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Conserved domains on  [gi|446457991|ref|WP_000535845|]
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ABC transporter ATP-binding protein [Staphylococcus argenteus]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11438919)

ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ATP transporter complex responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of substrates, similar to Escherichia coli polysialic acid transport ATP-binding protein KpsT, an energy coupling component for the transport of polysialic acid across the cytoplasmic membrane

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TagH super family cl43337
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
37-236 4.42e-14

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


The actual alignment was detected with superfamily member COG1134:

Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 72.04  E-value: 4.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVCTedlfyGYIedQALI------------HQTVETYtA 104
Cdd:COG1134   42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN-----GRV--SALLelgagfhpeltgRENIYLN-G 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991 105 QLIQLFPYEInDHKAEQIIQYAHLGEYKKKPVNQISKAAYAQLLLSIARSSKSNIIILNHVI---DylpPQFMERAIELT 181
Cdd:COG1134  114 RLLGLSRKEI-DEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLavgD---AAFQKKCLARI 189
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446457991 182 NDYIENNLTIVTIGDDVDKIAQVSNYIAWFSHGQLRMEGSLKQVIPLFKEHERDR 236
Cdd:COG1134  190 RELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAYEALLAGR 244
 
Name Accession Description Interval E-value
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
37-236 4.42e-14

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 72.04  E-value: 4.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVCTedlfyGYIedQALI------------HQTVETYtA 104
Cdd:COG1134   42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN-----GRV--SALLelgagfhpeltgRENIYLN-G 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991 105 QLIQLFPYEInDHKAEQIIQYAHLGEYKKKPVNQISKAAYAQLLLSIARSSKSNIIILNHVI---DylpPQFMERAIELT 181
Cdd:COG1134  114 RLLGLSRKEI-DEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLavgD---AAFQKKCLARI 189
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446457991 182 NDYIENNLTIVTIGDDVDKIAQVSNYIAWFSHGQLRMEGSLKQVIPLFKEHERDR 236
Cdd:COG1134  190 RELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAYEALLAGR 244
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
37-220 1.09e-13

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 70.25  E-value: 1.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVCTED----LFYGYIEDQALihqTVE---TYTAQLIQL 109
Cdd:cd03220   38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsslLGLGGGFNPEL---TGReniYLNGRLLGL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991 110 FPYEInDHKAEQIIQYAHLGEYKKKPVNQISKAAYAQLLLSIARSSKSNIIILNHVI---DylpPQFMERAIELTNDYIE 186
Cdd:cd03220  115 SRKEI-DEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLavgD---AAFQEKCQRRLRELLK 190
                        170       180       190
                 ....*....|....*....|....*....|....
gi 446457991 187 NNLTIVTIGDDVDKIAQVSNYIAWFSHGQLRMEG 220
Cdd:cd03220  191 QGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
1-256 1.95e-10

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 61.37  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991   1 MGSSIVLKllKVTHYYR----NKQN-KKWYLPFGYDAEDIDLNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDK 75
Cdd:PRK13546   1 MNVSVNIK--NVTKEYRiyrtNKERmKDALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  76 GKVVCTEDL----FYGYIEDQALIHQTVEtYTAQLIQLFPYEINDhKAEQIIQYAHLGEYKKKPVNQISKAAYAQLLLSI 151
Cdd:PRK13546  79 GKVDRNGEVsviaISAGLSGQLTGIENIE-FKMLCMGFKRKEIKA-MTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991 152 ARSSKSNIIILNHVIDYLPPQFMERAIELTNDYIENNLTIVTIGDDVDKIAQVSNYIAWFSHGQLRMEGSLKQVIPLFKE 231
Cdd:PRK13546 157 NITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEA 236
                        250       260
                 ....*....|....*....|....*
gi 446457991 232 HERDrLSLESEEEIQNFDLDWKKNR 256
Cdd:PRK13546 237 FLND-FKKKSKAEQKEFRNKLDESR 260
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
37-162 1.20e-05

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: 45.33  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991   37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVC-TEDLFY----------GYI--EDQALIHQTVET-- 101
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdGQDLTDderkslrkeiGYVfqDPQLFPRLTVREnl 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446457991  102 YTAQLIQLFPYEINDHKAEQIIQYAHLGEYKKKPVNQISKA-AYAQL-LLSIAR--SSKSNIIIL 162
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTlSGGQRqRVAIARalLTKPKLLLL 145
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
37-226 3.26e-03

