaRELGvqviYQDLSLFPNLTVAENIafeLN--LKGYF---GWF-----RKKQLREKALEILN---ELAftidpD 146
Cdd:PRK10938 336 -------KHIG----YVSSSLHLDYRVSTSV---RNviLSGFFdsiGIYqavsdRQQKLAQQWLDILGidkRTA-----D 396
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 147 TPVQFLPIAQRQQVAICRALVADARLVIMDEPTASLtrTEVNQLL--STVNYLKDKGIT-VVFVSHRLEEVKE-ISDRIT 222
Cdd:PRK10938 397 APFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGL--DPLNRQLvrRFVDVLISEGETqLLFVSHHAEDAPAcITHRLE 474

                 ....*
gi 491046221 223 VIRDG 227
Cdd:PRK10938 475 FVPDG 479
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
306-486 4.98e-07

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: 50.57  E-value: 4.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 306 LALSLFGITHPDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDRLTLGAILQQSI------ADNMVISILDRLktpwhlid 379
Cdd:cd03244   46 LLLALFRLVELSSGSILIDGVDIS-KIGLHDLRSRISIIPQDPVLFSGTIRSNLdpfgeySDEELWQALERV-------- 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 380 ekQCQDIVQEWIADLDIKVTDPNNALSTlsgGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLI--------- 450
Cdd:cd03244  117 --GLKEFVESLPGGLDTVVEEGGENLSV---GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIreafkdctv 191
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 491046221 451 ----HRLSGvgisillITDeaseayynCDRILHMKQGSIV 486
Cdd:cd03244  192 ltiaHRLDT-------IID--------SDRILVLDKGRVV 216
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
261-485 5.36e-07

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 51.87  E-value: 5.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 261 NAEDRRTVLEIKNLSRAgqY------RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklkNNT 334
Cdd:PRK09452   7 QPSSLSPLVELRGISKS--FdgkeviSNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI---THV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 335 DAIKRGIGYVsedrltlgaiLQQ-------SIADNmVISILDRLKTPWHLIDEK--------QCQDIVQEWIADLdikvt 399
Cdd:PRK09452  82 PAENRHVNTV----------FQSyalfphmTVFEN-VAFGLRMQKTPAAEITPRvmealrmvQLEEFAQRKPHQL----- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 400 dpnnalstlSGGNQQKVVLAKWILTRPKVLILDSPTVGVDigakdsiYKL-------IHRLS-GVGISILLITDEASEAY 471
Cdd:PRK09452 146 ---------SGGQQQRVAIARAVVNKPKVLLLDESLSALD-------YKLrkqmqneLKALQrKLGITFVFVTHDQEEAL 209
                        250
                 ....*....|....
gi 491046221 472 YNCDRILHMKQGSI 485
Cdd:PRK09452 210 TMSDRIVVMRDGRI 223
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
316-480 5.49e-07

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 50.48  E-value: 5.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 316 PDSGELFIEGKPVkLKNNTDAIKRGIGYVSEDRLTLGailqQSIADNMVISILDRLKTPwhliDEKQCQDIVQEWIADLD 395
Cdd:PRK10247  59 PTSGTLLFEGEDI-STLKPEIYRQQVSYCAQTPTLFG----DTVYDNLIFPWQIRNQQP----DPAIFLDDLERFALPDT 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 396 IkVTDPNNAlstLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYnC 474
Cdd:PRK10247 130 I-LTKNIAE---LSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINH-A 204

                 ....*.
gi 491046221 475 DRILHM 480
Cdd:PRK10247 205 DKVITL 210
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
409-483 6.06e-07

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 51.26  E-value: 6.06e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 409 SGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYAG 238
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
16-216 6.25e-07

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 50.34  E-value: 6.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  16 LRDLSKSFG------GHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVyapddgskieidgksyHRLTPDKArel 89
Cdd:COG2401   27 VAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA----------------LKGTPVAG--- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  90 gvQVIYQDLSLFPNLTVAENIAFELNLKgyfgwfrkkqlreKALEILNEL----AFTIdpDTPVQFLPIAQRQQVAICRA 165
Cdd:COG2401   88 --CVDVPDNQFGREASLIDAIGRKGDFK-------------DAVELLNAVglsdAVLW--LRRFKELSTGQKFRFRLALL 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491046221 166 LVADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRlEEVKE 216
Cdd:COG2401  151 LAERPKLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHH-YDVID 201
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
375-503 9.33e-07

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 50.42  E-value: 9.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 375 WHliDEKQCQDIVQEWIADLD----IKVTDPNNALStLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLI 450
Cdd:PRK14258 117 WR--PKLEIDDIVESALKDADlwdeIKHKIHKSALD-LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLI 193
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 451 HRL---SGVGISILL--------ITDEASEAYYNCDRILHMKQGSIVKEIVTDSINEQQLEEII 503
Cdd:PRK14258 194 QSLrlrSELTMVIVShnlhqvsrLSDFTAFFKGNENRIGQLVEFGLTKKIFNSPHDSRTREYVL 257
cbiO PRK13643
energy-coupling factor transporter ATPase;
282-486 1.07e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 50.50  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 282 DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKrgigyvsEDRLTLGAILQQSIAD 361
Cdd:PRK13643  24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK-------PVRKKVGVVFQFPESQ 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 362 NMVISIL-DRLKTPWHL-IDEKQCQDIVQEWIADLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVD 439
Cdd:PRK13643  97 LFEETVLkDVAFGPQNFgIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491046221 440 IGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
269-502 1.85e-06

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 49.16  E-value: 1.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRAGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGIThPDSGELFIEGKPVK-LKNNTDAIKRgiGYVSEd 347
Cdd:PRK03695   1 MQLNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEaWSAAELARHR--AYLSQ- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 348 rltlgailQQSIADNM-VISILDRlktpwHLIDEKQCQDI--VQEWIADLdIKVTDP-NNALSTLSGGNQQKVVLAKWIL 423
Cdd:PRK03695  77 --------QQTPPFAMpVFQYLTL-----HQPDKTRTEAVasALNEVAEA-LGLDDKlGRSVNQLSGGEWQRVRLAAVVL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 424 -----TRP--KVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKEIVTDSI-N 495
Cdd:PRK03695 143 qvwpdINPagQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVlT 222

