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Conserved domains on  [gi|877977460|emb|CHN12672|]
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thiamine transporter ATP-binding subunit [Salmonella enterica subsp. enterica serovar Typhi]

Protein Classification

thiamine ABC transporter ATP-binding protein ThiQ( domain architecture ID 11484934)

thiamine ABC transporter ATP-binding protein ThiQ is part of the thiamine transporter complex ThiBPQ and is responsible for coupling the energy of ATP hydrolysis to the import of thiamine and thiamine pyrophosphate (TPP)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
1-232 3.20e-169

thiamine ABC transporter ATP-binding protein ThiQ;


:

Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 465.21  E-value: 3.20e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQEN 80
Cdd:PRK10771   1 MLKLTDITWLYHHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  81 NLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:PRK10771  81 NLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 877977460 161 DPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALLGIKS 232
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLGIKS 232
 
Name Accession Description Interval E-value
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
1-232 3.20e-169

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 465.21  E-value: 3.20e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQEN 80
Cdd:PRK10771   1 MLKLTDITWLYHHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  81 NLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:PRK10771  81 NLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 877977460 161 DPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALLGIKS 232
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLGIKS 232
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
1-230 4.92e-146

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 406.45  E-value: 4.92e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQEN 80
Cdd:COG3840    1 MLRLDDLTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  81 NLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:COG3840   81 NLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 877977460 161 DPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASA--SALLGI 230
Cdd:COG3840  161 DPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPalAAYLGI 232
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
2-212 6.02e-122

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: 344.86  E-value: 6.02e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   2 LKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENN 81
Cdd:cd03298    1 VRLDKIRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  82 LFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:cd03298   81 LFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 877977460 162 PALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03298  161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
2-214 1.26e-120

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: 341.84  E-value: 1.26e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    2 LKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENN 81
Cdd:TIGR01277   1 LALDKVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   82 LFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:TIGR01277  81 LFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 877977460  162 PALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKT 214
Cdd:TIGR01277 161 PLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
19-158 7.47e-45

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 147.02  E-value: 7.47e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLT--PPSRRPVSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:pfam00005   5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerKSLRKEIGYVFQDPQLFPRLTVRENLRLGL 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460   97 NPGLTLNASQREKRDAIARQMGIESLMARL----PGELSGGQRQRVALARCLVREQPVLLLDEPFS 158
Cdd:pfam00005  85 LLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
19-199 1.19e-31

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 114.64  E-value: 1.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQennlfshLNVQQNIGLGL-- 96
Cdd:NF040873  12 DLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLP-------LTVRDLVAMGRwa 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 --NPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:NF040873  85 rrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAE 164
                        170       180
                 ....*....|....*....|....*
gi 877977460 175 IcRERQLTLLMVSHSVEDAARIAPR 199
Cdd:NF040873 165 E-HARGATVVVVTHDLELVRRADPC 188
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
12-195 3.16e-15

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 74.39  E-value: 3.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  12 HHLPMRF---------TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedHTLTP---PSRRPVSMLFQE 79
Cdd:NF033858 270 RGLTMRFgdftavdhvSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG--QPVDAgdiATRRRVGYMSQA 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  80 NNLFSHLNVQQNiglglnpgLTLNA-------SQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVL 151
Cdd:NF033858 348 FSLYGELTVRQN--------LELHArlfhlpaAEIAARvAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELL 419
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 877977460 152 LLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAAR 195
Cdd:NF033858 420 ILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER 463
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
19-228 8.20e-15

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 73.24  E-value: 8.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-----HtltppsRRPVS-----M---LfqENNLFSH 85
Cdd:NF033858  21 SLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDmadarH------RRAVCpriayMpqgL--GKNLYPT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  86 LNVQQNI-------GLGlnpgltlnASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPF 157
Cdd:NF033858  93 LSVFENLdffgrlfGQD--------AAERRRRiDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 158 SALDPALRQEMLTLVSDICRER-QLTLLMVSHSVEDAARIaprSIVVA--DGRIAWQGKTDELLSGQASAS------ALL 228
Cdd:NF033858 165 TGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEEAERF---DWLVAmdAGRVLATGTPAELLARTGADTleaafiALL 241
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
99-217 1.01e-12

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 66.30  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  99 GLTLNASQREKR---DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:NF000106 111 GR*LDLSRKDARaraDELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM 190
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 877977460 176 CRERQlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:NF000106 191 VRDGA-TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
GguA NF040905
sugar ABC transporter ATP-binding protein;
19-207 8.49e-11

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 60.96  E-value: 8.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGfLAPA---SGTLLIAGED---HTLTPPSRRPVSMLFQENNLFSHLNVQQNI 92
Cdd:NF040905  21 NLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVcrfKDIRDSEALGIVIIHQELALIPYLSIAENI 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLNPG----LTLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:NF040905 100 FLGNERAkrgvIDWNETNRRARELLAK-VGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAAL 178
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 877977460 169 LTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:NF040905 179 LDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGR 216
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
24-202 2.07e-10

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: 57.38  E-value: 2.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    24 RGEQVAILGPSGAGKSTLLNLIAGFLAPASGT-LLIAGEDHTLTPPSRRpvsmlfqennlfshlnvqqniglglnpgltl 102
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQL------------------------------- 49
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   103 nasqrekrdaiarqmgIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD-----ICR 177
Cdd:smart00382  50 ----------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKS 113
                          170       180
                   ....*....|....*....|....*
gi 877977460   178 ERQLTLLMVSHSVEDAARIAPRSIV 202
Cdd:smart00382 114 EKNLTVILTTNDEKDLGPALLRRRF 138
 
Name Accession Description Interval E-value
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
1-232 3.20e-169

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 465.21  E-value: 3.20e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQEN 80
Cdd:PRK10771   1 MLKLTDITWLYHHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  81 NLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:PRK10771  81 NLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 877977460 161 DPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALLGIKS 232
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLGIKS 232
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
1-230 4.92e-146

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 406.45  E-value: 4.92e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQEN 80
Cdd:COG3840    1 MLRLDDLTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  81 NLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:COG3840   81 NLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 877977460 161 DPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASA--SALLGI 230
Cdd:COG3840  161 DPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPalAAYLGI 232
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
2-212 6.02e-122

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: 344.86  E-value: 6.02e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   2 LKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENN 81
Cdd:cd03298    1 VRLDKIRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  82 LFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:cd03298   81 LFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 877977460 162 PALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03298  161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
2-214 1.26e-120

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: 341.84  E-value: 1.26e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    2 LKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENN 81
Cdd:TIGR01277   1 LALDKVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   82 LFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:TIGR01277  81 LFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 877977460  162 PALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKT 214
Cdd:TIGR01277 161 PLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
2-212 1.67e-87

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: 257.83  E-value: 1.67e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   2 LKLIDITWLYH--HLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQE 79
Cdd:cd03259    1 LELKGLSKTYGsvRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  80 NNLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSA 159
Cdd:cd03259   81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 877977460 160 LDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03259  161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
18-217 4.74e-74

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 228.44  E-value: 4.74e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLN 97
Cdd:COG3842   24 VSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQDYALFPHLTVAENVAFGLR 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  98 pGLTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:COG3842  104 -MRGVPKAEIRARvAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQ 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 877977460 177 RERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:COG3842  183 RELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
18-217 1.59e-67

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 211.47  E-value: 1.59e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGL- 96
Cdd:COG3839   22 IDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQSYALYPHMTVYENIAFPLk 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 NPGLtlNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:COG3839  102 LRKV--PKAEIDRRvREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRL 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 877977460 176 CRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:COG3839  180 HRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
2-207 2.34e-67

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: 205.50  E-value: 2.34e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   2 LKLIDITWLYHH--LPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHT----LTPPSRRPVSM 75
Cdd:cd03229    1 LELKNVSKRYGQktVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  76 LFQENNLFSHLNVQQNIGLGLnpgltlnasqrekrdaiarqmgieslmarlpgelSGGQRQRVALARCLVREQPVLLLDE 155
Cdd:cd03229   81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 877977460 156 PFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:cd03229  127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
18-209 4.60e-67

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 207.63  E-value: 4.60e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhTLTPPSRRpVSMLFQENNLFSHLNVQQNIGLGLn 97
Cdd:COG1116   30 VSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK--PVTGPGPD-RGVVFQEPALLPWLTVLDNVALGL- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  98 PGLTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:COG1116  106 ELRGVPKAERRERaRELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLW 185
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 877977460 177 RERQLTLLMVSHSVEDAARIAPRSIVVAD--GRIA 209
Cdd:COG1116  186 QETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
17-207 5.19e-64

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: 198.46  E-value: 5.19e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtLTPPSRRpVSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:cd03293   22 DISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP--VTGPGPD-RGYVFQQDALLPWLTVLDNVALGL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 NPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:cd03293   99 ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIW 178
                        170       180       190
                 ....*....|....*....|....*....|.
gi 877977460 177 RERQLTLLMVSHSVEDAARIAPRsIVVADGR 207
Cdd:cd03293  179 RETGKTVLLVTHDIDEAVFLADR-VVVLSAR 208
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
19-231 4.52e-63

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 199.99  E-value: 4.52e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLN 97
Cdd:COG1118   22 SLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPPRERRVGFVFQHYALFPHMTVAENIAFGLR 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  98 PGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICR 177
Cdd:COG1118  102 VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHD 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 178 ERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASA--LLGIK 231
Cdd:COG1118  182 ELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVarFLGCV 237
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
20-219 6.09e-61

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: 191.01  E-value: 6.09e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPG 99
Cdd:cd03299   20 LEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 LTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRER 179
Cdd:cd03299  100 KVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEF 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 877977460 180 QLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:cd03299  180 GVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
17-208 1.88e-60

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: 189.76  E-value: 1.88e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:cd03300   18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQNYALFPHLTVFENIAFGL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 NPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:cd03300   98 RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQ 177
                        170       180       190
                 ....*....|....*....|....*....|..
gi 877977460 177 RERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:cd03300  178 KELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
18-218 4.46e-59

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: 186.34  E-value: 4.46e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRPV----SMLFQENNLFSHLNVQQNI 92
Cdd:COG1127   24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDiTGLSEKELYELrrriGMLFQGGALFDSLTVFENV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLNPGLTLnaSQREKRDAIA---RQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:COG1127  104 AFPLREHTDL--SEAEIRELVLeklELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVID 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 877977460 170 TLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELL 218
Cdd:COG1127  182 ELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
1-219 6.88e-59

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: 186.40  E-value: 6.88e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDITWLYHHLPM--RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSR-RPVSML 76
Cdd:COG1120    1 MLEAENLSVGYGGRPVldDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlASLSRRELaRRIAYV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  77 FQENNLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQ----MGIESLMARLPGELSGGQRQRVALARCLVREQPVLL 152
Cdd:COG1120   81 PQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEalerTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 153 LDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG1120  161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
19-208 1.15e-58

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 184.86  E-value: 1.15e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-----RRPVSMLFQENNLFSHLNVQQNI 92
Cdd:COG1136   28 SLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDiSSLSERElarlrRRHIGFVFQFFNLLPELTALENV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLNPGlTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:COG1136  108 ALPLLLA-GVSRKERRERaRELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL 186
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 877977460 172 VSDICRERQLTLLMVSHSvEDAARIAPRSIVVADGRI 208
Cdd:COG1136  187 LRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
19-219 2.19e-58

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: 184.46  E-value: 2.19e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQ--ENNLFShLNVQQNIGL 94
Cdd:COG1122   21 SLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRelRRKVGLVFQnpDDQLFA-PTVEEDVAF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  95 GL-NPGLTlnASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:COG1122  100 GPeNLGLP--REEIRERvEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELL 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 877977460 173 SDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG1122  178 KRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
19-208 3.31e-58

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: 183.46  E-value: 3.31e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLTPPSRRPVSMLFQENNLFSHLNVQQNI 92
Cdd:cd03255   24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDisklseKELAAFRRRHIGFVFQSFNLLPDLTALENV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:cd03255  104 ELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELL 183
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 877977460 173 SDICRERQLTLLMVSHSvEDAARIAPRSIVVADGRI 208
Cdd:cd03255  184 RELNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
19-217 1.55e-57

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 182.95  E-value: 1.55e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-----RRPVSMLFQENNLFSHLNVQQNI- 92
Cdd:COG3638   23 SLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRalrrlRRRIGMIFQQFNLVPRLSVLTNVl 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 --GLGLNP---GLTLNASQREKRDAIA--RQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:COG3638  103 agRLGRTStwrSLLGLFPPEDRERALEalERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTA 182
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 877977460 166 QEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:COG3638  183 RQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
1-229 4.20e-57

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: 184.92  E-value: 4.20e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKlIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLTPPSRRPVS 74
Cdd:COG4148    2 MLE-VDFRLRRGGFTLDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsarGIFLPPHRRRIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  75 MLFQENNLFSHLNVQQNIGLGLNPglTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLD 154
Cdd:COG4148   81 YVFQEARLFPHLSVRGNLLYGRKR--APRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMD 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 155 EPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALLG 229
Cdd:COG4148  159 EPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGG 233
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
19-217 1.40e-56

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: 180.01  E-value: 1.40e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTP----PSRRPVSMLFQENNLFSHLNVQQNIG 93
Cdd:cd03261   20 DLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDiSGLSEaelyRLRRRMGMLFQSGALFDSLTVFENVA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 LGLNPGLTLNASQREKRDAIARQM-GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:cd03261  100 FPLREHTRLSEEEIREIVLEKLEAvGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLI 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:cd03261  180 RSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
19-220 3.03e-56

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 179.10  E-value: 3.03e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-RRPVSMLFQENNLFSHLNVQQNIGL--G 95
Cdd:COG1131   20 SLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQEPALYPDLTVRENLRFfaR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LNPgltLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:COG1131  100 LYG---LPRKEARERiDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRE 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 877977460 175 IcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSG 220
Cdd:COG1131  177 L-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
17-208 9.03e-56