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: 40.17  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991   37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVC---------TEDLFYG------YIedqALIHQTVET 101
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmTKPGPDGrgrakrYI---GILHQEYDL 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  102 YT--------AQLIQL-FPYEINDHKAEQIIQYAHLGEYKKKPV-----NQIS-----KAAYAQLLLSIARssksnIIIL 162
Cdd:TIGR03269 377 YPhrtvldnlTEAIGLeLPDELARMKAVITLKMVGFDEEKAEEIldkypDELSegerhRVALAQVLIKEPR-----IVIL 451
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446457991  163 NHVIDYLPPQFMERAIE-LTNDYIENNLTIVTIGDDVDKIAQVSNYIAWFSHGQLRMEGSLKQVI 226
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
 
Name Accession Description Interval E-value
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
37-236 4.42e-14

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 72.04  E-value: 4.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVCTedlfyGYIedQALI------------HQTVETYtA 104
Cdd:COG1134   42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN-----GRV--SALLelgagfhpeltgRENIYLN-G 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991 105 QLIQLFPYEInDHKAEQIIQYAHLGEYKKKPVNQISKAAYAQLLLSIARSSKSNIIILNHVI---DylpPQFMERAIELT 181
Cdd:COG1134  114 RLLGLSRKEI-DEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLavgD---AAFQKKCLARI 189
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446457991 182 NDYIENNLTIVTIGDDVDKIAQVSNYIAWFSHGQLRMEGSLKQVIPLFKEHERDR 236
Cdd:COG1134  190 RELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAYEALLAGR 244
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
37-220 1.09e-13

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 70.25  E-value: 1.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVCTED----LFYGYIEDQALihqTVE---TYTAQLIQL 109
Cdd:cd03220   38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsslLGLGGGFNPEL---TGReniYLNGRLLGL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991 110 FPYEInDHKAEQIIQYAHLGEYKKKPVNQISKAAYAQLLLSIARSSKSNIIILNHVI---DylpPQFMERAIELTNDYIE 186
Cdd:cd03220  115 SRKEI-DEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLavgD---AAFQEKCQRRLRELLK 190
                        170       180       190
                 ....*....|....*....|....*....|....
gi 446457991 187 NNLTIVTIGDDVDKIAQVSNYIAWFSHGQLRMEG 220
Cdd:cd03220  191 QGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
1-256 1.95e-10

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 61.37  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991   1 MGSSIVLKllKVTHYYR----NKQN-KKWYLPFGYDAEDIDLNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDK 75
Cdd:PRK13546   1 MNVSVNIK--NVTKEYRiyrtNKERmKDALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  76 GKVVCTEDL----FYGYIEDQALIHQTVEtYTAQLIQLFPYEINDhKAEQIIQYAHLGEYKKKPVNQISKAAYAQLLLSI 151
Cdd:PRK13546  79 GKVDRNGEVsviaISAGLSGQLTGIENIE-FKMLCMGFKRKEIKA-MTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991 152 ARSSKSNIIILNHVIDYLPPQFMERAIELTNDYIENNLTIVTIGDDVDKIAQVSNYIAWFSHGQLRMEGSLKQVIPLFKE 231
Cdd:PRK13546 157 NITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEA 236
                        250       260
                 ....*....|....*....|....*
gi 446457991 232 HERDrLSLESEEEIQNFDLDWKKNR 256
Cdd:PRK13546 237 FLND-FKKKSKAEQKEFRNKLDESR 260
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
37-246 2.71e-09

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 59.52  E-value: 2.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVvctedlfygYIEDQALIHQTVETYTAQL-----IQLFP 111
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV---------DIKGSAALIAISSGLNGQLtgienIELKG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991 112 YEINDHKAE------QIIQYAHLGEYKKKPVNQISKAAYAQLLLSIARSSKSNIIILNHVIDYLPPQFMERAIELTNDYI 185
Cdd:PRK13545 111 LMMGLTKEKikeiipEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFK 190
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446457991 186 ENNLTIVTIGDDVDKIAQVSNYIAWFSHGQLRMEGSLKQVIPLFKE--HERDRLSLESEEEIQ 246
Cdd:PRK13545 191 EQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEflKKYNQMSVEERKDFR 253
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
37-78 5.04e-07