                 ....*..
gi 491046221 496 EQQLEEI 502
Cdd:PRK03695 223 PENLAQV 229
cbiO PRK13650
energy-coupling factor transporter ATPase;
312-485 1.99e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 49.34  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 312 GITHPDSGELFIEGKPVKLKNNTDaIKRGIGYVSE--DRLTLGAILQQSIADNmvisiLDRLKTPWHLIDEKQCQDIvqE 389
Cdd:PRK13650  55 GLLEAESGQIIIDGDLLTEENVWD-IRHKIGMVFQnpDNQFVGATVEDDVAFG-----LENKGIPHEEMKERVNEAL--E 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 390 WIADLDIKVTDPnnalSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEAS 468
Cdd:PRK13650 127 LVGMQDFKEREP----ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIrDDYQMTVISITHDLD 202
                        170
                 ....*....|....*..
gi 491046221 469 EAYYNcDRILHMKQGSI 485
Cdd:PRK13650 203 EVALS-DRVLVMKNGQV 218
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
408-488 2.07e-06

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 49.01  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS-GVGISILLITDEASEAyYNCDRILHMKQGSIV 486
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNrEHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQ 225

                 ..
gi 491046221 487 KE 488
Cdd:PRK10584 226 EE 227
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
14-123 2.38e-06

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 50.12  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIdGKSyhrltpdkarelgVQV 93
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT-IKI-GET-------------VKL 389
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 491046221  94 IYQDLS---LFPNLTVAENIA----------FELNLKGYFGWF 123
Cdd:PRK11819 390 AYVDQSrdaLDPNKTVWEEISggldiikvgnREIPSRAYVGRF 432
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
267-486 2.97e-06

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 48.61  E-value: 2.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 267 TVLEIKNLS-RAGQYR---DINLNLKRGEVlglcgllgsgrteLAL-------------SLFGITHPDSGELFIEGKPVK 329
Cdd:PRK13548   1 AMLEARNLSvRLGGRTlldDVSLTLRPGEV-------------VAIlgpngagkstllrALSGELSPDSGEVRLNGRPLA 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 330 lknntdaikrgiGYVSEDRLTLGAILQQSIADNMVISILD--RL-KTPWHLiDEKQCQDIVQEWIADLDIKvtdpnnALS 406
Cdd:PRK13548  68 ------------DWSPAELARRRAVLPQHSSLSFPFTVEEvvAMgRAPHGL-SRAEDDALVAAALAQVDLA------HLA 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 407 -----TLSGGNQQKVVLAKwILT-------RPKVLILDSPTVGVDIGAKDSIYKLIHRL---SGVG-ISILliTDEASEA 470
Cdd:PRK13548 129 grdypQLSGGEQQRVQLAR-VLAqlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLaheRGLAvIVVL--HDLNLAA 205
                        250
                 ....*....|....*.
gi 491046221 471 YYnCDRILHMKQGSIV 486
Cdd:PRK13548 206 RY-ADRIVLLHQGRLV 220
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
281-456 3.10e-06

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: 48.24  E-value: 3.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNtDAIKRGIGYVSEDRLTLGAILQQSIA 360
Cdd:cd03248   31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH-KYLHSKVSLVGQEPVLFARSLQDNIA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 361 DNMVISILDRLKtpwHLIDEKQCQDIVQEWIADLDikvTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDI 440
Cdd:cd03248  110 YGLQSCSFECVK---EAAQKAHAHSFISELASGYD---TEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
                        170       180
                 ....*....|....*....|....*....
gi 491046221 441 GAKDSIYKLI-------------HRLSGV 456
Cdd:cd03248  184 ESEQQVQQALydwperrtvlviaHRLSTV 212
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
408-488 3.31e-06

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: 47.91  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEA-YYNCDRILHMKQGSIV 486
Cdd:cd03217  105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLdYIKPDRVHVLYDGRIV 184

                 ..
gi 491046221 487 KE 488
Cdd:cd03217  185 KS 186
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
408-501 3.54e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 48.93  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIK 245
                         90
                 ....*....|....*.
gi 491046221 488 EIVTDSI--NEQQLEE 501
Cdd:PRK13651 246 DGDTYDIlsDNKFLIE 261
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
408-488 3.79e-06

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 48.21  E-value: 3.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224

                 .
gi 491046221 488 E 488
Cdd:PRK11264 225 Q 225
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
408-488 3.93e-06

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 48.43  E-value: 3.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232

                 .
gi 491046221 488 E 488
Cdd:PRK10619 233 E 233
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
346-505 4.92e-06

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 47.85  E-value: 4.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 346 EDRLTLGAILQQ------SIADNMVISIldRLK--TPWHLIDEKQCQDIVQEWIADlDIKVTDPNNALStLSGGNQQKVV 417
Cdd:PRK14239  83 DLRKEIGMVFQQpnpfpmSIYENVVYGL--RLKgiKDKQVLDEAVEKSLKGASIWD-EVKDRLHDSALG-LSGGQQQRVC 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 418 LAKWILTRPKVLILDSPTVGVD-IGA---KDSIYKLIHRLsgvgiSILLITDEASEAYYNCDRILHMKQGSIV-----KE 488
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDpISAgkiEETLLGLKDDY-----TMLLVTRSMQQASRISDRTGFFLDGDLIeyndtKQ 233
                        170
                 ....*....|....*..
gi 491046221 489 IVTDSINeQQLEEIING 505
Cdd:PRK14239 234 MFMNPKH-KETEDYISG 249
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
269-454 5.29e-06

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 48.95  E-value: 5.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRAgqYR-------DINLNL-KRGEVLGLCGLLGSGRTeLALSLFGITHPDSGELFIEGKPVKLKNNTdAIKRG 340
Cdd:PRK10790 341 IDIDNVSFA--YRddnlvlqNINLSVpSRGFVALVGHTGSGKST-LASLLMGYYPLTEGEIRLDGRPLSSLSHS-VLRQG 416
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 341 IGYVSEDRLTLgailqqsiADNMVISI-LDRLKTP---WHLIDEKQCQDIVQEWIADLDIKVTDPNNalsTLSGGNQQKV 416
Cdd:PRK10790 417 VAMVQQDPVVL--------ADTFLANVtLGRDISEeqvWQALETVQLAELARSLPDGLYTPLGEQGN---NLSVGQKQLL 485
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491046221 417 VLAKWILTRPKVLILDSPTVGVDIGAKDSIYK----------LI---HRLS 454
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQalaavrehttLVviaHRLS 536
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
281-472 5.86e-06