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: 177.06  E-value: 9.03e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:cd03301   18 DLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQNYALYPHMTVYDNIAFGL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 NpgltlnaSQREKRDAI-------ARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:cd03301   98 K-------LRKVPKDEIdervrevAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMR 170
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 877977460 170 TLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:cd03301  171 AELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
1-194 2.55e-55

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 175.75  E-value: 2.55e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDITWLYHHLPM--RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAP---ASGTLLIAGEDHTLTPPSRRPVSM 75
Cdd:COG4136    1 MLSLENLTITLGGRPLlaPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  76 LFQENNLFSHLNVQQNIGLGLNPGLTlnasqREKRDAIARQM----GIESLMARLPGELSGGQRQRVALARCLVREQPVL 151
Cdd:COG4136   81 LFQDDLLFPHLSVGENLAFALPPTIG-----RAQRRARVEQAleeaGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 877977460 152 LLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAA 194
Cdd:COG4136  156 LLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAP 198
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
12-212 1.51e-54

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: 174.02  E-value: 1.51e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  12 HHLPMRFTLaveRGEQVAILGPSGAGKSTLLNLIAGFLAPASG------TLLIAGEDHTLTPPSRRPVSMLFQENNLFSH 85
Cdd:cd03297   13 FTLKIDFDL---NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlngTVLFDSRKKINLPPQQRKIGLVFQQYALFPH 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  86 LNVQQNIGLGLNpgLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:cd03297   90 LNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 877977460 166 QEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03297  168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
2-223 2.98e-54

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: 174.41  E-value: 2.98e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   2 LKLIDITWLYHHLPM---RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSML 76
Cdd:cd03295    1 IEFENVTKRYGGGKKavnNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVelRRKIGYV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  77 FQENNLFSHLNVQQNIGLGLnpglTLNASQREKRDAIARQ------MGIESLMARLPGELSGGQRQRVALARCLVREQPV 150
Cdd:cd03295   81 IQQIGLFPHMTVEENIALVP----KLLKWPKEKIRERADEllalvgLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460 151 LLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQAS 223
Cdd:cd03295  157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
19-217 1.13e-52

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: 170.06  E-value: 1.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-----RRPVSMLFQENNLFSHLNVQQNIG 93
Cdd:cd03256   21 SLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlRRQIGMIFQQFNLIERLSVLENVL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 LGLNP------GLTLNASQREKRDAIA--RQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:cd03256  101 SGRLGrrstwrSLFGLFPKEEKQRALAalERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASS 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 877977460 166 QEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:cd03256  181 RQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1-224 1.25e-52

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: 170.37  E-value: 1.25e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDITWLYHHLPMRFT------LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED--HTLTPPSRRP 72
Cdd:COG1124    1 MLEVRNLSVSYGQGGRRVPvlkdvsLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvtRRRRKAFRRR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  73 VSMLFQennlfshlnvqqNIGLGLNPGLTLNAS-----------QREKR-DAIARQMGI-ESLMARLPGELSGGQRQRVA 139
Cdd:COG1124   81 VQMVFQ------------DPYASLHPRHTVDRIlaeplrihglpDREERiAELLEQVGLpPSFLDRYPHQLSGGQRQRVA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 140 LARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG1124  149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228

                 ....*
gi 877977460 220 GQASA 224
Cdd:COG1124  229 GPKHP 233
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
20-224 3.55e-52

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: 168.67  E-value: 3.55e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNpg 99
Cdd:cd03296   23 LDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYALFRHMTVFDNVAFGLR-- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 lTLNASQREKRDAIARQ-------MGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:cd03296  101 -VKPRSERPPEAEIRAKvhellklVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWL 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASA 224
Cdd:cd03296  180 RRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASP 231
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
19-207 6.23e-52

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: 167.26  E-value: 6.23e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQE-NNLFSHLNVQQNIGLG 95
Cdd:cd03225   21 SLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKelRRKVGLVFQNpDDQFFGPTVEEEVAFG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LNpGLTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:cd03225  101 LE-NLGLPEEEIEERvEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKK 179
                        170       180       190
                 ....*....|....*....|....*....|...
gi 877977460 175 ICRERQlTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:cd03225  180 LKAEGK-TIIIVTHDLDLLLELADRVIVLEDGK 211
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
19-219 4.11e-51

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: 173.17  E-value: 4.11e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRP----VSMLFQ--ENNLFSHLNVQQN 91
Cdd:COG1123  285 SLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDlTKLSRRSLRElrrrVQMVFQdpYSSLNPRMTVGDI 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  92 IGLGLNPGLTLNASQREKR-DAIARQMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:COG1123  365 IAEPLRLHGLLSRAERRERvAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQIL 444
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 877977460 170 TLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG1123  445 NLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
1-219 5.86e-51

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: 165.45  E-value: 5.86e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDITWLYHHLPMRFT------LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS----- 69
Cdd:cd03258    1 MIELKNVSKVFGDTGGKVTalkdvsLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrka 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  70 RRPVSMLFQENNLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQP 149
Cdd:cd03258   81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 150 VLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:cd03258  161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
19-219 1.77e-50

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


Pssm-ID: 275314 [Multi-domain]  Cd Length: 277  Bit Score: 165.70  E-value: 1.77e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtLTP-------PSRRPVSMLFQ--ENNLFShLNVQ 89
Cdd:TIGR04521  25 SLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRD--ITAkkkkklkDLRKKVGLVFQfpEHQLFE-ETVY 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   90 QNIGLG-LNPGLTLNASQREKRDAIaRQMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:TIGR04521 102 KDIAFGpKNLGLSEEEAEERVKEAL-ELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKE 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 877977460  168 MLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:TIGR04521 181 ILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
2-208 2.59e-50

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 163.06  E-value: 2.59e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   2 LKLIDITWLYHHLPM--RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLF 77
Cdd:COG4619    1 LELEGLSFRVGGKPIlsPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlSAMPPPEwRRQVAYVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  78 QENNLFSHlNVQQNIGLGLNpgLTLNASQREKRDAIARQMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEP 156
Cdd:COG4619   81 QEPALWGG-TVRDNLPFPFQ--LRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 877977460 157 FSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:COG4619  158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
19-219 4.48e-50

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 163.24  E-value: 4.48e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtLTPPS------RRPVSMLFQENNLFSHLNVQQNI 92
Cdd:COG1126   21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGED--LTDSKkdinklRRKVGMVFQQFNLFPHLTVLENV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLnpgltLNASQREKRDAIAR------QMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:COG1126   99 TLAP-----IKVKKMSKAEAEERamelleRVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVG 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 877977460 167 EMLTLVSDICRERqLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG1126  174 EVLDVMRDLAKEG-MTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
18-212 1.52e-49

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 165.89  E-value: 1.52e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLN 97
Cdd:PRK09452  33 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQSYALFPHMTVFENVAFGLR 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  98 PGLTLNASQREK-RDAIaRQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:PRK09452 113 MQKTPAAEITPRvMEAL-RMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQ 191
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 877977460 177 RERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:PRK09452 192 RKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
1-225 2.74e-49

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 161.56  E-value: 2.74e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDITWLYHHLPM--RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-RRPVSMLF 77
Cdd:COG4555    1 MIEVENLSKKYGKVPAlkDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  78 QENNLFSHLNVQQNIGLgLNPGLTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEP 156
Cdd:COG4555   81 DERGLYDRLTVRENIRY-FAELYGLFDEELKKRiEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460 157 FSALDPALRQEMLTLVSDiCRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASAS 225
Cdd:COG4555  160 TNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEN 227
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
30-219 2.84e-49

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: 164.20  E-value: 2.84e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   30 ILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPGLTLNASQREK 109
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  110 RDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHS 189
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 877977460  190 VEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYE 190
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
19-218 9.62e-49

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: 160.89  E-value: 9.62e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHT------LTPPSRRPVSMLFQENNLFSHLNVQQNI 92
Cdd:cd03294   44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamsrkeLRELRRKKISMVFQSFALLPHRTVLENV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLN-PGLTLNASQREKRDAIArQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:cd03294  124 AFGLEvQGVPRAEREERAAEALE-LVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE 202
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 877977460 172 VSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELL 218
Cdd:cd03294  203 LLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
19-222 2.83e-48

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 159.10  E-value: 2.83e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTP------PSRRPVSMLFQennlfshLNVQQNI 92
Cdd:COG1121   26 SLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARrrigyvPQRAEVDWDFP-------ITVRDVV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLNPGL----TLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:COG1121   99 LMGRYGRRglfrRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEAL 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 877977460 169 LTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWqGKTDELLSGQA 222
Cdd:COG1121  179 YELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPEN 230
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
19-217 1.06e-47

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 161.16  E-value: 1.06e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNP 98
Cdd:PRK11607  39 SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQ 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  99 GltlNASQREKRDAIARQMGI---ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:PRK11607 119 D---KLPKAEIASRVNEMLGLvhmQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDI 195
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 877977460 176 CRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK11607 196 LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
20-208 2.06e-47

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


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 155.77  E-value: 2.06e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS----RRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:cd03262   21 LTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGMVFQQFNLFPHLTVLENITLA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LnpgltLNASQREKRDAIARQM------GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:cd03262  101 P-----IKVKGMSKAEAEERALellekvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVL 175
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 877977460 170 TLVSDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:cd03262  176 DVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
20-212 2.39e-47

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: 156.13  E-value: 2.39e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-----RRPVSMLFQenNLFSHLN----VQQ 90
Cdd:cd03257   26 FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkirRKEIQMVFQ--DPMSSLNprmtIGE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  91 NIGLGLNPGLTLNASQREKRDAIARQMGI---ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:cd03257  104 QIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQ 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 877977460 168 MLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03257  184 ILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
20-217 4.90e-47

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 159.42  E-value: 4.90e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPG 99
Cdd:PRK11000  24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSYALYPHLSVAENMSFGLKLA 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 LTlNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRE 178
Cdd:PRK11000 104 GA-KKEEINQRvNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKR 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 877977460 179 RQLTLLMVSHSVEDAARIAPRsIVVAD-GRIAWQGKTDEL 217
Cdd:PRK11000 183 LGRTMIYVTHDQVEAMTLADK-IVVLDaGRVAQVGKPLEL 221
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
17-209 1.48e-46

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 155.02  E-value: 1.48e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTlTPPSRRPVsmLFQENNLFSHLNVQQNIGLGL 96
Cdd:COG4525   25 DVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT-GPGADRGV--VFQKDALLPWLNVLDNVAFGL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 npglTLNASQREKRDAIARQM----GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:COG4525  102 ----RLRGVPKAERRARAEELlalvGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELL 177
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARIAPRSIVVAD--GRIA 209
Cdd:COG4525  178 LDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIV 216
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
28-219 2.27e-46

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 157.20  E-value: 2.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   28 VAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE------DHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNpgLT 101
Cdd:TIGR02142  26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrKGIFLPPEKRRIGYVFQEARLFPHLSVRGNLRYGMK--RA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  102 LNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQL 181
Cdd:TIGR02142 104 RPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGI 183
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 877977460  182 TLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:TIGR02142 184 PILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
19-219 2.75e-46

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: 153.75  E-value: 2.75e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRP---VSMLFQENNLFSHLNVQQNIGLG 95
Cdd:cd03219   20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRTFQIPRLFPELTVLENVMVA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LNPGLTLNASQ----------REKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:cd03219  100 AQARTGSGLLLararreereaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEET 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 877977460 166 QEMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:cd03219  180 EELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
12-216 1.75e-45

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: 152.12  E-value: 1.75e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  12 HHLPMRF---------TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRP---VSMLFQE 79
Cdd:COG0411    8 RGLTKRFgglvavddvSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgIARTFQN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  80 NNLFSHLNVQQNIGLG---------LNPGLTLNASQREKRDAIAR------QMGIESLMARLPGELSGGQRQRVALARCL 144
Cdd:COG0411   88 PRLFPELTVLENVLVAaharlgrglLAALLRLPRARREEREARERaeelleRVGLADRADEPAGNLSYGQQRRLEIARAL 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 877977460 145 VREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDE 216
Cdd:COG0411  168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
19-219 3.18e-45

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: 150.28  E-value: 3.18e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRP---VSMLFQENNLFSHLNVQQNIGLG 95
Cdd:cd03224   20 SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYVPEGRRIFPELTVEENLLLG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LNPGltlnaSQREKRDAIARQMGI----ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:cd03224  100 AYAR-----RRAKRKARLERVYELfprlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEA 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 877977460 172 VSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:cd03224  175 IREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
19-227 3.62e-45

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: 157.37  E-value: 3.62e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPA---SGTLLIAGEDHTLTPPSRRP--VSMLFQE-NNLFSHLNVQQNI 92
Cdd:COG1123   26 SLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGrrIGMVFQDpMTQLNPVTVGDQI 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:COG1123  106 AEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLL 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASAL 227
Cdd:COG1123  186 RELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAV 240
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
19-219 3.83e-45

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 151.01  E-value: 3.83e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtLTPPS------RRPVSMLFQENNLFSHLNVQQNI 92
Cdd:PRK09493  21 DLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLK--VNDPKvderliRQEAGMVFQQFYLFPHLTALENV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGlnPGLTLNASQREKRD---AIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:PRK09493  99 MFG--PLRVRGASKEEAEKqarELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVL 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 877977460 170 TLVSDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK09493 177 KVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
19-208 3.92e-45

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: 148.70  E-value: 3.92e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-RRPVSMLFQENNLFSHLNVQQNIglgln 97
Cdd:cd03230   20 SLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPEEPSLYENLTVRENL----- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  98 pgltlnasqrekrdaiarqmgieslmarlpgELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIcR 177
Cdd:cd03230   95 -------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLREL-K 142
                        170       180       190
                 ....*....|....*....|....*....|.
gi 877977460 178 ERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:cd03230  143 KEGKTILLSSHILEEAERLCDRVAILNNGRI 173
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
19-158 7.47e-45