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: 50.58  E-value: 5.04e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKV 78
Cdd:cd03257   21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSI 62
cbiO PRK13644
energy-coupling factor transporter ATPase;
37-226 3.28e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 48.83  E-value: 3.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVV------CTEDLFYGYIEDQALIHQTVET--------- 101
Cdd:PRK13644  18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgidtGDFSKLQGIRKLVGIVFQNPETqfvgrtvee 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991 102 ---YTAQLIQLFPYEINDhKAEQIIQYAHLGEYKKKPVNQISKAAYAQLLLSIARSSKSNIIILNHVIDYLPPQFMERAI 178
Cdd:PRK13644  98 dlaFGPENLCLPPIEIRK-RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446457991 179 ELTNDYIENNLTIVTIGDDVDKIaQVSNYIAWFSHGQLRMEGSLKQVI 226
Cdd:PRK13644 177 ERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVL 223
cbiO PRK13650
energy-coupling factor transporter ATPase;
26-202 4.57e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 48.19  E-value: 4.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  26 LPFGY--DAEDIDLNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVCTEDLF-----------YGYI--- 89
Cdd:PRK13650  10 LTFKYkeDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteenvwdirhkIGMVfqn 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  90 EDQALIHQTVETYTAQLI--QLFPYEINDHKAEQIIQYAHLGEYKKKPVNQISKAAYAQLLLSIARSSKSNIIILNHVID 167
Cdd:PRK13650  90 PDNQFVGATVEDDVAFGLenKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446457991 168 YLPPqfmERAIELTNdYI-----ENNLTIVTIGDDVDKIA 202
Cdd:PRK13650 170 MLDP---EGRLELIK-TIkgirdDYQMTVISITHDLDEVA 205
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
37-78 4.72e-06

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: 49.13  E-value: 4.72e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKV 78
Cdd:COG1123  281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
37-162 1.20e-05

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: 45.33  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991   37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVC-TEDLFY----------GYI--EDQALIHQTVET-- 101
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdGQDLTDderkslrkeiGYVfqDPQLFPRLTVREnl 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446457991  102 YTAQLIQLFPYEINDHKAEQIIQYAHLGEYKKKPVNQISKA-AYAQL-LLSIAR--SSKSNIIIL 162
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTlSGGQRqRVAIARalLTKPKLLLL 145
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
37-215 1.25e-05

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: 46.31  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKV-VCTEDLFY----------GYI----EDQaLIHQTVET 101
Cdd:cd03225   17 LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlVDGKDLTKlslkelrrkvGLVfqnpDDQ-FFGPTVEE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991 102 YTAQ-LIQL-FPYEINDHKAEQIIQYAHLGEYKKKPVNQIS-----KAAYAQLLlsiarSSKSNIIILNHVIDYLPPQFM 174
Cdd:cd03225   96 EVAFgLENLgLPEEEIEERVEEALELVGLEGLRDRSPFTLSggqkqRVAIAGVL-----AMDPDILLLDEPTAGLDPAGR 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446457991 175 ERAIELTNDYIENNLTIVTIGDDVDKIAQVSNYIAWFSHGQ 215
Cdd:cd03225  171 RELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
37-116 3.06e-05

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: 44.51  E-value: 3.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVCtedlfygyieDQALIHQTVET-------YTAQLIQL 109
Cdd:cd03246   18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL----------DGADISQWDPNelgdhvgYLPQDDEL 87

                 ....*..
gi 446457991 110 FPYEIND 116
Cdd:cd03246   88 FSGSIAE 94
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
37-192 8.18e-05