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 47.77  E-value: 5.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELaLSLF-GITHPDSGELFIEGKPVKlknnTDAIKRGIGYVSEdrltlGAILQQSI 359
Cdd:PRK11248  18 EDINLTLESGELLVVLGPSGCGKTTL-LNLIaGFVPYQHGSITLDGKPVE----GPGAERGVVFQNE-----GLLPWRNV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 360 ADNMVISIldRLKTpwhlIDEKQCQDIVQEWIADLDIKVTDpNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVD 439
Cdd:PRK11248  88 QDNVAFGL--QLAG----VEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
                        170       180       190
                 ....*....|....*....|....*....|....
gi 491046221 440 IGAKDSIYKLIHRL-SGVGISILLITDEASEAYY 472
Cdd:PRK11248 161 AFTREQMQTLLLKLwQETGKQVLLITHDIEEAVF 194
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
281-489 7.04e-06

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 47.50  E-value: 7.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPV-KLKNNTDAIKRGigyvsedrLTLGAILQQ-- 357
Cdd:PRK11629  26 HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsKLSSAAKAELRN--------QKLGFIYQFhh 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 358 -----SIADNMVISILDRLKTPwhlideKQCQDIVQEWIADLDIKvTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILD 432
Cdd:PRK11629  98 llpdfTALENVAMPLLIGKKKP------AEINSRALEMLAAVGLE-HRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 433 SPTVGVDIGAKDSIYKLIHRLSGV-GISILLITDEASEAyYNCDRILHMKQGSIVKEI 489
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLA-KRMSRQLEMRDGRLTAEL 227
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
267-487 7.09e-06

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 47.48  E-value: 7.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 267 TVLEIKNLSRAGQYR-------------DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNn 333
Cdd:PRK15112   3 TLLEVRNLSKTFRYRtgwfrrqtveavkPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 334 tdaikrgIGYVSEdRLTLgaILQQ-SIADNMVISILDRLKTPWHLIDEKQCQDIVQEWIADLDIKVTDPNNAL---STLS 409
Cdd:PRK15112  82 -------YSYRSQ-RIRM--IFQDpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASyypHMLA 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 410 GGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGV-GISILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
cbiO PRK13640
energy-coupling factor transporter ATPase;
382-486 7.75e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 47.49  E-value: 7.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 382 QCQDIVQEWIAD---LDIKVTDPNNalstLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVG 457
Cdd:PRK13640 119 EMIKIVRDVLADvgmLDYIDSEPAN----LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNN 194
                         90       100       110
                 ....*....|....*....|....*....|..
gi 491046221 458 ISILLIT---DEASEAyyncDRILHMKQGSIV 486
Cdd:PRK13640 195 LTVISIThdiDEANMA----DQVLVLDDGKLL 222
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
406-486 8.84e-06

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: 46.64  E-value: 8.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 406 STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGvGISILLITDEASeAYYNCDRILHMKQGSI 485
Cdd:cd03369  124 LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLR-TIIDYDKILVMDAGEV 201

                 .
gi 491046221 486 V 486
Cdd:cd03369  202 K 202
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
394-485 9.42e-06

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 48.14  E-value: 9.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 394 LDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIgakDSIYKLIHRLSGVGISILLIT------DEA 467
Cdd:COG0488  139 LGFPEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL---ESIEWLEEFLKNYPGTVLVVShdryflDRV 215
                         90
                 ....*....|....*...
gi 491046221 468 seayynCDRILHMKQGSI 485
Cdd:COG0488  216 ------ATRILELDRGKL 227
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
408-487 9.74e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 47.32  E-value: 9.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVD-IGAK---DSIYKLiHRLSgvGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDpKGRKemmEMFYKL-HKEK--GLTTVLVTHSMEDAARYADQIVVMHKG 222

                 ....
gi 491046221 484 SIVK 487
Cdd:PRK13634 223 TVFL 226
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
312-486 9.93e-06

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


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 46.72  E-value: 9.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 312 GITHPDSGELFIEG----------KPVKL---KNNTDA---IKRGIGYVSEDRLTLGAILQQSIAdnmviSILDRLKtpw 375
Cdd:cd03298   46 GFETPQSGRVLINGvdvtaappadRPVSMlfqENNLFAhltVEQNVGLGLSPGLKLTAEDRQAIE-----VALARVG--- 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 376 hlidekqcqdivqewIADLDIKVTDpnnalsTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-S 454
Cdd:cd03298  118 ---------------LAGLEKRLPG------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhA 176
                        170       180       190
                 ....*....|....*....|....*....|..
gi 491046221 455 GVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:cd03298  177 ETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
281-486 1.26e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 46.92  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklknntDAIKRGIGYVSEDRLTLGAILQQSI- 359
Cdd:PRK13638  18 KGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL------DYSKRGLLALRQQVATVFQDPEQQIf 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 360 ---ADNMVISILDRLKTPwhlidEKQCQDIVQEWIADLDIKVTDpNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTV 436
Cdd:PRK13638  92 ytdIDSDIAFSLRNLGVP-----EAEITRRVDEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 491046221 437 GVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
281-497 1.28e-05

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 46.90  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDRLTLGAI-LQQSI 359
Cdd:PRK10253  24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ-HYASKEVARRIGLLAQNATTPGDItVQELV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 360 ADNMVISilDRLKTPWHLIDEKQCQDIVQEW-IADLDIKVTDpnnalsTLSGGNQQKVVLAKWILTRPKVLILDSPTVGV 438
Cdd:PRK10253 103 ARGRYPH--QPLFTRWRKEDEEAVTKAMQATgITHLADQSVD------TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 439 DIGAKDSIYKLIHRLSGV-GISILLITDEASEAYYNCDRILHMKQGSIV-----KEIVTDSINEQ 497
Cdd:PRK10253 175 DISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVaqgapKEIVTAELIER 239
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
316-486 1.39e-05