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 147.02  E-value: 7.47e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLT--PPSRRPVSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:pfam00005   5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerKSLRKEIGYVFQDPQLFPRLTVRENLRLGL 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460   97 NPGLTLNASQREKRDAIARQMGIESLMARL----PGELSGGQRQRVALARCLVREQPVLLLDEPFS 158
Cdd:pfam00005  85 LLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
19-217 1.80e-44

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: 148.48  E-value: 1.80e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFL-----APASGTLLIAGED--HTLTPPS--RRPVSMLFQENNLFsHLNVQ 89
Cdd:cd03260   20 SLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDiyDLDVDVLelRRRVGMVFQKPNPF-PGSIY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  90 QNIGLGLNPGLTLNASQREKRDAIA-RQMGI-ESLMARL-PGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:cd03260   99 DNVAYGLRLHGIKLKEELDERVEEAlRKAALwDEVKDRLhALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTA 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 877977460 167 EMLTLVSDICRErqLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:cd03260  179 KIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
19-212 5.10e-44

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: 146.04  E-value: 5.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedhtltppsrRPVSmlfqennlfshlnvqqniglglnp 98
Cdd:cd03214   19 SLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG----------KDLA------------------------ 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  99 glTLNASQREKRDAIARQ----MGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:cd03214   65 --SLSPKELARKIAYVPQalelLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRR 142
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 877977460 175 ICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03214  143 LARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
19-221 5.86e-44

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: 154.92  E-value: 5.86e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFsHLNVQQNIGLGl 96
Cdd:COG4988  357 SLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDlSDLDPASwRRQIAWVPQNPYLF-AGTIRENLRLG- 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 NPgltlNASQREKRDAiARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:COG4988  435 RP----DASDEELEAA-LEAAGLDEFVAALPdgldtplGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 166 QEMLTLVSDICRERqlTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELLSGQ 221
Cdd:COG4988  510 AEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAKN 562
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
18-228 1.47e-43

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: 154.15  E-value: 1.47e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFSHlNVQQNIGLG 95
Cdd:COG4987  354 LSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDlRDLDEDDlRRRIAVVPQRPHLFDT-TLRENLRLA 432
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 lNPgltlNASQREKRDAIaRQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:COG4987  433 -RP----DATDEELWAAL-ERVGLGDWLAALPdgldtwlGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAAT 506
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 877977460 165 RQEMLTLVSDICRERqlTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:COG4987  507 EQALLADLLEALAGR--TVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNGRYRQLY 567
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
18-219 5.63e-43

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: 153.84  E-value: 5.63e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFSHlNVQQNIGLG 95
Cdd:COG2274  494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlRQIDPASlRRQIGVVLQDVFLFSG-TIRENITLG 572
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 lNPGLTLnasqrEKRDAIARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:COG2274  573 -DPDATD-----EEIIEAARLAGLHDFIEALPmgydtvvGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAET 646
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 165 RQEMLTLVSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLS 219
Cdd:COG2274  647 EAIILENLRRLLKGR--TVIIIAHrlsTIRLADRI----IVLDKGRIVEDGTHEELLA 698
cbiO PRK13637
energy-coupling factor transporter ATPase;
19-216 8.03e-43

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 146.35  E-value: 8.03e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS----RRPVSMLFQ--ENNLFSHlNVQQNI 92
Cdd:PRK13637  27 NIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdiRKKVGLVFQypEYQLFEE-TIEKDI 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGL-NPGLtlnaSQREKRDAIARQMGI-----ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:PRK13637 106 AFGPiNLGL----SEEEIENRVKRAMNIvgldyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 877977460 167 EMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDE 216
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
18-218 3.03e-42

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 150.70  E-value: 3.03e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFsHLNVQQNIGLG 95
Cdd:COG1132  359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDiRDLTLESlRRQIGVVPQDTFLF-SGTIRENIRYG 437
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 lNPgltlNASQREKRDAiARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDP-- 162
Cdd:COG1132  438 -RP----DATDEEVEEA-AKAAQAHEFIEALPdgydtvvGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTet 511
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 163 --ALRQEMLTLVsdicreRQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELL 218
Cdd:COG1132  512 eaLIQEALERLM------KGRTTIVIAHrlsTIRNADRI----LVLDDGRIVEQGTHEELL 562
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
19-223 5.77e-42

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 145.61  E-value: 5.77e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNp 98
Cdd:PRK10851  22 SLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALFRHMTVFDNIAFGLT- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  99 glTLNASQREKRDAIARQ-------MGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK10851 101 --VLPRRERPNAAAIKAKvtqllemVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRW 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 877977460 172 VSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQAS 223
Cdd:PRK10851 179 LRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPAT 230
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
19-230 6.73e-42

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: 142.43  E-value: 6.73e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRP---VSMLFQENNLFSHLNVQQNIGLG 95
Cdd:COG0410   23 SLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgIGYVPEGRRIFPSLTVEENLLLG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 lnpgltlnASQREKRDAIARQMgiESLMARLP----------GELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:COG0410  103 --------AYARRDRAEVRADL--ERVYELFPrlkerrrqraGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIV 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 166 QEMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALLGI 230
Cdd:COG0410  173 EEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLGV 236
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
20-219 9.10e-42

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 143.62  E-value: 9.10e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIagEDHTLTP--------PSRRPVSMLFQ--ENNLFSHlNVQ 89
Cdd:PRK13634  28 VSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI--GERVITAgkknkklkPLRKKVGIVFQfpEHQLFEE-TVE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  90 QNIGLG-LNPGLTlnasqREKRDAIARQM----GI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:PRK13634 105 KDICFGpMNFGVS-----EEDAKQKAREMielvGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 164 LRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFA 235
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
19-208 9.14e-42

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 141.34  E-value: 9.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLT----PPSRRPVSMLFQENNLFSHLNVQQNIG 93
Cdd:COG2884   22 SLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlSRLKrreiPYLRRRIGVVFQDFRLLPDRTVYENVA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 LGLnpgLTLNASQREKRDAIA---RQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT 170
Cdd:COG2884  102 LPL---RVTGKSRKEIRRRVRevlDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIME 178
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 877977460 171 LVSDICReRQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:COG2884  179 LLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRL 215
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
19-218 2.29e-41

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: 140.76  E-value: 2.29e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRP---VSMLFQENNLFSHLNVQQNIGLG 95
Cdd:cd03218   20 SLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRArlgIGYLPQEASIFRKLTVEENILAV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:cd03218  100 LEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 877977460 176 cRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELL 218
Cdd:cd03218  180 -KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
18-207 4.15e-41

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: 137.76  E-value: 4.15e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQennlfshlnvqqniglg 95
Cdd:cd00267   18 VSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEelRRRIGYVPQ----------------- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 lnpgltlnasqrekrdaiarqmgieslmarlpgeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:cd00267   81 ----------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL 126
                        170       180       190
                 ....*....|....*....|....*....|..
gi 877977460 176 CrERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:cd00267  127 A-EEGRTVIIVTHDPELAELAADRVIVLKDGK 157
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
20-217 1.55e-40

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 141.78  E-value: 1.55e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPg 99
Cdd:PRK11432  27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGYGLKM- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 LTLNASQREKRDAIARQM----GIESlmaRLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:PRK11432 106 LGVPKEERKQRVKEALELvdlaGFED---RYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIREL 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 877977460 176 CRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK11432 183 QQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
19-210 2.10e-40

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: 137.66  E-value: 2.10e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTP------PSRRPVSMLFQennlfshLNVQQNI 92
Cdd:cd03235   19 SFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERkrigyvPQRRSIDRDFP-------ISVRDVV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLNP--GLTLNASQREKRDAIA--RQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:cd03235   92 LMGLYGhkGLFRRLSKADKAKVDEalERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDI 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 877977460 169 LTLVSDICRERqLTLLMVSHSVEDAARIAPRSIVVADGRIAW 210
Cdd:cd03235  172 YELLRELRREG-MTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
19-215 2.63e-40

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 138.61  E-value: 2.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTL---LNLIAGflaPASGTLLIAGEDHTL-TPPS-------RRPVSMLFQENNLFSHLN 87
Cdd:PRK11124  22 TLDCPQGETLVLLGPSGAGKSSLlrvLNLLEM---PRSGTLNIAGNHFDFsKTPSdkairelRRNVGMVFQQYNLWPHLT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  88 VQQNI------GLGLNpgltlnasqreKRDAIARQMGI------ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDE 155
Cdd:PRK11124  99 VQQNLieapcrVLGLS-----------KDQALARAEKLlerlrlKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460 156 PFSALDPalrqEMLTLVSDICRERQ---LTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTD 215
Cdd:PRK11124 168 PTAALDP----EITAQIVSIIRELAetgITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
20-217 3.67e-40

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


Pssm-ID: 131368 [Multi-domain]  Cd Length: 243  Bit Score: 138.20  E-value: 3.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTP-----PSRRPVSMLFQENNLFSHLNVQQNI-- 92
Cdd:TIGR02315  23 LNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkklrKLRRRIGMIFQHYNLIERLTVLENVlh 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   93 -GLGLNPGL-----TLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:TIGR02315 103 gRLGYKPTWrsllgRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSK 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 877977460  167 EMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:TIGR02315 183 QVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
18-207 5.05e-40

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: 135.59  E-value: 5.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFShLNVQQNIglg 95
Cdd:cd03228   21 VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslRKNIAYVPQDPFLFS-GTIRENI--- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 lnpgltlnasqrekrdaiarqmgieslmarlpgeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:cd03228   97 ----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAL 142
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 877977460 176 CRERqlTLLMVSH---SVEDAARIaprsIVVADGR 207
Cdd:cd03228  143 AKGK--TVIVIAHrlsTIRDADRI----IVLDDGR 171
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
19-219 9.70e-40

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 137.21  E-value: 9.70e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS----RRpvSMLFQENNL-FShLNVQQNIG 93
Cdd:PRK13548  22 SLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarRR--AVLPQHSSLsFP-FTVEEVVA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 LGLNPgltLNASQREKRDAIARQM---GIESLMARLPGELSGGQRQRVALARCLVR------EQPVLLLDEPFSALDPAL 164
Cdd:PRK13548  99 MGRAP---HGLSRAEDDALVAAALaqvDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAH 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 165 RQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGK-----TDELLS 219
Cdd:PRK13548 176 QHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTpaevlTPETLR 235
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
19-219 9.84e-40

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 137.84  E-value: 9.84e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhTLTPPS----RRPVSMLFQE-NNLFSHLNVQQNIG 93
Cdd:PRK13635  27 SFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM--VLSEETvwdvRRQVGMVFQNpDNQFVGATVQDDVA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 LGL-NPGLTLNASQREKRDAIaRQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK13635 105 FGLeNIGVPREEMVERVDQAL-RQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETV 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13635 184 RQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
17-217 1.69e-39

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: 135.71  E-value: 1.69e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRPVSMLFQENNLFSHLNVQQNIGL- 94
Cdd:cd03263   20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSiRTDRKAARQSLGYCPQFDALFDELTVREHLRFy 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  95 ----GLNpgltlNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT 170
Cdd:cd03263  100 arlkGLP-----KSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWD 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 877977460 171 LVSDICRERqlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:cd03263  175 LILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
19-219 2.77e-39

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 138.29  E-value: 2.77e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS----RRPVSMLFQENNLFSHLNVQQNIG 93
Cdd:COG1135   25 SLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDlTALSERElraaRRKIGMIFQHFNLLSSRTVAENVA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 LglnPgLTLNASQREKRDAIARQM----GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:COG1135  105 L---P-LEIAGVPKAEIRKRVAELlelvGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSIL 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 877977460 170 TLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG1135  181 DLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
19-207 4.47e-39

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


Pssm-ID: 131721 [Multi-domain]  Cd Length: 214  Bit Score: 134.30  E-value: 4.47e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-----HTLTPPSRRPVSMLFQENNLFSHLNVQQNIG 93
Cdd:TIGR02673  22 SLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDvnrlrGRQLPLLRRRIGVVFQDFRLLPDRTVYENVA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   94 LGLN-PGLTLNASQREKRdAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:TIGR02673 102 LPLEvRGKKEREIQRRVG-AALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLL 180
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 877977460  173 SDICReRQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:TIGR02673 181 KRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
2-212 4.99e-39

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 135.14  E-value: 4.99e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   2 LKLIDITWLYHHLPMRF--TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLT-PPS-------RR 71
Cdd:COG4161    3 IQLKNINCFYGSHQALFdiNLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSqKPSekairllRQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  72 PVSMLFQENNLFSHLNVQQNIG------LGLNpgltlNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLV 145
Cdd:COG4161   83 KVGMVFQQYNLWPHLTVMENLIeapckvLGLS-----KEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 146 REQPVLLLDEPFSALDPALRQEmltlVSDICRERQ---LTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:COG4161  158 MEPQVLLFDEPTAALDPEITAQ----VVEIIRELSqtgITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
19-208 5.41e-39

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 134.07  E-value: 5.41e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-----HTLTPPSRRPVSMLFQENNLFSHLNVQQNIG 93
Cdd:cd03292   21 NISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrGRAIPYLRRKIGVVFQDFRLLPDRNVYENVA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 LGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVS 173
Cdd:cd03292  101 FALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLK 180
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 877977460 174 DIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:cd03292  181 KI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
19-219 6.49e-39

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 138.31  E-value: 6.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS------RRPVSMLFQENNLFSHLNVQQNI 92
Cdd:COG4175   47 SFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKelrelrRKKMSMVFQHFALLPHRTVLENV 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLN----PgltlnasqREKRDAIARQM----GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:COG4175  127 AFGLEiqgvP--------KAERRERAREAlelvGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLI 198
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460 165 RQEM----LTLVsdicRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG4175  199 RREMqdelLELQ----AKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILT 253
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
20-219 6.86e-39