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: 43.81  E-value: 8.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVV--------CTEDLFyGYI-EDQAL------IHQTVet 101
Cdd:cd03269   16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldiAARNRI-GYLpEERGLypkmkvIDQLV-- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991 102 YTAQLIQLFPYEINdHKAEQIIQYAHLGEYKKKPVNQISKA--AYAQLLLSIARSSKsnIIILNHVIDYLPP---QFMER 176
Cdd:cd03269   93 YLAQLKGLKKEEAR-RRIDEWLERLELSEYANKRVEELSKGnqQKVQFIAAVIHDPE--LLILDEPFSGLDPvnvELLKD 169
                        170
                 ....*....|....*.
gi 446457991 177 AIeltNDYIENNLTIV 192
Cdd:cd03269  170 VI---RELARAGKTVI 182
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
37-251 1.55e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 43.44  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKV------VCTEDLFY-----GYI---EDQALIHQTVETY 102
Cdd:PRK13632  25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkidgitISKENLKEirkkiGIIfqnPDNQFIGATVEDD 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991 103 TAqliqlFPYE---INDHKAEQII-QYAH---LGEY-KKKPVN----QISKAAYAQLLlsiarSSKSNIIILNHVIDYLP 170
Cdd:PRK13632 105 IA-----FGLEnkkVPPKKMKDIIdDLAKkvgMEDYlDKEPQNlsggQKQRVAIASVL-----ALNPEIIIFDESTSMLD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991 171 PQFMERAIELTNDYIEN-NLTIVTIGDDVDKIAQvSNYIAWFSHGQLRMEGSLKQViplfkeherdrlsLESEEEIQNFD 249
Cdd:PRK13632 175 PKGKREIKKIMVDLRKTrKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEI-------------LNNKEILEKAK 240

                 ..
gi 446457991 250 LD 251
Cdd:PRK13632 241 ID 242
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
25-79 1.60e-04

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: 43.24  E-value: 1.60e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446457991  25 YLPFGYDAEDIdLNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVV 79
Cdd:cd03252    7 RFRYKPDGPVI-LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL 60
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
28-78 2.37e-04

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: 43.67  E-value: 2.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446457991  28 FGYDAEDID-LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKV 78
Cdd:COG2274  481 FRYPGDSPPvLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI 532
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
7-140 2.45e-04

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: 42.48  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991   7 LKLLKVTHYYRNKQNKKWYLpfgydaedidlNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKV-VCTEDLF 85
Cdd:cd03255    1 IELKNLSKTYGGGGEKVQAL-----------KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrVDGTDIS 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446457991  86 Y--------------GYI-EDQALI-HQTVE---TYTAQLIQLFPYEINDhKAEQIIQYAHLGEYKKKPVNQIS 140
Cdd:cd03255   70 KlsekelaafrrrhiGFVfQSFNLLpDLTALenvELPLLLAGVPKKERRE-RAEELLERVGLGDRLNHYPSELS 142
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
37-240 2.55e-04

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 43.29  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVCT-EDL-------------FYGYiedqALI-HQTVET 101
Cdd:PRK11607  35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgVDLshvppyqrpinmmFQSY----ALFpHMTVEQ 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991 102 YTA-QLIQ--LFPYEINDhKAEQIIQYAHLGEYKKKPVNQISKAAYAQLLLSIARSSKSNIIILNHVIDYLPPQFMERAI 178
Cdd:PRK11607 111 NIAfGLKQdkLPKAEIAS-RVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQ 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446457991 179 ELTNDYIEN-NLTIVTIGDDVDKIAQVSNYIAWFSHGQLRMEGSLKQVIplfkEHERDRLSLE 240
Cdd:PRK11607 190 LEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY----EHPTTRYSAE 248
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
26-226 3.41e-04

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: 42.97  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  26 LPFGYDAEDID-LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIkPDKGKV-----VCTEDLFYGYIEDQ----ALI 95
Cdd:COG1123   10 LSVRYPGGDVPaVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRIsgevlLDGRDLLELSEALRgrriGMV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  96 HQTVETytaqliQLFPYEINDH-----------------KAEQIIQYAHLGEYKKKPVNQISKAAYAQLLLSIARSSKSN 158
Cdd:COG1123   89 FQDPMT------QLNPVTVGDQiaealenlglsraearaRVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446457991 159 IIILNHVIDYLPPQFMERAIELTNDYI-ENNLTIVTIGDDVDKIAQVSNYIAWFSHGQLRMEGSLKQVI 226
Cdd:COG1123  163 LLIADEPTTALDVTTQAEILDLLRELQrERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
26-78 3.88e-04