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: 46.38  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 316 PDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDRltlgAILQQSIADNMVISILDRlktpwhlIDEKQCQDIVQEWIADLD 395
Cdd:cd03249   55 PTSGEILLDGVDIR-DLNLRWLRSQIGLVSQEP----VLFDGTIAENIRYGKPDA-------TDEEVEEAAKKANIHDFI 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 396 IKVTDPNNAL-----STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSgVGISILLITDEASeA 470
Cdd:cd03249  123 MSLPDGYDTLvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLS-T 200
                        170
                 ....*....|....*.
gi 491046221 471 YYNCDRILHMKQGSIV 486
Cdd:cd03249  201 IRNADLIAVLQNGQVV 216
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
344-494 1.44e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 46.63  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 344 VSEDRLTLGAILQQ------SIADNMVISILDRlktpwHLIDEKQCQDIVQEWIADLDI--KVTDP-NNALSTLSGGNQQ 414
Cdd:PRK14271  96 VLEFRRRVGMLFQRpnpfpmSIMDNVLAGVRAH-----KLVPRKEFRGVAQARLTEVGLwdAVKDRlSDSPFRLSGGQQQ 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 415 KVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGvGISILLITDEASEAYYNCDRILHMKQGSIVKEIVTDSI 494
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD-RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
398-488 1.78e-05

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 46.66  E-value: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 398 VTDPNNALST----LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS-GVGISILLITDEASEAYY 472
Cdd:PRK11022 140 IPDPASRLDVyphqLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAE 219
                         90
                 ....*....|....*.
gi 491046221 473 NCDRILHMKQGSIVKE 488
Cdd:PRK11022 220 AAHKIIVMYAGQVVET 235
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
269-485 2.03e-05

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 46.76  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS--RAGQ--YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTdAIKRGIGYV 344
Cdd:PRK09536   4 IDVSDLSveFGDTtvLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR-AASRRVASV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 345 SEDrltlgailqQSIADNM-VISILDRLKTPwHL--IDEKQCQD--IVQEWIADLDI-KVTDpnNALSTLSGGNQQKVVL 418
Cdd:PRK09536  83 PQD---------TSLSFEFdVRQVVEMGRTP-HRsrFDTWTETDraAVERAMERTGVaQFAD--RPVTSLSGGERQRVLL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 419 AKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISIL-LITDEASEAYYnCDRILHMKQGSI 485
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVaAIHDLDLAARY-CDELVLLADGRV 217
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
358-487 2.03e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 45.99  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 358 SIADNMVISI-LDRLKTPWHLIDEkqcqdiVQEWI---ADLDIKVTDP-NNALSTLSGGNQQKVVLAKWILTRPKVLILD 432
Cdd:PRK14267 101 TIYDNVAIGVkLNGLVKSKKELDE------RVEWAlkkAALWDEVKDRlNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 433 SPTVGVDIGAKDSIYKLIHRLSGvGISILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
7-179 2.10e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 47.43  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   7 ADKSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS-KI---EIDgksyhrlt 82
Cdd:NF033858 260 DDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEaWLfgqPVD-------- 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  83 pdkARELGV--QVIY--QDLSLFPNLTVAENIafELNLKGYfgwfrkkQL-REKALEILNELA--FTIDP--DTPVQFLP 153
Cdd:NF033858 332 ---AGDIATrrRVGYmsQAFSLYGELTVRQNL--ELHARLF-------HLpAAEIAARVAEMLerFDLADvaDALPDSLP 399
                        170       180
                 ....*....|....*....|....*...
gi 491046221 154 --IAQRQQVAIcrALVADARLVIMDEPT 179
Cdd:NF033858 400 lgIRQRLSLAV--AVIHKPELLILDEPT 425
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
408-477 2.14e-05

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 46.44  E-value: 2.14e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGV-GISILLITDEASEAYYNCDRI 477
Cdd:COG4170  159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLISHDLESISQWADTI 229
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
400-440 2.21e-05

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 47.25  E-value: 2.21e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 491046221 400 DPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDI 440
Cdd:PRK11147 149 DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI 189
cbiO PRK13649
energy-coupling factor transporter ATPase;
408-487 2.22e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 46.28  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVL 225
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
316-486 2.44e-05

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 46.70  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 316 PDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDrltlGAILQQSIADNMVISILDrlktpwhlIDEKQCQDIVQ-----EW 390
Cdd:COG1132  392 PTSGRILIDGVDIR-DLTLESLRRQIGVVPQD----TFLFSGTIRENIRYGRPD--------ATDEEVEEAAKaaqahEF 458
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 391 IADLdikvtdPN--NAL-----STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGA----KDSIYKLI--------- 450
Cdd:COG1132  459 IEAL------PDgyDTVvgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETealiQEALERLMkgrttivia 532
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 491046221 451 HRLSgvgiSILlitdeaseayyNCDRILHMKQGSIV 486
Cdd:COG1132  533 HRLS----TIR-----------NADRILVLDDGRIV 553
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
258-485 2.61e-05

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 46.89  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 258 PPNNAEDRRTVLEIKNLSRAgqYRD-------INLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKL 330
Cdd:PRK10522 312 PRPQAFPDWQTLELRNVTFA--YQDngfsvgpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 331 kNNTDAIKRGIGYVSEDrltlgailqqsiadnmvISILDRLKTPwhlidEKQCQD--IVQEWIADLDI--KVTDPNNALS 406
Cdd:PRK10522 390 -EQPEDYRKLFSAVFTD-----------------FHLFDQLLGP-----EGKPANpaLVEKWLERLKMahKLELEDGRIS 446
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 407 T--LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIY-KLIHRLSGVGISILLITDEasEAYY-NCDRILHMKQ 482
Cdd:PRK10522 447 NlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYqVLLPLLQEMGKTIFAISHD--DHYFiHADRLLEMRN 524

                 ...
gi 491046221 483 GSI 485
Cdd:PRK10522 525 GQL 527
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
26-221 3.71e-05

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: 44.24  E-value: 3.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  26 HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTisGVYAPddgskieidgksyhrltpdkarelGVQVIYQDLSLFPnlt 105
Cdd:cd03238    8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNE--GLYAS------------------------GKARLISFLPKFS--- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 106 vaeniafelnlkgyfgwfRKKQLREKALEILNELAFT-IDPDTPVQFLPIAQRQQVAICRALVADAR--LVIMDEPTASL 182
Cdd:cd03238   59 ------------------RNKLIFIDQLQFLIDVGLGyLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL 120
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491046221 183 TRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEiSDRI 221
Cdd:cd03238  121 HQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWI 158
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
408-492 3.95e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 45.61  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
                         90
                 ....*....|
gi 491046221 488 -----EIVTD 492
Cdd:PRK13631 257 tgtpyEIFTD 266
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
384-486 5.01e-05