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


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 135.64  E-value: 6.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhTLTPPS----RRPVSMLFQ--ENNLFSHLnVQQNIG 93
Cdd:TIGR04520  23 LSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD-TLDEENlweiRKKVGMVFQnpDNQFVGAT-VEDDVA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   94 LGL-NPGLtlNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:TIGR04520 101 FGLeNLGV--PREEMRKRvDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLET 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 877977460  172 VSDICRERQLTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELLS 219
Cdd:TIGR04520 179 IRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFS 225
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
19-218 7.16e-39

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: 134.83  E-value: 7.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASG-TLLIAGEDHTLTPPSR-RP----VSMLFQENnLFSHLNVQQ-- 90
Cdd:COG1119   23 SWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWElRKriglVSPALQLR-FPRDETVLDvv 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  91 ------NIGLGLNPGltlnASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:COG1119  102 lsgffdSIGLYREPT----DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGA 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 165 RQEMLTLVSDICRERQLTLLMVSHSVEDaarIAP---RSIVVADGRIAWQGKTDELL 218
Cdd:COG1119  178 RELLLALLDKLAAEGAPTLVLVTHHVEE---IPPgitHVLLLKDGRVVAAGPKEEVL 231
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
20-219 1.42e-38

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 134.47  E-value: 1.42e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPP----SRRPVsmLFQENNLFSHLNVQQNIGLG 95
Cdd:COG4559   22 LTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPwelaRRRAV--LPQHSSLAFPFTVEEVVALG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LNPGltlnASQREKRDAIARQ----MGIESLMARLPGELSGGQRQRVALARCL------VREQP-VLLLDEPFSALDPAL 164
Cdd:COG4559  100 RAPH----GSSAAQDRQIVREalalVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPrWLFLDEPTSALDLAH 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 165 RQEMLTLVSDICReRQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG4559  176 QHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLT 229
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
20-206 1.65e-38

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 134.06  E-value: 1.65e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTlTPPSRRPVsmLFQENNLFSHLNVQQNIGLGLNpg 99
Cdd:PRK11248  22 LTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-GPGAERGV--VFQNEGLLPWRNVQDNVAFGLQ-- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 ltLNASQREKRDAIARQM----GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:PRK11248  97 --LAGVEKMQRLEIAHQMlkkvGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKL 174
                        170       180       190
                 ....*....|....*....|....*....|.
gi 877977460 176 CRERQLTLLMVSHSVEDAARIAPRSIVVADG 206
Cdd:PRK11248 175 WQETGKQVLLITHDIEEAVFMATELVLLSPG 205
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
20-206 2.34e-38

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: 132.97  E-value: 2.34e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVsmlFQENNLFSHLNVQQNIGLGLNPG 99
Cdd:TIGR01184   6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVV---FQNYSLLPWLTVRENIALAVDRV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  100 L-TLNASQREK--RDAIArQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:TIGR01184  83 LpDLSKSERRAivEEHIA-LVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIW 161
                         170       180       190
                  ....*....|....*....|....*....|
gi 877977460  177 RERQLTLLMVSHSVEDAARIAPRSIVVADG 206
Cdd:TIGR01184 162 EEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
6-219 4.81e-38

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: 132.35  E-value: 4.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   6 DITWLYHhlPMRFTL-----AVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQ 78
Cdd:cd03253    5 NVTFAYD--PGRPVLkdvsfTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDiREVTLDSlRRAIGVVPQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  79 ENNLFsHLNVQQNIGLGlnpglTLNASQREKRDAiARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVRE 147
Cdd:cd03253   83 DTVLF-NDTIGYNIRYG-----RPDATDEEVIEA-AKAAQIHDKIMRFPdgydtivGErglkLSGGEKQRVAIARAILKN 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 148 QPVLLLDEPFSALDPALRQEMLTLVSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLS 219
Cdd:cd03253  156 PPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHrlsTIVNADKI----IVLKDGRIVERGTHEELLA 224
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
19-208 7.82e-38

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: 131.79  E-value: 7.82e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtLTPPS--------RRPVSMLFQENNLFSHLNVQQ 90
Cdd:COG4181   32 SLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD--LFALDedararlrARHVGFVFQSFQLLPTLTALE 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  91 NIGLglnPgLTLnasqREKRDAIAR------QMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:COG4181  110 NVML---P-LEL----AGRRDARARaralleRVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAAT 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 877977460 165 RQEMLTLVSDICRERQLTLLMVSHSVEDAARiAPRSIVVADGRI 208
Cdd:COG4181  182 GEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRL 224
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
18-195 8.41e-38

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


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 130.81  E-value: 8.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhTLTPPSRRPVSM-------LFQENNLFSHLNVQQ 90
Cdd:TIGR03608  17 LNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQE-TPPLNSKKASKFrreklgyLFQNFALIENETVEE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   91 NIGLGLnpgLTLNASQREKRDAIAR---QMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:TIGR03608  96 NLDLGL---KYKKLSKKEKREKKKEaleKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDE 172
                         170       180
                  ....*....|....*....|....*...
gi 877977460  168 MLTLVSDICRERQlTLLMVSHSVEDAAR 195
Cdd:TIGR03608 173 VLDLLLELNDEGK-TIIIVTHDPEVAKQ 199
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
19-208 1.90e-37

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 133.82  E-value: 1.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGL-N 97
Cdd:PRK11650  24 DLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQNYALYPHMSVRENMAYGLkI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  98 PGLTlnASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:PRK11650 104 RGMP--KAEIEERvAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLH 181
                        170       180       190
                 ....*....|....*....|....*....|..
gi 877977460 177 RERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:PRK11650 182 RRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
19-223 1.34e-36

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 132.85  E-value: 1.34e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAG------EDHTLTPPSRRPVSMLFQENNLFSHLNVQQNI 92
Cdd:PRK10070  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakiSDAELREVRRKKIAMVFQSFALMPHMTVLDNT 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQAS 223
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN 258
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
18-208 2.39e-36

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 128.66  E-value: 2.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRP--VSMLFQENNL--FSHLNVQQNIG 93
Cdd:COG1101   25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAkyIGRVFQDPMMgtAPSMTIEENLA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 L--------GLNPGltLNASQREK-RDAIAR-QMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:COG1101  105 LayrrgkrrGLRRG--LTKKRRELfRELLATlGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPK 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 877977460 164 LRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:COG1101  183 TAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
1-207 2.88e-36

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: 126.82  E-value: 2.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDIT------WLYHHLpmrfTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRPV 73
Cdd:COG4133    2 MLEAENLScrrgerLLFSGL----SFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPiRDAREDYRRRL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  74 SMLFQENNLFSHLNVQQNIGL--GLNPgltLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVL 151
Cdd:COG4133   78 AYLGHADGLKPELTVRENLRFwaALYG---LRADREAIDEALEA-VGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 152 LLDEPFSALDPALRQEMLTLVSDiCRERQLTLLMVSHSVEDAAriAPRSIVVADGR 207
Cdd:COG4133  154 LLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLELA--AARVLDLGDFK 206
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
29-222 3.87e-36

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 130.38  E-value: 3.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  29 AILGPSGAGKSTLLNLIAGFLAPASGtlLIAGEDHTLT--------PPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPgl 100
Cdd:PRK11144  28 AIFGRSGAGKTSLINAISGLTRPQKG--RIVLNGRVLFdaekgiclPPEKRRIGYVFQDARLFPHYKVRGNLRYGMAK-- 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 101 tlnaSQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQ 180
Cdd:PRK11144 104 ----SMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREIN 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 877977460 181 LTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQA 222
Cdd:PRK11144 180 IPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
19-218 7.08e-36

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 127.12  E-value: 7.08e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSR--RPVSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:COG4604   21 SLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQENHINSRLTVRELVAFGR 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 NP---GlTLNASQREK-RDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:COG4604  101 FPyskG-RLTAEDREIiDEAIAY-LDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLL 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELL 218
Cdd:COG4604  179 RRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
1-219 8.02e-36

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 129.54  E-value: 8.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDITWLYHHLPMRFT------LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS----- 69
Cdd:PRK11153   1 MIELKNISKVFPQGGRTIHalnnvsLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrka 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  70 RRPVSMLFQENNLFSHLNVQQNIGLglnPgLTLNASQREKRDAIARQM----GIESLMARLPGELSGGQRQRVALARCLV 145
Cdd:PRK11153  81 RRQIGMIFQHFNLLSSRTVFDNVAL---P-LELAGTPKAEIKARVTELlelvGLSDKADRYPAQLSGGQKQRVAIARALA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 877977460 146 REQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFS 230
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
20-219 2.03e-35

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 125.53  E-value: 2.03e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRP---VSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:COG1137   24 LEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRArlgIGYLPQEASIFRKLTVEDNILAVL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 NPgLTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDP-AlrqemltlVSD 174
Cdd:COG1137  104 EL-RKLSKKEREERlEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPiA--------VAD 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 877977460 175 I------CRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG1137  175 IqkiirhLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILN 225
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
18-219 3.18e-35

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: 124.96  E-value: 3.18e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFShLNVQQNIGLG 95
Cdd:cd03249   22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDiRDLNLRWlRSQIGLVSQEPVLFD-GTIAENIRYG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LNPGltlnasQREKRDAIARQMGIESLMARLP-----------GELSGGQRQRVALARCLVREQPVLLLDEPFSALD--- 161
Cdd:cd03249  101 KPDA------TDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDaes 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 162 PALRQEMLtlvSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLS 219
Cdd:cd03249  175 EKLVQEAL---DRAMKGR--TTIVIAHrlsTIRNADLI----AVLQNGQVVEQGTHDELMA 226
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
19-219 5.40e-35

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: 130.19  E-value: 5.40e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTL----LNLIagflaPASGTLLIAGED-HTLTP----PSRRPVSMLFQenNLFSHLN-- 87
Cdd:COG4172  306 SLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDlDGLSRralrPLRRRMQVVFQ--DPFGSLSpr 378
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  88 --VQQNIGLGL---NPGLTlnASQREKR-DAIARQMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:COG4172  379 mtVGQIIAEGLrvhGPGLS--AAERRARvAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSAL 456
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 161 DPALRQEMLTLVSDICRERQLTLLMVSH--SVEDAarIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG4172  457 DVSVQAQILDLLRDLQREHGLAYLFISHdlAVVRA--LAHRVMVMKDGKVVEQGPTEQVFD 515
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
18-219 6.77e-35

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: 124.27  E-value: 6.77e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFSHlNVQQNIGLG 95
Cdd:cd03251   21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDvRDYTLASlRRQIGLVSQDVFLFND-TVAENIAYG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 lnpglTLNASQREKRDAiARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDpaL 164
Cdd:cd03251  100 -----RPGATREEVEEA-ARAANAHEFIMELPegydtviGErgvkLSGGQRQRIAIARALLKDPPILILDEATSALD--T 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 165 RQEMltLVSDICRE--RQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLS 219
Cdd:cd03251  172 ESER--LVQAALERlmKNRTTFVIAHrlsTIENADRI----VVLEDGKIVERGTHEELLA 225
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
20-208 8.04e-35

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 124.79  E-value: 8.04e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLiAGEdhtlTPPS--RRPVSMLFQENNLFSHLNVQQNIGLGLN 97
Cdd:PRK11247  33 LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AGT----APLAeaREDTRLMFQDARLLPWKKVIDNVGLGLK 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  98 PGLTLNAsqrekRDAIArQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICR 177
Cdd:PRK11247 108 GQWRDAA-----LQALA-AVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQ 181
                        170       180       190
                 ....*....|....*....|....*....|.
gi 877977460 178 ERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:PRK11247 182 QHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
20-224 8.09e-35

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 124.53  E-value: 8.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIaGFL-APASGTLLIAGE--------DHTLTPPSRRPV-------SMLFQENNLF 83
Cdd:COG4598   29 LTARKGDVISIIGSSGSGKSTFLRCI-NLLeTPDSGEIRVGGEeirlkpdrDGELVPADRRQLqrirtrlGMVFQSFNLW 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  84 SHLNVQQNIGLGlnPgltLNASQREKRDAIARQM------GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPF 157
Cdd:COG4598  108 SHMTVLENVIEA--P---VHVLGRPKAEAIERAEallakvGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPT 182
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 158 SALDPALRQEMLTLVSDICRE-RqlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASA 224
Cdd:COG4598  183 SALDPELVGEVLKVMRDLAEEgR--TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSE 248
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
19-219 9.89e-35

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: 123.75  E-value: 9.89e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHlNVQQNIGLGl 96
Cdd:cd03252   22 SLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLFNR-SIRDNIALA- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 NPGLTlnasqREKRDAIARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:cd03252  100 DPGMS-----MERVIEAAKLAGAHDFISELPegydtivGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 877977460 166 QEMLTLVSDICRERqlTLLMVSHSVEdAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:cd03252  175 HAIMRNMHDICAGR--TVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLA 225
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
20-219 1.02e-34

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 124.09  E-value: 1.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIA----------GEDHTLTPPSRRPVSMLFQENNLFSHLNVQ 89
Cdd:PRK11264  24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtarslSQQKGLIRQLRQHVGFVFQNFNLFPHRTVL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  90 QNIGLGlnpGLTLNASQREKRDAIARQM----GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:PRK11264 104 ENIIEG---PVIVKGEPKEEATARARELlakvGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELV 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 877977460 166 QEMLTLVSDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK11264 181 GEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
19-217 5.44e-34

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 127.06  E-value: 5.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS---RRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:COG1129   24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaqAAGIAIIHQELNLVPNLSVAENIFLG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LNP--GLTLN-ASQREKRDAIARQMGIE-SLMARLpGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:COG1129  104 REPrrGGLIDwRAMRRRARELLARLGLDiDPDTPV-GDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRI 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 877977460 172 VSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:COG1129  183 IRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
19-224 1.41e-33