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 42.31  E-value: 3.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446457991  26 LPFGY-DAEDIDLNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKV 78
Cdd:PRK13635  11 ISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI 64
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
37-78 4.63e-04

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: 41.72  E-value: 4.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKV 78
Cdd:cd03261   16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEV 57
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
11-88 8.72e-04

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 41.80  E-value: 8.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  11 KVTHYYRNKQNKKWY--------LPFGYDAEDIdLNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVCTE 82
Cdd:PRK15064 302 RQNPFIRFEQDKKLHrnalevenLTKGFDNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSE 380

                 ....*.
gi 446457991  83 DLFYGY 88
Cdd:PRK15064 381 NANIGY 386
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
37-79 1.25e-03

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: 39.72  E-value: 1.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVV 79
Cdd:cd03216   16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL 58
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
37-80 1.53e-03

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 40.44  E-value: 1.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVC 80
Cdd:PRK10419  28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW 71
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
39-78 1.99e-03

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 39.91  E-value: 1.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446457991  39 NISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKV 78
Cdd:PRK11701  24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
37-78 2.52e-03

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: 39.49  E-value: 2.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKV 78
Cdd:cd03258   21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSV 62
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
37-111 2.83e-03

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: 38.71  E-value: 2.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVC-TEDLfyGYIEDQALIHQTVETYTAQLIQLFP 111
Cdd:cd03229   16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdGEDL--TDLEDELPPLRRRIGMVFQDFALFP 89
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
37-226 3.26e-03

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: 40.17  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991   37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVC---------TEDLFYG------YIedqALIHQTVET 101
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmTKPGPDGrgrakrYI---GILHQEYDL 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  102 YT--------AQLIQL-FPYEINDHKAEQIIQYAHLGEYKKKPV-----NQIS-----KAAYAQLLLSIARssksnIIIL 162
Cdd:TIGR03269 377 YPhrtvldnlTEAIGLeLPDELARMKAVITLKMVGFDEEKAEEIldkypDELSegerhRVALAQVLIKEPR-----IVIL 451
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446457991  163 NHVIDYLPPQFMERAIE-LTNDYIENNLTIVTIGDDVDKIAQVSNYIAWFSHGQLRMEGSLKQVI 226
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
28-78 4.78e-03

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 39.38  E-value: 4.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446457991  28 FGYDAEDIDLNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKV 78
Cdd:COG1132  347 FSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI 397
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
28-92 4.84e-03

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 39.28  E-value: 4.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446457991  28 FGYDAEDIdLNNISLHIYQGEALGIIGEVESSK-ALVgQLLAGAIKPDKGKVVCTEDLFYGYIeDQ 92
Cdd:COG0488  323 KSYGDKTL-LDDLSLRIDRGDRIGLIGPNGAGKsTLL-KLLAGELEPDSGTVKLGETVKIGYF-DQ 385
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
37-163 5.52e-03

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 38.56  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457991  37 LNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVCTEDLFYGYIEDQALIHQTVETYTAQLIQLFPyeiND 116
Cdd:PRK09544  20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLTVNRFLRLRP---GT 96
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446457991 117 HKAEQI-----IQYAHLGEYkkkPVNQISKAAYAQLLLSIARSSKSNIIILN 163
Cdd:PRK09544  97 KKEDILpalkrVQAGHLIDA---PMQKLSGGETQRVLLARALLNRPQLLVLD 145
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
36-91 5.89e-03

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 39.41  E-value: 5.89e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446457991  36 DLNNISLH-----IYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVVCTEDLFYG--YIED 91
Cdd:PRK13409 349 KLGDFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKpqYIKP 411
cbiO PRK13637
energy-coupling factor transporter ATPase;
7-79 5.90e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 38.88  E-value: 5.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446457991   7 LKLLKVTHYYRNKQnkkwylPFgydaEDIDLNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKVV 79
Cdd:PRK13637   3 IKIENLTHIYMEGT------PF----EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKII 65
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
28-78 7.27e-03

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: 37.98  E-value: 7.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446457991  28 FGYDAEDIDLNNISLHIYQGEALGIIGEVESSKALVGQLLAGAIKPDKGKV 78
Cdd:cd03254   10 FSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQI 60
 
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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