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 45.00  E-value: 5.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 384 QDIVQEWIADLDIkVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLI 463
Cdd:PRK11231 116 NARVNQAMEQTRI-NHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTV 194
                         90       100
                 ....*....|....*....|...
gi 491046221 464 TDEASEAYYNCDRILHMKQGSIV 486
Cdd:PRK11231 195 LHDLNQASRYCDHLVVLANGHVM 217
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
1-241 5.25e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 45.50  E-value: 5.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   1 MTSTSKADKSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCG--KSTLIKTISGvyaPDDGSKieidgkSY 78
Cdd:NF000106   1 MTRKTISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRR------PW 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  79 HRLTPDKARelgvQVIYQDLSLFPNLTVAENIAFE----LNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPI 154
Cdd:NF000106  72 RF*TWCANR----RALRRTIG*HRPVR*GRRESFSgrenLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 155 AQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWP 234
Cdd:NF000106 148 GMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227

                 ....*..
gi 491046221 235 AEGLTTR 241
Cdd:NF000106 228 VDELKTK 234
cbiO PRK13641
energy-coupling factor transporter ATPase;
380-493 6.02e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 44.82  E-value: 6.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 380 EKQCQDIVQEWIADLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGIS 459
Cdd:PRK13641 118 EDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHT 197
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 491046221 460 ILLITDEASEAYYNCDRILHMKQGSIVK-----EIVTDS 493
Cdd:PRK13641 198 VILVTHNMDDVAEYADDVLVLEHGKLIKhaspkEIFSDK 236
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
79-221 6.38e-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: 45.77  E-value: 6.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   79 HRLTPDKareLGVQVIYQDLSLFPNLTVAENIAF--ELNLKGyfgwfRKKQLREKAL-EILNELAFTID-------PDTP 148
Cdd:TIGR00630 414 TRLKPEA---LAVTVGGKSIADVSELSIREAHEFfnQLTLTP-----EEKKIAEEVLkEIRERLGFLIDvgldylsLSRA 485
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221  149 VQFLPIAQRQQVAICRALvaDARLV----IMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRlEEVKEISDRI 221
Cdd:TIGR00630 486 AGTLSGGEAQRIRLATQI--GSGLTgvlyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAADYV 559
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
406-488 7.47e-05

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 44.79  E-value: 7.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 406 STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKL---IHRLsgVGISILLITDEASEAYYNCDRILHMKQ 482
Cdd:PRK11153 139 AQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELlkdINRE--LGLTIVLITHEMDVVKRICDRVAVIDA 216

                 ....*.
gi 491046221 483 GSIVKE 488
Cdd:PRK11153 217 GRLVEQ 222
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
281-497 7.78e-05

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: 44.56  E-value: 7.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPvklknntdaikrgIGYVSEDRLTlgAILQQSIA 360
Cdd:cd03294   41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQD-------------IAAMSRKELR--ELRRKKIS 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 361 dnMVI---------SILDRLKTPWHL--IDEKQCQDIVQEWIADLDIKvTDPNNALSTLSGGNQQKVVLAKWILTRPKVL 429
Cdd:cd03294  106 --MVFqsfallphrTVLENVAFGLEVqgVPRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDIL 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 430 ILDSPTVGVDIGAKDSIYKLIHRLSG-VGISILLITDEASEAYYNCDRILHMKQGSIV-----KEIVTDSINEQ 497
Cdd:cd03294  183 LMDEAFSALDPLIRREMQDELLRLQAeLQKTIVFITHDLDEALRLGDRIAIMKDGRLVqvgtpEEILTNPANDY 256
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
404-497 7.94e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 44.73  E-value: 7.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 404 ALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:NF000106 141 AAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRG 220
                         90
                 ....*....|....
gi 491046221 484 SIVKEIVTDSINEQ 497
Cdd:NF000106 221 RVIADGKVDELKTK 234
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
375-486 8.25e-05

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 45.22  E-value: 8.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 375 WHLIDEKQCQDIVQEWIADLDIKVTDPNnalSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS 454
Cdd:PRK11174 456 QQALENAWVSEFLPLLPQGLDTPIGDQA---AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS 532
                         90       100       110
                 ....*....|....*....|....*....|..
gi 491046221 455 GvGISILLITDEAsEAYYNCDRILHMKQGSIV 486
Cdd:PRK11174 533 R-RQTTLMVTHQL-EDLAQWDQIWVMQDGQIV 562
PLN03232 PLN03232
ABC transporter C family member; Provisional
44-260 8.56e-05

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 45.35  E-value: 8.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   44 LAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELgVQVIYQDLSLFPNlTVAENI-AF-ELNLKGYFG 121
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKG-RIMIDDCDVAKFGLTDLRRV-LSIIPQSPVLFSG-TVRFNIdPFsEHNDADLWE 1343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  122 WFRKKQLREkaleILNELAFTIDPDTPV--QFLPIAQRQQVAICRALVADARLVIMDEPTASLTrTEVNQLLSTVNYLKD 199
Cdd:PLN03232 1344 ALERAHIKD----VIDRNPFGLDAEVSEggENFSVGQRQLLSLARALLRRSKILVLDEATASVD-VRTDSLIQRTIREEF 1418
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221  200 KGITVVFVSHRLEEVKEiSDRITVIRDGQKIGTWPAEGLTTRKITELMTgldIVHERKPPN 260
Cdd:PLN03232 1419 KSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFR---MVHSTGPAN 1475
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
281-481 8.92e-05

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 44.49  E-value: 8.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVK--LKNNTdaikrgIGYV--SEDRLTLGAILQ 356
Cdd:PRK15056  24 RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqaLQKNL------VAYVpqSEEVDWSFPVLV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 357 QSIAdnmvisILDRL-KTPWHLIDEKQCQDIVQEWIADLDIkVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPT 435
Cdd:PRK15056  98 EDVV------MMGRYgHMGWLRRAKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 491046221 436 VGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMK 481
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
402-488 9.37e-05

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: 43.07  E-value: 9.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 402 NNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLI-------------HRLSGVgisillitdeas 468
Cdd:cd03247   93 NNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIfevlkdktliwitHHLTGI------------ 160
                         90       100
                 ....*....|....*....|
gi 491046221 469 eayYNCDRILHMKQGSIVKE 488
Cdd:cd03247  161 ---EHMDKILFLENGKIIMQ 177
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
401-463 1.01e-04

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: 43.08  E-value: 1.01e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 401 PNNALSTLSGGNQQKVVLAKWILTRPK--VLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLI 463
Cdd:cd03238   81 LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILI 145
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
408-492 1.01e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 43.96  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIV- 486
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLa 218