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: 127.29  E-value: 1.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFsHLNVQQNIGLGl 96
Cdd:TIGR03375 485 SLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVPQDPRLF-YGTLRDNIALG- 562
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   97 NPGLTLNASQRekrdaIARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:TIGR03375 563 APYADDEEILR-----AAELAGVTEFVRRHPdgldmqiGErgrsLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSE 637
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460  166 QEMLTLVSDICRERqlTLLMVSH--SVEDaarIAPRSIVVADGRIAWQGKTDELLSGQASA 224
Cdd:TIGR03375 638 ERFKDRLKRWLAGK--TLVLVTHrtSLLD---LVDRIIVMDNGRIVADGPKDQVLEALRKG 693
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
19-212 6.12e-33

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: 118.85  E-value: 6.12e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHlNVQQNIGLGL 96
Cdd:cd03245   24 SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLFYG-TLRDNITLGA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 npgltLNASQREKRDAiARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:cd03245  103 -----PLADDERILRA-AELAGVTDFVNKHPngldlqiGErgrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 877977460 166 QEMLTLVSDICRERqlTLLMVSHSVEdAARIAPRSIVVADGRIAWQG 212
Cdd:cd03245  177 ERLKERLRQLLGDK--TLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
19-219 7.55e-33

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: 120.93  E-value: 7.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAP---ASGTLLIAGED-HTLTPPSRRP-----VSMLFQENnlFSHLN-- 87
Cdd:COG0444   25 SFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDlLKLSEKELRKirgreIQMIFQDP--MTSLNpv 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  88 --VQQNIGLGLNPGLTLNASQREKRdAIA--RQMGI---ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:COG0444  103 mtVGDQIAEPLRIHGGLSKAEARER-AIEllERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTAL 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 161 DPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRsIVV--AdGRIAWQGKTDELLS 219
Cdd:COG0444  182 DVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADR-VAVmyA-GRIVEEGPVEELFE 240
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
19-217 1.68e-32

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 119.10  E-value: 1.68e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-----HTLTPPSRRPVSMLFQENNLFSHLNVQQNIG 93
Cdd:PRK11831  27 SLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipamsRSRLYTVRKRMSMLFQSGALFTDMNVFDNVA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 LGLN-----PGLTLNASQREKRDAIARQmGIESLMarlPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:PRK11831 107 YPLRehtqlPAPLLHSTVMMKLEAVGLR-GAAKLM---PSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 877977460 169 LTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK11831 183 VKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
18-212 2.87e-32

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: 115.87  E-value: 2.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRPVSMLFQENNLFShLNVQQNIGLgl 96
Cdd:cd03247   21 LSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPvSDLEKALSSLISVLNQRPYLFD-TTLRNNLGR-- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 npgltlnasqrekrdaiarqmgieslmarlpgELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:cd03247   98 --------------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVL 145
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 877977460 177 RERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQG 212
Cdd:cd03247  146 KDK--TLIWITHhltGIEHMDKI----LFLENGKIIMQG 178
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
1-218 3.03e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 118.17  E-value: 3.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDITWLYhhlPMRFTLA-------VERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE---DHTLTPpSR 70
Cdd:PRK13632   7 MIKVENVSFSY---PNSENNAlknvsfeINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGItisKENLKE-IR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  71 RPVSMLFQE-NNLFSHLNVQQNIGLGL-NPGLTlnasqREKRDAI----ARQMGIESLMARLPGELSGGQRQRVALARCL 144
Cdd:PRK13632  83 KKIGIIFQNpDNQFIGATVEDDIAFGLeNKKVP-----PKKMKDIiddlAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 877977460 145 VREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAArIAPRSIVVADGRIAWQGKTDELL 218
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEIL 230
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
29-212 7.71e-32

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: 115.75  E-value: 7.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  29 AILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-RRPVSMLFQENNLFSHLNVQQNIG-LGLNPGLtlNASQ 106
Cdd:cd03264   29 GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlRRRIGYLPQEFGVYPNFTVREFLDyIAWLKGI--PSKE 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 107 REKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERqlTLLM 185
Cdd:cd03264  107 VKARvDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVIL 184
                        170       180
                 ....*....|....*....|....*..
gi 877977460 186 VSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03264  185 STHIVEDVESLCNQVAVLNKGKLVFEG 211
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
19-211 9.63e-32

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: 113.68  E-value: 9.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRrpvsmlfqennlfshlnvqqniglglnp 98
Cdd:cd03216   20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD---------------------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  99 gltlnasqrekrdaiARQMGIESLMarlpgELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIcRE 178
Cdd:cd03216   72 ---------------ARRAGIAMVY-----QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL-RA 130
                        170       180       190
                 ....*....|....*....|....*....|...
gi 877977460 179 RQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQ 211
Cdd:cd03216  131 QGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
18-218 1.06e-31

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: 115.79  E-value: 1.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFSHlNVQQNIGLG 95
Cdd:cd03254   22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDiRDISRKSlRSMIGVVLQDTFLFSG-TIMENIRLG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 lnpgltLNASQREKRDAIARQMGIESLMARLP-----------GELSGGQRQRVALARCLVREQPVLLLDEPFSALDP-- 162
Cdd:cd03254  101 ------RPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTet 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 163 -ALRQEMLTLVSDicrerQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELL 218
Cdd:cd03254  175 eKLIQEALEKLMK-----GRTSIIIAHrlsTIKNADKI----LVLDDGKIIEEGTHDELL 225
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
18-219 1.15e-31

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 118.14  E-value: 1.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLavERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-----RRPVSMLFQenNLFSHLNVQQNI 92
Cdd:PRK11308  36 FTL--ERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkllRQKIQIVFQ--NPYGSLNPRKKV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLNPGLTLN-----ASQREKRDAIARQMGIESLMA-RLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:PRK11308 112 GQILEEPLLINtslsaAERREKALAMMAKVGLRPEHYdRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQA 191
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 877977460 167 EMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK11308 192 QVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFN 244
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
19-199 1.19e-31

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 114.64  E-value: 1.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQennlfshLNVQQNIGLGL-- 96
Cdd:NF040873  12 DLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLP-------LTVRDLVAMGRwa 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 --NPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:NF040873  85 rrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAE 164
                        170       180
                 ....*....|....*....|....*
gi 877977460 175 IcRERQLTLLMVSHSVEDAARIAPR 199
Cdd:NF040873 165 E-HARGATVVVVTHDLELVRRADPC 188
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
19-221 1.43e-31

type I secretion system ABC transporter, HlyB 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: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 121.77  E-value: 1.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHlNVQQNIGLGl 96
Cdd:TIGR01846 477 NLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFSR-SIRDNIALC- 554
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   97 NPGLTLnasqrEKRDAIARQMGIESLMARLP-----------GELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:TIGR01846 555 NPGAPF-----EHVIHAAKLAGAHDFISELPqgyntevgekgANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESE 629
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460  166 QEMLTLVSDICRERqlTLLMVSHSVeDAARIAPRSIVVADGRIAWQGKTDELLSGQ 221
Cdd:TIGR01846 630 ALIMRNMREICRGR--TVIIIAHRL-STVRACDRIIVLEKGQIAESGRHEELLALQ 682
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
20-219 1.67e-31

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 119.18  E-value: 1.67e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTL--TPPSRRpVSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:PRK09536  24 LSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvEALsaRAASRR-VASVPQDTSLSFEFDVRQVVEMGR 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 NPGLTLNASQREKRDAIARQ----MGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK09536 103 TPHRSRFDTWTETDRAAVERamerTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELV 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 877977460 173 SDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK09536 183 RRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
cbiO PRK13641
energy-coupling factor transporter ATPase;
22-221 2.09e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 116.47  E-value: 2.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  22 VERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS------RRPVSMLFQ--ENNLFSHlNVQQNIG 93
Cdd:PRK13641  30 LEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkklRKKVSLVFQfpEAQLFEN-TVLKDVE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 LG-LNPGLTlnaSQREKRDAIA--RQMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:PRK13641 109 FGpKNFGFS---EDEAKEKALKwlKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMM 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 877977460 170 TLVSDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQ 221
Cdd:PRK13641 186 QLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
19-224 2.35e-31

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 115.84  E-value: 2.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS---------------RRPVSMLFQENNLF 83
Cdd:PRK10619  25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrllRTRLTMVFQHFNLW 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  84 SHLNVQQNIGLGlnPGLTLNASQREKRDAIAR---QMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSA 159
Cdd:PRK10619 105 SHMTVLENVMEA--PIQVLGLSKQEARERAVKylaKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSA 182
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 160 LDPALRQEMLTLVSDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASA 224
Cdd:PRK10619 183 LDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
18-203 2.99e-31

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: 120.08  E-value: 2.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHlNVQQNIGLG 95
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAWVPQHPFLFAG-TIAENIRLA 419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   96 LnPGLTLNASQREKRDAIARQM------GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:TIGR02857 420 R-PDASDAEIREALERAGLDEFvaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVL 498
                         170       180       190
                  ....*....|....*....|....*....|....
gi 877977460  170 TLVSDICRERqlTLLMVSHSVEDAARiAPRSIVV 203
Cdd:TIGR02857 499 EALRALAQGR--TVLLVTHRLALAAL-ADRIVVL 529
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
19-212 3.23e-31

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: 114.39  E-value: 3.23e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhTLTPP--SRRPVSMLFQENNLFSHLNVQQNIGL-- 94
Cdd:cd03266   25 SFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD-VVKEPaeARRRLGFVSDSTGLYDRLTARENLEYfa 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  95 ---GLNPgltlnASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:cd03266  104 glyGLKG-----DELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 877977460 172 VSDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03266  179 IRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
20-193 3.67e-31

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


Pssm-ID: 130234 [Multi-domain]  Cd Length: 190  Bit Score: 113.29  E-value: 3.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE--DHT---LTPpSRRPVSMLFQ--ENNLFSHlNVQQNI 92
Cdd:TIGR01166  13 FAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEplDYSrkgLLE-RRQRVGLVFQdpDDQLFAA-DVDQDV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   93 GLG-LNPGLTLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:TIGR01166  91 AFGpLNLGLSEAEVERRVREALTA-VGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAI 169
                         170       180
                  ....*....|....*....|..
gi 877977460  172 VSDIcRERQLTLLMVSHSVEDA 193
Cdd:TIGR01166 170 LRRL-RAEGMTVVISTHDVDLA 190
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
23-219 4.19e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 115.67  E-value: 4.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  23 ERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLT--PPSRRPVSMLFQ--ENNLFSHlNVQQNIGLG-LN 97
Cdd:PRK13652  28 PRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEniREVRKFVGLVFQnpDDQIFSP-TVEQDIAFGpIN 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  98 PGLTlNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICR 177
Cdd:PRK13652 107 LGLD-EETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPE 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 877977460 178 ERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13652 186 TYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL 227
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
20-219 5.63e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 115.33  E-value: 5.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS----RRPVSMLFQ--ENNLFShLNVQQNIG 93
Cdd:PRK13636  27 INIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmklRESVGMVFQdpDNQLFS-ASVYQDVS 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 LG-LNPGLTLNASQREKRDAIARQmGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK13636 106 FGaVNLKLPEDEVRKRVDNALKRT-GIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLL 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13636 185 VEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
19-217 1.18e-30

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: 112.85  E-value: 1.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-RRPVSMLFQENNLFSHLNVQQNIGL-GL 96
Cdd:cd03265   20 SFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQDLSVDDELTGWENLYIhAR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 NPGLTlNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:cd03265  100 LYGVP-GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLK 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 877977460 177 RERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:cd03265  179 EEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
20-219 1.30e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 114.02  E-value: 1.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS----RRPVSMLFQ--ENNLFSHlNVQQNIG 93
Cdd:PRK13639  23 FKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllevRKTVGIVFQnpDDQLFAP-TVEEDVA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 LG-LNPGLTLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK13639 102 FGpLNLGLSKEEVEKRVKEALKA-VGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLL 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 877977460 173 SDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13639 181 YDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
19-217 1.38e-30

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 115.21  E-value: 1.38e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRP----VSMLFQenNLFSHLNVQQNIG 93
Cdd:COG4608   38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDiTGLSGRELRPlrrrMQMVFQ--DPYASLNPRMTVG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 LGLNPGLTLN--ASQREKRDAIA---RQMGIESLMA-RLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:COG4608  116 DIIAEPLRIHglASKAERRERVAellELVGLRPEHAdRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQ 195
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 877977460 168 MLTLVSDICRERQLTLLMVSH--SVedaAR-IAPRSIVVADGRIAWQGKTDEL 217
Cdd:COG4608  196 VLNLLEDLQDELGLTYLFISHdlSV---VRhISDRVAVMYLGKIVEIAPRDEL 245
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
22-218 1.68e-30

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


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 118.38  E-value: 1.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  22 VERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFshlN--VQQNIGLGlN 97
Cdd:COG5265  381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDiRDVTQASlRAAIGIVPQDTVLF---NdtIAYNIAYG-R 456
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  98 PGltlnASQREKRDAiARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:COG5265  457 PD----ASEEEVEAA-ARAAQIHDFIESLPdgydtrvGErglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTER 531
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 167 EMLTLVSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELL 218
Cdd:COG5265  532 AIQAALREVARGR--TTLVIAHrlsTIVDADEI----LVLEAGRIVERGTHAELL 580
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-219 2.33e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 113.67  E-value: 2.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDI---TWLYHHLPMRFTLA-----VERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhTLTPPS--- 69
Cdd:PRK13650   1 MSNIIEVknlTFKYKEDQEKYTLNdvsfhVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD--LLTEENvwd 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  70 -RRPVSMLFQE-NNLFSHLNVQQNIGLGL-NPGLTLNaSQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVR 146
Cdd:PRK13650  79 iRHKIGMVFQNpDNQFVGATVEDDVAFGLeNKGIPHE-EMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460 147 EQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAArIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFS 229
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
19-228 2.87e-30