                 ....*....
gi 491046221 487 ---KEIVTD 492
Cdd:PRK13647 219 egdKSLLTD 227
PLN03140 PLN03140
ABC transporter G family member; Provisional
29-245 1.27e-04

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 44.84  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGvyaPDDGSKIEIDGK--SYHRLTPDKARELGVqvIYQDLSLFPNLTV 106
Cdd:PLN03140  896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRisGFPKKQETFARISGY--CEQNDIHSPQVTV 970
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  107 AENIAFE--LNLKGYFGWFRKKQLREKALEI--LNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASL 182
Cdd:PLN03140  971 RESLIYSafLRLPKEVSKEEKMMFVDEVMELveLDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221  183 TRTEVNQLLSTVNYLKDKGITVVFVSHRLE-EVKEISDRITVI-RDGQKIGTWPAeGLTTRKITE 245
Cdd:PLN03140 1051 DARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMkRGGQVIYSGPL-GRNSHKIIE 1114
cbiO PRK13645
energy-coupling factor transporter ATPase;
408-486 1.58e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 43.46  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS-GVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
393-484 2.06e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 44.43  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  393 DLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPK--VLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLIT-DEASE 469
Cdd:PRK00635  462 DLGLPYLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEhDEQMI 541
                          90
                  ....*....|....*
gi 491046221  470 AYynCDRILHMKQGS 484
Cdd:PRK00635  542 SL--ADRIIDIGPGA 554
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
172-215 2.34e-04

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: 43.85  E-value: 2.34e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 491046221  172 LVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVK 215
Cdd:TIGR00630 853 LYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIK 896
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
405-483 2.49e-04

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: 41.28  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 405 LSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGvgiSILLIT------DEAseayynCDRIL 478
Cdd:cd03221   68 FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG---TVILVShdryflDQV------ATKII 138

                 ....*
gi 491046221 479 HMKQG 483
Cdd:cd03221  139 ELEDG 143
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
406-455 2.57e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 43.86  E-value: 2.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 491046221  406 STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG 455
Cdd:PTZ00265  578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKG 627
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
316-486 2.96e-04

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 43.41  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 316 PDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDRLtlgaILQQSIADNMVISILDRLKTPWHLIDEK-QCQDIVQEWIADL 394
Cdd:PRK13657 387 PQSGRILIDGTDIR-TVTRASLRRNIAVVFQDAG----LFNRSIEDNIRVGRPDATDEEMRAAAERaQAHDFIERKPDGY 461
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 395 DIKVTDPNNALStlsGGNQQKVVLAKWILTRPKVLILDSPTVGVDI-------GAKDSIYK------LIHRLSGVgisil 461
Cdd:PRK13657 462 DTVVGERGRQLS---GGERQRLAIARALLKDPPILILDEATSALDVeteakvkAALDELMKgrttfiIAHRLSTV----- 533
                        170       180
                 ....*....|....*....|....*
gi 491046221 462 litdeaseayYNCDRILHMKQGSIV 486
Cdd:PRK13657 534 ----------RNADRILVFDNGRVV 548
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
269-486 3.38e-04

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 42.76  E-value: 3.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS-----RAGQY---RDINLNLKRGEVlglcgllgsgrtelalslFGI---------T---------HPDSGELF 322
Cdd:COG1135    2 IELENLSktfptKGGPVtalDDVSLTIEKGEI------------------FGIigysgagksTlircinlleRPTSGSVL 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 323 IEGKPVKLKNNTD--AIKRGIGYvsedrltlgaILQQ-------SIADN----MVISILDRLKtpwhlIDEKqcqdiVQE 389
Cdd:COG1135   64 VDGVDLTALSERElrAARRKIGM----------IFQHfnllssrTVAENvalpLEIAGVPKAE-----IRKR-----VAE 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 390 wIADLdikV--TDPNNAL-STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLI----HRLsgvGISILL 462
Cdd:COG1135  124 -LLEL---VglSDKADAYpSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLkdinREL---GLTIVL 196
                        250       260
                 ....*....|....*....|....*..
gi 491046221 463 ITDEAS---EAyynCDRILHMKQGSIV 486
Cdd:COG1135  197 ITHEMDvvrRI---CDRVAVLENGRIV 220
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
267-469 3.60e-04

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 42.44  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 267 TVLEIKNLS-RAGQ---YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGkpvklkNNTDAIKRGIG 342
Cdd:PRK11831   6 NLVDMRGVSfTRGNrciFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG------ENIPAMSRSRL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 343 YVSEDRLTLgaiLQQSIADNMVISILDRLKtpWHLIDEKQCQDIVQEWIADLDIKVTDPNNAL----STLSGGNQQKVVL 418
Cdd:PRK11831  80 YTVRKRMSM---LFQSGALFTDMNVFDNVA--YPLREHTQLPAPLLHSTVMMKLEAVGLRGAAklmpSELSGGMARRAAL 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491046221 419 AKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASE 469
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPE 206
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
11-68 3.78e-04

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 43.23  E-value: 3.78e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221  11 DPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDG 68
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG 367
PLN03232 PLN03232
ABC transporter C family member; Provisional
375-487 4.10e-04

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 43.43  E-value: 4.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  375 WHLIDEKQCQDIVQEWIADLDIKVTDPNNALSTlsgGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIhRLS 454
Cdd:PLN03232 1342 WEALERAHIKDVIDRNPFGLDAEVSEGGENFSV---GQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTI-REE 1417
                          90       100       110
                  ....*....|....*....|....*....|...
gi 491046221  455 GVGISILLITDEASeAYYNCDRILHMKQGSIVK 487
Cdd:PLN03232 1418 FKSCTMLVIAHRLN-TIIDCDKILVLSSGQVLE 1449
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
359-468 4.24e-04

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


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 42.81  E-value: 4.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  359 IADNMVISILDRLKTPwHLIDEKQCQDIVQEWiadldikvtdpnnaLSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGV 438
Cdd:TIGR00954 549 LSDKDLEQILDNVQLT-HILEREGGWSAVQDW--------------MDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
                          90       100       110
                  ....*....|....*....|....*....|
gi 491046221  439 DIGAKDSIYKLIHRlsgVGISILLITDEAS 468
Cdd:TIGR00954 614 SVDVEGYMYRLCRE---FGITLFSVSHRKS 640
ycf16 CHL00131
sulfate ABC transporter protein; Validated
409-487 4.30e-04