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


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 112.98  E-value: 2.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-----RRPVSMLFQENnlFSHLN----VQ 89
Cdd:TIGR02769  31 SLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqrrafRRDVQLVFQDS--PSAVNprmtVR 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   90 QNIGLGLNPGLTLNASQREKR-DAIARQMGIES-LMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:TIGR02769 109 QIIGEPLRHLTSLDESEQKARiAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAV 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460  168 MLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:TIGR02769 189 ILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFKHPAGRNL 249
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
19-217 4.49e-30

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


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 111.46  E-value: 4.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRP---VSMLFQENNLFSHLNVQQNIGLG 95
Cdd:TIGR03410  20 SLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAragIAYVPQGREIFPRLTVEENLLTG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   96 LNpgltlnASQREKRDAIARQMGI----ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:TIGR03410 100 LA------ALPRRSRKIPDEIYELfpvlKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRV 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 877977460  172 VSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:TIGR03410 174 IRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
19-217 4.93e-30

daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]


Pssm-ID: 130256 [Multi-domain]  Cd Length: 302  Bit Score: 113.25  E-value: 4.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-RRPVSMLFQENNLFSHLNVQQNIGLgln 97
Cdd:TIGR01188  13 NFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKvRRSIGIVPQYASVDEDLTGRENLEM--- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   98 PGLTLNASQREKRDAIARQMGIESLMA---RLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:TIGR01188  90 MGRLYGLPKDEAEERAEELLELFELGEaadRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRA 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 877977460  175 IcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:TIGR01188 170 L-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
18-221 8.27e-30

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 112.00  E-value: 8.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE--DHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:PRK10253  26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiQHYASKEVARRIGLLAQNATTPGDITVQELVARG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LNPGLTLNASQR-EKRDAIARQM---GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK10253 106 RYPHQPLFTRWRkEDEEAVTKAMqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 877977460 172 VSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQ 221
Cdd:PRK10253 186 LSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAE 235
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
19-229 1.01e-29

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 111.14  E-value: 1.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTP---PSRRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:PRK10895  23 SLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhaRARRGIGYLPQEASIFRRLSVYDNLMAV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LNPGLTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:PRK10895 103 LQIRDDLSAEQREDRaNELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEH 182
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 175 IcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALLG 229
Cdd:PRK10895 183 L-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
19-228 1.82e-29

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 110.93  E-value: 1.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-----RRPVSMLFQENnlFSHLNVQQNIG 93
Cdd:PRK10419  32 SLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkafRRDIQMVFQDS--ISAVNPRKTVR 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 LGLNPGL----TLNASQREKR-DAIARQMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:PRK10419 110 EIIREPLrhllSLDKAERLARaSEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAG 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 168 MLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:PRK10419 190 VIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFSSPAGRVL 250
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
20-209 6.87e-29

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


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 108.21  E-value: 6.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSR-----RPVSMLFQENNLFSHLNVQQNIG 93
Cdd:TIGR02211  26 LSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSlSKLSSNERaklrnKKLGFIYQFHHLLPDFTALENVA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   94 LglnPGLTLNASQREKRD---AIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT 170
Cdd:TIGR02211 106 M---PLLIGKKSVKEAKErayEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFD 182
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 877977460  171 LVSDICRERQLTLLMVSHSVEDAARIaPRSIVVADGRIA 209
Cdd:TIGR02211 183 LMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLF 220
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
14-229 9.93e-29

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 108.54  E-value: 9.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  14 LPMRF---------TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPP---SRRPVSMLFQENN 81
Cdd:PRK11300  11 LMMRFggllavnnvNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqiARMGVVRTFQHVR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  82 LFSHLNVQQN--------IGLGLNPGL-TLNASQREKRDAIAR------QMGIESLMARLPGELSGGQRQRVALARCLVR 146
Cdd:PRK11300  91 LFREMTVIENllvaqhqqLKTGLFSGLlKTPAFRRAESEALDRaatwleRVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 147 EQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASA 226
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIKA 250

                 ...
gi 877977460 227 LLG 229
Cdd:PRK11300 251 YLG 253
cbiO PRK13649
energy-coupling factor transporter ATPase;
19-213 2.85e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 107.91  E-value: 2.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTP------PSRRPVSMLFQ--ENNLFSHlNVQQ 90
Cdd:PRK13649  27 NLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikQIRKKVGLVFQfpESQLFEE-TVLK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  91 NIGLG-LNPGLTlnasqREKRDAIARQ----MGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:PRK13649 106 DVAFGpQNFGVS-----QEEAEALAREklalVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 877977460 165 RQEMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGK 213
Cdd:PRK13649 181 RKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
19-212 3.45e-28

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: 106.65  E-value: 3.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtltPPSRRP-----VSMLF-QENNLFSHLNVQQNI 92
Cdd:cd03267   41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV----PWKRRKkflrrIGVVFgQKTQLWWDLPVIDSF 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GL-----GLNPgltlnASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:cd03267  117 YLlaaiyDLPP-----ARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 877977460 168 MLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03267  192 IRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
19-189 4.64e-28

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: 110.91  E-value: 4.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFsHLNVQQNIGLGl 96
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevRRRVSVCAQDAHLF-DTTVRENLRLA- 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   97 NPgltlNASQREKRDAiARQMGIESLMARLPG-----------ELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:TIGR02868 433 RP----DATDEELWAA-LERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETA 507
                         170       180
                  ....*....|....*....|....
gi 877977460  166 QEMLTLVSDICRERqlTLLMVSHS 189
Cdd:TIGR02868 508 DELLEDLLAALSGR--TVVLITHH 529
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
19-212 6.44e-28

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: 105.44  E-value: 6.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedHTLTPPSRRPVSMLFQENNLFSHLNVQ-QNIGLGLN 97
Cdd:cd03269   20 SFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--KPLDIAARNRIGYLPEERGLYPKMKVIdQLVYLAQL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  98 PGLTLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIcR 177
Cdd:cd03269   98 KGLKKEEARRRIDEWLER-LELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIREL-A 175
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 877977460 178 ERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03269  176 RAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
cbiO PRK13640
energy-coupling factor transporter ATPase;
19-219 7.97e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 106.81  E-value: 7.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAP-ASGTLLIAGEDHTLTPPS----RRPVSMLFQE-NNLFSHLNVQQNI 92
Cdd:PRK13640  27 SFSIPRGSWTALIGHNGSGKSTISKLINGLLLPdDNPNSKITVDGITLTAKTvwdiREKVGIVFQNpDNQFVGATVGDDV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGL-NPGLTLNASQREKRDAIArQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK13640 107 AFGLeNRAVPRPEMIKIVRDVLA-DVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKL 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 877977460 172 VSDICRERQLTLLMVSHSVEDAArIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13640 186 IRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFS 232
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
15-228 9.25e-28

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 110.32  E-value: 9.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  15 PMRFTLavERGEQVAILGPSGAGKSTLLNLIAGFLaPASGTLLIAG-EDHTLTPPS-RRPVSMLFQENNLFsHLNVQQNI 92
Cdd:PRK11174 368 PLNFTL--PAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGiELRELDPESwRKHLSWVGQNPQLP-HGTLRDNV 443
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGlNPgltlNASQREKRDAIArQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:PRK11174 444 LLG-NP----DASDEQLQQALE-NAWVSEFLPLLPqgldtpiGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 162 P--------ALRQEMltlvsdicreRQLTLLMVSHSVEDAARIaPRSIVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:PRK11174 518 AhseqlvmqALNAAS----------RRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAGGLFATLL 581
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
19-219 1.06e-27

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 105.87  E-value: 1.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSR--RPVSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:PRK11231  22 SLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQHHLTPEGITVRELVAYGR 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 NPGLT----LNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK11231 102 SPWLSlwgrLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLM 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 877977460 173 sdicRERQL---TLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK11231 182 ----RELNTqgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
18-222 1.36e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 107.24  E-value: 1.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLI---------AGEDHTLTPPS---------RRPVSMLFQ- 78
Cdd:PRK13631  45 ISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELITNPYSkkiknfkelRRRVSMVFQf 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  79 -ENNLFSHlNVQQNIGLGlnPgLTLNASQREKRDAIAR---QMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLL 153
Cdd:PRK13631 125 pEYQLFKD-TIEKDIMFG--P-VALGVKKSEAKKLAKFylnKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIF 200
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460 154 DEPFSALDPALRQEMLTLVSDiCRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQA 222
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
19-219 1.83e-27

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: 109.51  E-value: 1.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLI-AGEDHT-LTPP-------SRRPVSMLFQENNLFSHLNVQ 89
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVdMTKPgpdgrgrAKRYIGILHQEYDLYPHRTVL 383
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   90 QN----IGLGLNPGL-------TLNASQREKRDAiarqmgiESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFS 158
Cdd:TIGR03269 384 DNlteaIGLELPDELarmkaviTLKMVGFDEEKA-------EEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460  159 ALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
19-208 2.65e-27

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 109.43  E-value: 2.65e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLTPPSRRPVSMLFQENNLFSHLNVQQNI 92
Cdd:PRK10535  28 SLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvatldaDALAQLRREHFGFIFQRYHLLSHLTAAQNV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GL-GLNPGLTLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK10535 108 EVpAVYAGLERKQRLLRAQELLQR-LGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAI 186
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 877977460 172 VSDIcRERQLTLLMVSHSVEDAARiAPRSIVVADGRI 208
Cdd:PRK10535 187 LHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
4-208 3.20e-27

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 103.49  E-value: 3.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   4 LIDITWLYHHLPMRF---TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtlTPPSRRPVSMLFQEN 80
Cdd:cd03226    2 IENISFSYKKGTEILddlSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVMQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  81 NLFSHL---NVQQNIGLGLNPGltlnASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPF 157
Cdd:cd03226   79 DVDYQLftdSVREELLLGLKEL----DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 877977460 158 SALDPalrqEMLTLVSDICRERQL---TLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:cd03226  155 SGLDY----KNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGAI 204
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
18-219 6.90e-27

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 107.88  E-value: 6.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAG---EDHTLTPpSRRPVSMLFQENNLFSHlNVQQNIGL 94
Cdd:TIGR02203 351 ISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdlADYTLAS-LRRQVALVSQDVVLFND-TIANNIAY 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   95 GLNPGLTLNASQREKRDAIARQM------GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:TIGR02203 429 GRTEQADRAEIERALAAAYAQDFvdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLV 508
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 877977460  169 LTLVSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLS 219
Cdd:TIGR02203 509 QAALERLMQGR--TTLVIAHrlsTIEKADRI----VVMDDGRIVERGTHNELLA 556
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
19-208 8.71e-27

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: 101.52  E-value: 8.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHlNVQQNIglgl 96
Cdd:cd03246   22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNelGDHVGYLPQDDELFSG-SIAENI---- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 npgltlnasqrekrdaiarqmgieslmarlpgeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIc 176
Cdd:cd03246   97 ---------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL- 142
                        170       180       190
                 ....*....|....*....|....*....|..
gi 877977460 177 RERQLTLLMVSHSVEdAARIAPRSIVVADGRI 208
Cdd:cd03246  143 KAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
6-208 1.15e-26

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 102.55  E-value: 1.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   6 DITWLYHHLPMR-----FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE-----DHTLTppsRRPVSM 75
Cdd:cd03248   16 NVTFAYPTRPDTlvlqdVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyEHKYL---HSKVSL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  76 LFQENNLFSHlNVQQNIGLGLNP---GLTLNASQREKRDAIARQM--GIESLMARLPGELSGGQRQRVALARCLVREQPV 150
Cdd:cd03248   93 VGQEPVLFAR-SLQDNIAYGLQScsfECVKEAAQKAHAHSFISELasGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 151 LLLDEPFSALDPALRQEMLTLVSDiCRERQlTLLMVSH---SVEDAARIaprsIVVADGRI 208
Cdd:cd03248  172 LILDEATSALDAESEQQVQQALYD-WPERR-TVLVIAHrlsTVERADQI----LVLDGGRI 226
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
19-217 2.03e-26

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 102.42  E-value: 2.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLL---N----LIAGflAPASGTLLIAGED---HTLTPPS-RRPVSMLFQENNLFSHlN 87
Cdd:COG1117   31 NLDIPENKVTALIGPSGCGKSTLLrclNrmndLIPG--ARVEGEILLDGEDiydPDVDVVElRRRVGMVFQKPNPFPK-S 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  88 VQQNIGLGLNpgltLN-ASQREKRDAIARqmgiESL-MARLPGE-----------LSGGQRQRVALARCLVREQPVLLLD 154
Cdd:COG1117  108 IYDNVAYGLR----LHgIKSKSELDEIVE----ESLrKAALWDEvkdrlkksalgLSGGQQQRLCIARALAVEPEVLLMD 179
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 155 EPFSALDP--ALRQE--MLTLvsdicRErQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:COG1117  180 EPTSALDPisTAKIEelILEL-----KK-DYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
cbiO PRK13646
energy-coupling factor transporter ATPase;
20-219 2.63e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 102.94  E-value: 2.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIagEDHTLTP--------PSRRPVSMLFQ--ENNLFSHlNVQ 89
Cdd:PRK13646  28 TEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHktkdkyirPVRKRIGMVFQfpESQLFED-TVE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  90 QNIGLG-LNPGLTLNASQREKRDAIArQMGIE-SLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:PRK13646 105 REIIFGpKNFKMNLDEVKNYAHRLLM-DLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQ 183
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 877977460 168 MLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13646 184 VMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
18-218 3.28e-26

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: 106.18  E-value: 3.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSR--RPVSMLFQENNLFSHlNVQQNIGLg 95
Cdd:TIGR03796 498 FSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVlaNSVAMVDQDIFLFEG-TVRDNLTL- 575
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   96 LNPGLTLNASQREKRDAiarqmGIESLMARLPGE-----------LSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:TIGR03796 576 WDPTIPDADLVRACKDA-----AIHDVITSRPGGydaelaegganLSGGQRQRLEIARALVRNPSILILDEATSALDPET 650
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460  165 RQEmltlVSDICRERQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELL 218
Cdd:TIGR03796 651 EKI----IDDNLRRRGCTCIIVAHrlsTIRDCDEI----IVLERGKVVQRGTHEELW 699
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
19-212 3.82e-26