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 41.94  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 409 SGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLIT------DeaseaYYNCDRILHMKQ 482
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILIThyqrllD-----YIKPDYVHVMQN 227

                 ....*
gi 491046221 483 GSIVK 487
Cdd:CHL00131 228 GKIIK 232
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
281-488 4.87e-04

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: 41.83  E-value: 4.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEG---KPVKLKNntdaIKRGIGYVSEDRLtlgaILQQ 357
Cdd:cd03251   19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLAS----LRRQIGLVSQDVF----LFND 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 358 SIADNMVISILDrlktpwhlIDEKQCQDIVQ-----EWIADL----DIKVTDPNnalSTLSGGNQQKVVLAKWILTRPKV 428
Cdd:cd03251   91 TVAENIAYGRPG--------ATREEVEEAARaanahEFIMELpegyDTVIGERG---VKLSGGQRQRIAIARALLKDPPI 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 429 LILDSPTVGVDIGAKDSIYKLIHRLSgVGISILLITDEASeAYYNCDRILHMKQGSIVKE 488
Cdd:cd03251  160 LILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLS-TIENADRIVVLEDGKIVER 217
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
407-484 4.89e-04

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: 43.08  E-value: 4.89e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221   407 TLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGS 484
Cdd:TIGR01257 2070 TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGA 2147
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
252-450 5.43e-04

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: 43.01  E-value: 5.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   252 IVHERKPPNNAEDRRTVlEIKNLS---RAGQ---YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEG 325
Cdd:TIGR00957 1269 QIQETAPPSGWPPRGRV-EFRNYClryREDLdlvLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG 1347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   326 KPVKlKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDrlktPWHLIDEKQCQDIVQEWIADLDIKVTDPNNAL 405
Cdd:TIGR00957 1348 LNIA-KIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEE----VWWALELAHLKTFVSALPDKLDHECAEGGENL 1422
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 491046221   406 STlsgGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLI 450
Cdd:TIGR00957 1423 SV---GQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI 1464
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
408-496 5.79e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 41.82  E-value: 5.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGvGISILLITDEASEAYYNCDRILHMKQGSIV- 486
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFPQQAARISDYVAFLYKGQIVe 225
                         90
                 ....*....|....
gi 491046221 487 ----KEIVTDSINE 496
Cdd:PRK14247 226 wgptREVFTNPRHE 239
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
38-227 6.40e-04

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: 40.43  E-value: 6.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221    38 KGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEIDGKSYHRLTPDKARELGVQVIYQDLSlfpnltvaeniafelnlk 117
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS------------------ 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   118 gyfgwfrkkqlREKALEILNELAFTIDPDtpvqflpiaqrqqvaicralvadarLVIMDEPTASLTRTEVNQLLSTV--- 194
Cdd:smart00382  63 -----------GELRLRLALALARKLKPD-------------------------VLILDEITSLLDAEQEALLLLLEelr 106
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 491046221   195 ---NYLKDKGITVVFVSHRLEEVKE-----ISDRITVIRDG 227
Cdd:smart00382 107 lllLLKSEKNLTVILTTNDEKDLGPallrrRFDRRIVLLLI 147
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
406-486 8.92e-04

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 42.02  E-value: 8.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 406 STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDE---ASEAyyncDRILHMKQ 482
Cdd:PRK10535 143 SQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDpqvAAQA----ERVIEIRD 218

                 ....
gi 491046221 483 GSIV 486
Cdd:PRK10535 219 GEIV 222
PLN03130 PLN03130
ABC transporter C family member; Provisional
29-227 9.60e-04

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 42.03  E-value: 9.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEIDGKsyhrltpdkarelgVQVIYQdLSLFPNLTVAE 108
Cdd:PLN03130  633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGT--------------VAYVPQ-VSWIFNATVRD 697
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  109 NIAF--ELNLKGYFGWFRKKQLREKaLEILNELAFTIDPDTPVQfLPIAQRQQVAICRALVADARLVIMDEPTASLTRTE 186
Cdd:PLN03130  698 NILFgsPFDPERYERAIDVTALQHD-LDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 491046221  187 VNQLLSTVnyLKD--KGITVVFVSHRLEEVKEIsDRITVIRDG 227
Cdd:PLN03130  776 GRQVFDKC--IKDelRGKTRVLVTNQLHFLSQV-DRIILVHEG 815
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
27-112 1.16e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 40.24  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIeidgksYHRLTPDKARELGVQVIYQDLSLFPNLTV 106
Cdd:PRK13541  14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIY------YKNCNINNIAKPYCTYIGHNLGLKLEMTV 87

                 ....*.
gi 491046221 107 AENIAF 112
Cdd:PRK13541  88 FENLKF 93
PLN03130 PLN03130
ABC transporter C family member; Provisional
309-486 1.20e-03

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 41.65  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  309 SLFGITHPDSGELFIEGkpvklknnTDAIKRGIgyvSEDRLTLGAILQQSIADNMVISI-LDRLKTP-----WHLIDEKQ 382
Cdd:PLN03130 1284 ALFRIVELERGRILIDG--------CDISKFGL---MDLRKVLGIIPQAPVLFSGTVRFnLDPFNEHndadlWESLERAH 1352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  383 CQDIVQEWIADLDIKVTDpnnALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLI------------ 450
Cdd:PLN03130 1353 LKDVIRRNSLGLDAEVSE---AGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIreefksctmlii 1429
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 491046221  451 -HRLSgvgisilLITDeaseayynCDRILHMKQGSIV 486
Cdd:PLN03130 1430 aHRLN-------TIID--------CDRILVLDAGRVV 1451
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
377-435 1.82e-03

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: 40.69  E-value: 1.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  377 LIDEK-QCQDIVQEWIA-DLDIKVTDPNNAL---------STLSGGNQQKVVLAKWILTRPKVLILDSPT 435
Cdd:TIGR03719 120 LAAEQaELQEIIDAADAwDLDSQLEIAMDALrcppwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPT 189
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
406-486 1.91e-03

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 40.63  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 406 STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG-VGISILLITDEASEAYYNCDRILHMKQGS 484
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAReINIPILYVSHSLDEILRLADRVVVLEQGK 206

                 ..
gi 491046221 485 IV 486
Cdd:PRK11144 207 VK 208
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
407-450 2.13e-03

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 40.78  E-value: 2.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 491046221  407 TLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLI 450
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
24-221 2.42e-03