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: 101.19  E-value: 3.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFL---APASGTLLIAGEdhtltPPSR----RPVSMLFQENNLFSHLNVQQN 91
Cdd:cd03234   27 SLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQ-----PRKPdqfqKCVAYVRQDDILLPGLTVRET 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  92 IGLGLNPGLT--LNASQREKRDAIA--RQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:cd03234  102 LTYTAILRLPrkSSDAIRKKRVEDVllRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 877977460 168 MLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03234  182 LVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
19-218 4.90e-26

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 105.59  E-value: 4.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLtppsRRPVSMLFQENNLFSHlNVQQNI 92
Cdd:TIGR01193 494 SLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrHTL----RQFINYLPQEPYIFSG-SILENL 568
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   93 GLGLNPGLTLNASQR-----EKRDAIAR-QMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:TIGR01193 569 LLGAKENVSQDEIWAaceiaEIKDDIENmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEK 648
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 877977460  167 EmltLVSDICRERQLTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELL 218
Cdd:TIGR01193 649 K---IVNNLLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
2-219 4.94e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 102.47  E-value: 4.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   2 LKLIDITWLYHH-LPMRF------TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLL----------------I 58
Cdd:PRK13651   3 IKVKNIVKIFNKkLPTELkaldnvSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekeK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  59 AGEDHTLTPPS----------RRPVSMLFQ--ENNLFSHlNVQQNIGLG-LNPGLTLNASQREKRDAIaRQMGI-ESLMA 124
Cdd:PRK13651  83 VLEKLVIQKTRfkkikkikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFGpVSMGVSKEEAKKRAAKYI-ELVGLdESYLQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 125 RLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQlTLLMVSHSVEDAARIAPRSIVVA 204
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFK 239
                        250
                 ....*....|....*
gi 877977460 205 DGRIAWQGKTDELLS 219
Cdd:PRK13651 240 DGKIIKDGDTYDILS 254
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
19-228 6.53e-26

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 105.04  E-value: 6.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFSHlNVQQNIGLGl 96
Cdd:PRK13657 355 SFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDiRTVTRASlRRNIAVVFQDAGLFNR-SIEDNIRVG- 432
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 npglTLNASQREKRDAIARQMGIESLMARLPG----------ELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:PRK13657 433 ----RPDATDEEMRAAAERAQAHDFIERKPDGydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSALDVETEA 508
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 167 EMLTLVSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:PRK13657 509 KVKAALDELMKGR--TTFIIAHrlsTVRNADRI----LVFDNGRVVESGSFDELVARGGRFAALL 567
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
19-216 8.72e-26

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 104.34  E-value: 8.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS---RRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:COG3845   25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdaiALGIGMVHQHFMLVPNLTVAENIVLG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LNPGltlnASQREKRDAIARQmgIESLMARLP---------GELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:COG3845  105 LEPT----KGGRLDRKAARAR--IRELSERYGldvdpdakvEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEAD 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 877977460 167 EMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDE 216
Cdd:COG3845  179 ELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
20-208 1.02e-25

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 100.24  E-value: 1.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSR-----RPVSMLFQENNLFSHLNVQQNIG 93
Cdd:PRK10584  31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlHQMDEEARaklraKHVGFVFQSFMLIPTLNALENVE 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 LglnPGLTLNASQREKRD---AIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT 170
Cdd:PRK10584 111 L---PALLRGESSRQSRNgakALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 877977460 171 LVSDICRERQLTLLMVSHSVEDAARiAPRSIVVADGRI 208
Cdd:PRK10584 188 LLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
2-221 1.46e-25

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 104.14  E-value: 1.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   2 LKLIDITWLYHHLPM----RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSM 75
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpvlkGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAalRQAISV 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  76 LFQENNLFSHlNVQQNIGLGLNpgltlNASQrEKRDAIARQMGIESLMARLPG----------ELSGGQRQRVALARCLV 145
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNLLLAAP-----NASD-EALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALL 491
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460 146 REQPVLLLDEPFSALDPALRQEMLTLVSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLSGQ 221
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHrltGLEQFDRI----CVMDNGQIIEQGTHQELLAQQ 564
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
20-221 1.69e-25

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: 99.54  E-value: 1.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtlTPPSRRPVSMLFQENNLFSH--LNVQQN------ 91
Cdd:TIGR03771   1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS---PGKGWRHIGYVPQRHEFAWDfpISVAHTvmsgrt 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   92 --IGLGLNPGLtlnASQREKRDAIaRQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:TIGR03771  78 ghIGWLRRPCV---ADFAAVRDAL-RRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 877977460  170 TLVSDICRErQLTLLMVSHSVEDAARIAPRsIVVADGRIAWQGKTDELLSGQ 221
Cdd:TIGR03771 154 ELFIELAGA-GTAILMTTHDLAQAMATCDR-VVLLNGRVIADGTPQQLQDPA 203
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
20-219 1.91e-25

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: 103.61  E-value: 1.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKS----TLLNLIAGFLAPASGTLLIAGEDHTLTPPSR------RPVSMLFQE-----NNLFS 84
Cdd:COG4172   31 FDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQEpmtslNPLHT 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  85 hlnVQQNIGLGLNPGLTLNASQREKRdAIA--RQMGI---ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSA 159
Cdd:COG4172  111 ---IGKQIAEVLRLHRGLSGAAARAR-ALEllERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTA 186
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 160 LDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG4172  187 LDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFA 246
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
19-228 2.17e-25

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 104.03  E-value: 2.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLtppsRRPVSMLFQENNLFSHlNVQQNI 92
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPlvqydhHYL----HRQVALVGQEPVLFSG-SVRENI 575
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   93 GLGLNpgltlnASQREKRDAIARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:TIGR00958 576 AYGLT------DTPDEEIMAAAKAANAHDFIMEFPngydtevGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  162 PALRQemlTLVSDICRErQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:TIGR00958 650 AECEQ---LLQESRSRA-SRTVLLIAHrlsTVERADQI----LVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
20-212 2.80e-25

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: 98.44  E-value: 2.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLN-P 98
Cdd:cd03268   21 LHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGFYPNLTARENLRLLARlL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  99 GLtlnasqREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIcR 177
Cdd:cd03268  101 GI------RKKRiDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSL-R 173
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 877977460 178 ERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03268  174 DQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
25-208 3.46e-25

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 98.41  E-value: 3.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-----HTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPG 99
Cdd:PRK10908  28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrlkNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 LTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICREr 179
Cdd:PRK10908 108 GASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV- 186
                        170       180
                 ....*....|....*....|....*....
gi 877977460 180 QLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:PRK10908 187 GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
18-189 4.13e-25

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 98.25  E-value: 4.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLavERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHlNVQQNIglg 95
Cdd:PRK10247  28 FSL--RAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyRQQVSYCAQTPTLFGD-TVYDNL--- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LNPGLTLNasQREKRDAIAR---QMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK10247 102 IFPWQIRN--QQPDPAIFLDdleRFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEI 179
                        170
                 ....*....|....*...
gi 877977460 172 VSDICRERQLTLLMVSHS 189
Cdd:PRK10247 180 IHRYVREQNIAVLWVTHD 197
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
20-219 6.68e-25

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 102.34  E-value: 6.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED--HTLTPPSRRPVSMLFQENNLFSHlNVQQNIgLGLN 97
Cdd:TIGR03797 474 LQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDlaGLDVQAVRRQLGVVLQNGRLMSG-SIFENI-AGGA 551
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   98 PgLTLNASQREKR------DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDpalrQEMLTL 171
Cdd:TIGR03797 552 P-LTLDEAWEAARmaglaeDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD----NRTQAI 626
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 877977460  172 VSDICRERQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLS 219
Cdd:TIGR03797 627 VSESLERLKVTRIVIAHrlsTIRNADRI----YVLDAGRVVQQGTYDELMA 673
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
19-222 1.05e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 98.65  E-value: 1.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtLTPPS----RRPVSMLFQ--ENNLFShLNVQQNI 92
Cdd:PRK13647  25 SLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE--VNAENekwvRSKVGLVFQdpDDQVFS-STVWDDV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLG-LNPGLTLNASQREKRDAIaRQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPAlRQEMLTL 171
Cdd:PRK13647 102 AFGpVNMGLDKDEVERRVEEAL-KAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR-GQETLME 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 172 VSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGK----TDELLSGQA 222
Cdd:PRK13647 180 ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDksllTDEDIVEQA 234
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
18-219 1.96e-24

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 97.22  E-value: 1.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGfLAPASGTLLIAGEDHTLTPPSR--RPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:COG4138   15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALH 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LNPGLTLNASQREKrDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPV-------LLLDEPFSALDPALRQEM 168
Cdd:COG4138   94 QPAGASSEAVEQLL-AQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTinpegqlLLLDEPMNSLDVAQQAAL 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 877977460 169 LTLVSDICrERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG4138  173 DRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
11-212 2.01e-24

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 100.94  E-value: 2.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  11 YHHLPMRFTLAVERGEQVAILGPSGAGKST----LLNLIAgflapASGTLLIAGED-HTLTP----PSRRPVSMLFQENN 81
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPlHNLNRrqllPVRHRIQVVFQDPN 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  82 --LFSHLNVQQNIGLGL---NPglTLNASQREKR-DAIARQMGIE-SLMARLPGELSGGQRQRVALARCLVREQPVLLLD 154
Cdd:PRK15134 373 ssLNPRLNVLQIIEEGLrvhQP--TLSAAQREQQvIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 155 EPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
20-217 2.29e-24

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 97.39  E-value: 2.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLN----LIAGFLAPASGTLLI------AGEDHTLTPPSRRPVSMLFQENNLFSHLNVQ 89
Cdd:PRK09984  25 LNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLgrtvqrEGRLARDIRKSRANTGYIFQQFNLVNRLSVL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  90 QNI---GLGLNPGLT-----LNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:PRK09984 105 ENVligALGSTPFWRtcfswFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 162 PALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK09984 185 PESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
cbiO PRK13643
energy-coupling factor transporter ATPase;
20-208 2.68e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 97.88  E-value: 2.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTP------PSRRPVSMLFQ--ENNLFSHlNVQQN 91
Cdd:PRK13643  27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeikPVRKKVGVVFQfpESQLFEE-TVLKD 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  92 IGLG-LNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT 170
Cdd:PRK13643 106 VAFGpQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ 185
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 877977460 171 LVSDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:PRK13643 186 LFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHI 222
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
19-219 2.78e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 97.47  E-value: 2.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS---RRPVSMLFQ--ENNLFSHLnVQQNIG 93
Cdd:PRK13633  30 NLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwdiRNKAGMVFQnpDNQIVATI-VEEDVA 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 -----LGLNPgltlnASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:PRK13633 109 fgpenLGIPP-----EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREV 183
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 877977460 169 LTLVSDICRERQLTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13633 184 VNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFK 233
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
19-208 2.79e-24

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 96.42  E-value: 2.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSR-----RPVSMLFQENNLFSHLNVQQNI 92
Cdd:PRK11629  29 SFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmSKLSSAAKaelrnQKLGFIYQFHHLLPDFTALENV 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK11629 109 AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLL 188
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARIApRSIVVADGRI 208
Cdd:PRK11629 189 GELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
19-221 4.24e-24

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 97.57  E-value: 4.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRPVSMLFQENNLFSHLNVQQNIGL-GL 96
Cdd:PRK13537  27 SFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPvPSRARHARQRVGVVPQFDNLDPDFTVRENLLVfGR 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 NPGLTlNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT-LVSDI 175
Cdd:PRK13537 107 YFGLS-AAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWErLRSLL 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 877977460 176 CRERqlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQ 221
Cdd:PRK13537 186 ARGK--TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
18-163 6.71e-24

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 94.56  E-value: 6.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAveRGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRpVSMLFQENNLFSHLNVQQNIGLGLN 97
Cdd:PRK13539  23 FTLA--AGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVAENLEFWAA 99
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460  98 pglTLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:PRK13539 100 ---FLGGEELDIAAALEA-VGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
cbiO PRK13642
energy-coupling factor transporter ATPase;
19-219 7.58e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 96.32  E-value: 7.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhTLTPPS----RRPVSMLFQE-NNLFSHLNVQQNIG 93
Cdd:PRK13642  27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE--LLTAENvwnlRRKIGMVFQNpDNQFVGATVEDDVA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 LGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVS 173
Cdd:PRK13642 105 FGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIH 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 877977460 174 DICRERQLTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13642 185 EIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
29-219 1.09e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 95.36  E-value: 1.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  29 AILGPSGAGKSTLLNLIAGFL-----APASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHLNVQQNIGLGLNPGLT 101
Cdd:PRK14247  33 ALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIelRRRVQMVFQIPNPIPNLSIFENVALGLKLNRL 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 102 LNAS---QREKRDAIARQMGIESLMARL---PGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:PRK14247 113 VKSKkelQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL 192
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 877977460 176 crERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK14247 193 --KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
29-218 1.16e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 95.29  E-value: 1.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  29 AILGPSGAGKSTLLNLIAGFL-----APASGTLLIAGED---HTLTPPS-RRPVSMLFQENNLFSHLNVQQNIGLGLNpg 99
Cdd:PRK14267  34 ALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNiysPDVDPIEvRREVGMVFQYPNPFPHLTIYDNVAIGVK-- 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 ltLNASQREKRD-------AIARQMGIESLMARL---PGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:PRK14267 112 --LNGLVKSKKEldervewALKKAALWDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIE 189
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 877977460 170 TLVSDIcrERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELL 218
Cdd:PRK14267 190 ELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
18-210 1.28e-23