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 38.88  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  24 GGHR-ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYapddgskieidGKSYHRLTPDKARELGVQVIYQDLSLFp 102
Cdd:cd03227    5 GRFPsYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLAL-----------GGAQSATRRRSGVKAGCIVAAVSAELI- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 103 nltvaeniafelnlkgyfgwFRKKQLrEKALEILNELAFtidpdtpvqflpiaqrqQVAIcrALVADARLVIMDEPTASL 182
Cdd:cd03227   73 --------------------FTRLQL-SGGEKELSALAL-----------------ILAL--ASLKPRPLYILDEIDRGL 112
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491046221 183 TRTEVNQLLSTVNYLKDKGITVVFVSHRlEEVKEISDRI 221
Cdd:cd03227  113 DPRDGQALAEAILEHLVKGAQVIVITHL-PELAELADKL 150
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
154-227 3.09e-03

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 39.51  E-value: 3.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 154 IAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTV-NYLKDKgiTVVFVSHRLEEVKEiSDRITVIRDG 227
Cdd:cd03288  159 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVmTAFADR--TVVTIAHRVSTILD-ADLVLVLSRG 230
COG4637 COG4637
Predicted ATPase [General function prediction only];
27-56 3.58e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 39.53  E-value: 3.58e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 491046221  27 RALRNIDLTLnkGEVHCLAGTNGCGKSTLI 56
Cdd:COG4637   11 KSLRDLELPL--GPLTVLIGANGSGKSNLL 38
GguA NF040905
sugar ABC transporter ATP-binding protein;
29-247 4.06e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 39.77  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISG-VYAPDDGSKIEIDGKSYHRLTPDKARELGVQVIYQD---LSLfpNL 104
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrSYGRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDrkgYGL--NL 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 105 --TVAENIAFElNLKGY--FGW------------FRKKqLREKALEIlnelaftidpDTPVQFLPIAQRQQVAICRALVA 168
Cdd:NF040905 354 idDIKRNITLA-NLGKVsrRGVideneeikvaeeYRKK-MNIKTPSV----------FQKVGNLSGGNQQKVVLSKWLFT 421
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 169 DARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELM 247
Cdd:NF040905 422 DPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQERIMRLI 500
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
113-230 4.31e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 39.81  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  113 ELNLKGYFGWFRKKQLREKAL-EIL----NELAFTID-------PDTPVQFLPIAQRQQVAICRALVADARLV--IMDEP 178
Cdd:PRK00635  426 QMSLQELFIFLSQLPSKSLSIeEVLqglkSRLSILIDlglpyltPERALATLSGGEQERTALAKHLGAELIGItyILDEP 505
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 491046221  179 TASLTRTEVNQLLSTVNYLKDKGITVVFVSHRlEEVKEISDRITVIRDGQKI 230
Cdd:PRK00635  506 SIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRIIDIGPGAGI 556
PLN03211 PLN03211
ABC transporter G-25; Provisional
402-483 4.36e-03

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 39.86  E-value: 4.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 402 NNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKdsiYKLIHRLSGV---GISILL-ITDEASEAYYNCDRI 477
Cdd:PLN03211 201 NSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA---YRLVLTLGSLaqkGKTIVTsMHQPSSRVYQMFDSV 277

                 ....*.
gi 491046221 478 LHMKQG 483
Cdd:PLN03211 278 LVLSEG 283
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
408-494 4.61e-03

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 39.40  E-value: 4.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS-GVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238

                 ....*...
gi 491046221 487 KEIVTDSI 494
Cdd:PRK15093 239 ETAPSKEL 246
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
14-75 4.65e-03

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: 38.32  E-value: 4.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221  14 ITLRDLSKSFGGHRALRNIDlTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDG 75
Cdd:cd03222    1 QLYPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD-NDEWDG 60
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
407-463 4.96e-03

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: 39.61  E-value: 4.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221  407 TLSGGNQQKVVLAKWILTR---PKVLILDSPTVGVDIgakDSIYKL---IHRLSGVGISILLI 463
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHF---DDIKKLlevLQRLVDKGNTVVVI 888
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
172-215 5.04e-03

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


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 38.75  E-value: 5.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVK 215
Cdd:cd03271  193 LYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK 236
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
27-139 5.89e-03

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


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 38.83  E-value: 5.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221  27 RALRNIDLTLNKGE-VHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEIDGKSY-------------------HRLTPDKA 86
Cdd:COG3950   12 RGFEDLEIDFDNPPrLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLlirngefgdsaklilyygtSRLLLDGP 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491046221  87 RELGVQVIYQDLSLFPNLtvAENIAFELNLKGYFGWFR--KKQLREKALEILNEL 139
Cdd:COG3950   92 LKKLERLKEEYFSRLDGY--DSLLDEDSNLREFLEWLReyLEDLENKLSDELDEK 144
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
375-496 6.03e-03

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 39.51  E-value: 6.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221   375 WHLIDEKQCQDIVQEWIADLDIKVTDPNnalSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYK-LIHRL 453
Cdd:TIGR01271 1324 WKVAEEVGLKSVIEQFPDKLDFVLVDGG---YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKtLKQSF 1400
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 491046221   454 SGVGIsilLITDEASEAYYNCDRILhMKQGSIVKEIvtDSINE 496
Cdd:TIGR01271 1401 SNCTV---ILSEHRVEALLECQQFL-VIEGSSVKQY--DSIQK 1437
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
281-484 7.37e-03

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: 38.30  E-value: 7.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKpvklknntdaikrgIGYVSEdrltLGAILQQSIA 360
Cdd:cd03291   54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQ----FSWIMPGTIK 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 361 DNMVISIldrlktpwhLIDEKQCQDIVQEWIADLDI-KVTDPNNALS-----TLSGGNQQKVVLAKWILTRPKVLILDSP 434
Cdd:cd03291  116 ENIIFGV---------SYDEYRYKSVVKACQLEEDItKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSP 186
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491046221 435 TVGVDIGAKDSIY-KLIHRLSGVGISILLITDeaSEAYYNCDRILHMKQGS 484
Cdd:cd03291  187 FGYLDVFTEKEIFeSCVCKLMANKTRILVTSK--MEHLKKADKILILHEGS 235
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
403-470 7.96e-03

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 38.22  E-value: 7.96e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 403 NALStLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLsGVGISILLITDEASEA 470
Cdd:PRK14243 148 SGLS-LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQA 213
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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