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 98.21  E-value: 1.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAgedHTLTppsrrpVSMLFQEN-NLFSHLNVQQNIGlGL 96
Cdd:COG0488  334 LSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG---ETVK------IGYFDQHQeELDPDKTVLDELR-DG 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 NPGLTlnasQREKRDAIARqMGIESLMARLP-GELSGGQRQRVALARCLVREQPVLLLDEPFSALDPalrqEMLTLVSDI 175
Cdd:COG0488  404 APGGT----EQEVRGYLGR-FLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI----ETLEALEEA 474
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 877977460 176 CRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAW 210
Cdd:COG0488  475 LDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
19-218 2.14e-23

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 95.92  E-value: 2.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedhtLTPPSRRP-----VSMLF-QENNLFSHLNVQQNi 92
Cdd:COG4586   42 SFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG----YVPFKRRKefarrIGVVFgQRSQLWWDLPAIDS- 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 glglnpgLTLNAS--------QREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:COG4586  117 -------FRLLKAiyripdaeYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 877977460 165 RQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELL 218
Cdd:COG4586  190 KEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELK 243
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
19-229 2.78e-23

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 93.79  E-value: 2.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS---RRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:PRK11614  25 SLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkimREAVAIVPEGRRVFSRMTVEENLAMG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 lnpGLTLNASQREKRdaIARqmgIESLMARL-------PGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:PRK11614 105 ---GFFAERDQFQER--IKW---VYELFPRLherriqrAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQI 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 169 LTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALLG 229
Cdd:PRK11614 177 FDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
15-219 3.56e-23

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 94.09  E-value: 3.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  15 PMRFTLavERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIagEDHTLT-----PPSRRpVSMLFQENNlfSHLNVQ 89
Cdd:PRK15112  31 PLSFTL--REGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI--DDHPLHfgdysYRSQR-IRMIFQDPS--TSLNPR 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  90 QNIGLGLNPGLTLN----ASQREKR-DAIARQMGIESLMARL-PGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:PRK15112 104 QRISQILDFPLRLNtdlePEQREKQiIETLRQVGLLPDHASYyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 164 LRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK15112 184 MRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1-217 3.74e-23

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 94.79  E-value: 3.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDITwlyhhlpMRF---------TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtLTPPSRR 71
Cdd:COG4152    1 MLELKGLT-------KRFgdktavddvSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP--LDPEDRR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  72 PVSMLFQENNLFSHLNVQQNIG-LG-LNpGLTLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQP 149
Cdd:COG4152   72 RIGYLPEERGLYPKMKVGEQLVyLArLK-GLSKAEAKRRADEWLER-LGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 877977460 150 VLLLDEPFSALDP----ALRQEMLTLvsdicRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:COG4152  150 LLILDEPFSGLDPvnveLLKDVIREL-----AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
29-224 6.89e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 93.62  E-value: 6.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  29 AILGPSGAGKSTLL-------NLIAGFlaPASGTLLIAGE---DHTLTPPSRRPVSMLFQENNLFShLNVQQNIGLG--- 95
Cdd:PRK14271  51 SLMGPTGSGKTTFLrtlnrmnDKVSGY--RYSGDVLLGGRsifNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGvra 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 --LNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVS 173
Cdd:PRK14271 128 hkLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR 207
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 877977460 174 DICreRQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASA 224
Cdd:PRK14271 208 SLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
18-217 7.14e-23

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 96.27  E-value: 7.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLavERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHT-LTPPSRRPVSMLF--QENNLFSHLNVQQNIGL 94
Cdd:PRK15439  32 FTL--HAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArLTPAKAHQLGIYLvpQEPLLFPNLSVKENILF 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  95 glnpGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPAlrqEMLTLVSD 174
Cdd:PRK15439 110 ----GLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPA---ETERLFSR 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 877977460 175 I--CRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK15439 183 IreLLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
19-219 1.02e-22

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 92.80  E-value: 1.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLA------PASGTLLIAGED--HTLTPPSRRPVSMLFQENNLFSHLNVQQ 90
Cdd:PRK14246  30 TIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDifQIDAIKLRKEVGMVFQQPNPFPHLSIYD 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  91 NIGLGLNP-GLTLNASQREKRDAIARQMGI-ESLMARL---PGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:PRK14246 110 NIAYPLKShGIKEKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNS 189
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 877977460 166 QEMLTLVSDIcrERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK14246 190 QAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
cbiO PRK13645
energy-coupling factor transporter ATPase;
19-221 1.14e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 93.53  E-value: 1.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAgeDHTLtpPS-----------RRPVSMLFQ--ENNLFSH 85
Cdd:PRK13645  31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG--DYAI--PAnlkkikevkrlRKEIGLVFQfpEYQLFQE 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  86 lNVQQNIGLGlnpGLTLNASQREKRDAIARQMGIESL----MARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:PRK13645 107 -TIEKDIAFG---PVNLGENKQEAYKKVPELLKLVQLpedyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 162 PALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQ 221
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQ 242
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
18-208 1.74e-22

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: 90.18  E-value: 1.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRpvsmlfqennlfshlnvqQNIGLGLN 97
Cdd:cd03215   19 VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA------------------IRAGIAYV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  98 PGltlnasQReKRDAIARQMGIESLMArLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIcR 177
Cdd:cd03215   81 PE------DR-KREGLVLDLSVAENIA-LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-A 151
                        170       180       190
                 ....*....|....*....|....*....|.
gi 877977460 178 ERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:cd03215  152 DAGKAVLLISSELDELLGLCDRILVMYEGRI 182
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
19-212 2.51e-22

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: 90.30  E-value: 2.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPA--SGTLLIAGEDHTLTPPSRRpVSMLFQENNLFSHLNVQqniglgl 96
Cdd:cd03213   29 SGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVR------- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 npgltlnasqrekrdaiarqmgiESLM--ARLPGeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:cd03213  101 -----------------------ETLMfaAKLRG-LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRR 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 877977460 175 ICRErQLTLLMVSHSvedaariaPRS---------IVVADGRIAWQG 212
Cdd:cd03213  157 LADT-GRTIICSIHQ--------PSSeifelfdklLLLSQGRVIYFG 194
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
19-219 2.91e-22

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: 94.43  E-value: 2.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRP-VSMLFQENNLFSHlNVQQNIGLgl 96
Cdd:COG4618  352 SFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADlSQWDREELGRhIGYLPQDVELFDG-TIAENIAR-- 428
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 npgltLNASQREKRDAIARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDP--- 162
Cdd:COG4618  429 -----FGDADPEKVVAAAKLAGVHEMILRLPdgydtriGEggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDege 503
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 163 -ALRQEMLTLvsdicRERQLTLLMVSHSVEdAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG4618  504 aALAAAIRAL-----KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVLA 555
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
19-216 4.13e-22

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 90.91  E-value: 4.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhtltppsrrpVSMLFqennlfshlnvqqNIGLGLNP 98
Cdd:COG1134   46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-----------VSALL-------------ELGAGFHP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  99 GLT------LNASQ--------REKRDAIARQMGIESLMaRLP-GELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:COG1134  102 ELTgreniyLNGRLlglsrkeiDEKFDEIVEFAELGDFI-DQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 877977460 164 LRQEMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDE 216
Cdd:COG1134  181 FQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
25-218 4.66e-22

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 91.14  E-value: 4.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLTPPSRRpvsMLFQENNLFshlnVQQNIGLGLNP 98
Cdd:PRK11701  32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlYALSEAERR---RLLRTEWGF----VHQHPRDGLRM 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  99 GLTLNASQREK------------RDAIARQMG-IESLMAR---LPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDP 162
Cdd:PRK11701 105 QVSAGGNIGERlmavgarhygdiRATAGDWLErVEIDAARiddLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV 184
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 163 ALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELL 218
Cdd:PRK11701 185 SVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
19-219 5.00e-22

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: 93.95  E-value: 5.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLTPPsrrpVSMLFQENNLFSHlNVQQNI 92
Cdd:TIGR01842 338 SFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADlkqwdrETFGKH----IGYLPQDVELFPG-TVAENI 412
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   93 G-LGLNPgltlnasQREKRDAIARQMGIESLMARLP-----------GELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:TIGR01842 413 ArFGENA-------DPEKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460  161 DP----ALRQEMLTLvsdicRERQLTLLMVSHSVEdAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:TIGR01842 486 DEegeqALANAIKAL-----KARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLA 542
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
26-217 7.12e-22

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 90.61  E-value: 7.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  26 EQVAILGPSGAGKSTLLNLI--AGFLAP---ASGTLLIAGED----HTLTPPSRRPVSMLFQENNLFShLNVQQNI--GL 94
Cdd:PRK14239  32 EITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNiyspRTDTVDLRKEIGMVFQQPNPFP-MSIYENVvyGL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  95 GLNpGLTLNASQREKRDAIARQMGI-ESLMARLPGE---LSGGQRQRVALARCLVREQPVLLLDEPFSALDP---ALRQE 167
Cdd:PRK14239 111 RLK-GIKDKQVLDEAVEKSLKGASIwDEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPisaGKIEE 189
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 877977460 168 MLTLVSDicrerQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK14239 190 TLLGLKD-----DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
18-230 8.02e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 90.58  E-value: 8.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTL-----AVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIagEDHTLTPPS----RRPVSMLFQE-NNLFSHLN 87
Cdd:PRK13648  23 FTLkdvsfNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY--NNQAITDDNfeklRKHIGIVFQNpDNQFVGSI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  88 VQQNIGLGL-NPGLTLNASQREKRDAIaRQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:PRK13648 101 VKYDVAFGLeNHAVPYDEMHRRVSEAL-KQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 877977460 167 EMLTLVSDICRERQLTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELLSgqaSASALLGI 230
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD---HAEELTRI 239
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
18-219 8.69e-22

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 89.99  E-value: 8.69e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLaPASGTLLIAG---EDHTLTPPSRRPVSMLFQENNLFShLNVQQNIGL 94
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGqplEAWSAAELARHRAYLSQQQTPPFA-MPVFQYLTL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  95 GLNPGLTLNASQREKRDaIARQMGIESLMARLPGELSGGQRQRVALARCLVREQP-------VLLLDEPFSALDPALRQE 167
Cdd:PRK03695  93 HQPDKTRTEAVASALNE-VAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLDVAQQAA 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 877977460 168 MLTLVSDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK03695 172 LDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLT 222
cbiO PRK13644
energy-coupling factor transporter ATPase;
20-219 9.00e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 90.82  E-value: 9.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAG---EDHTLTPPSRRPVSMLFQE-NNLFSHLNVQQNIGLG 95
Cdd:PRK13644  23 LVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtGDFSKLQGIRKLVGIVFQNpETQFVGRTVEEDLAFG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 lNPGLTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:PRK13644 103 -PENLCLPPIEIRKRvDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKK 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 877977460 175 IcRERQLTLLMVSHSVEDaARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13644 182 L-HEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLS 224
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
17-212 1.50e-21

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 93.15  E-value: 1.50e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:TIGR01257  948 RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDiETNLDAVRQSLGMCPQHNILFHHLTVAEHILFY 1027
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    96 LN-PGLTLNASQREKrDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:TIGR01257 1028 AQlKGRSWEEAQLEM-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK 1106
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 877977460   175 ICRERqlTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:TIGR01257 1107 YRSGR--TIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
20-218 1.80e-21

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 92.39  E-value: 1.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAG---EDHTLTPpSRRPVSMLFQENNLFSHlNVQQNIGLGL 96
Cdd:PRK11176 364 FKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLAS-LRNQVALVSQNVHLFND-TIANNIAYAR 441
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 NPGLTLNASQREKRDAIArqMGIESLMAR----LPGE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:PRK11176 442 TEQYSREQIEEAARMAYA--MDFINKMDNgldtVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAI 519
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 877977460 169 LTLVSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELL 218
Cdd:PRK11176 520 QAALDELQKNR--TSLVIAHrlsTIEKADEI----LVVEDGEIVERGTHAELL 566
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
10-221 3.10e-21

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 89.08  E-value: 3.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  10 LYHHLPMRFTLaverGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE--DHTLTPPSRRPVSMLFQENNLFSHLN 87
Cdd:PRK10575  26 LLHPLSLTFPA----GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplESWSSKAFARKVAYLPQQLPAAEGMT 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  88 VQQNIGLGLNP---GL-TLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:PRK10575 102 VRELVAIGRYPwhgALgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 164 LRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQ 221
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
19-188 6.85e-21

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 90.51  E-value: 6.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIagedhtltPPSRRpVSMLFQENNLFSHLNVQQNIGLGLNP 98
Cdd:COG0488   18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------PKGLR-IGYLPQEPPLDDDLTVLDTVLDGDAE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  99 GLTLnasqREKRDAIARQMG---------------------------IESLMARL----------PGELSGGQRQRVALA 141
Cdd:COG0488   89 LRAL----EAELEELEAKLAepdedlerlaelqeefealggweaearAEEILSGLgfpeedldrpVSELSGGWRRRVALA 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 877977460 142 RCLVREQPVLLLDEPFSALD-PALR--QEMLtlvsdicRERQLTLLMVSH 188
Cdd:COG0488  165 RALLSEPDLLLLDEPTNHLDlESIEwlEEFL-------KNYPGTVLVVSH 207
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
18-202 7.14e-21

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: 87.85  E-value: 7.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVE-----RGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNvqqni 92
Cdd:cd03237   13 FTLEVEggsisESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRDLLSSITK----- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGlnpgltlnaSQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDpalrQEMLTLV 172
Cdd:cd03237   88 DFY---------THPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD----VEQRLMA 154
                        170       180       190
                 ....*....|....*....|....*....|....
gi 877977460 173 SDICR----ERQLTLLMVSHSVEDAARIAPRSIV 202
Cdd:cd03237  155 SKVIRrfaeNNEKTAFVVEHDIIMIDYLADRLIV 188
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
25-219 9.31e-21

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 90.49  E-value: 9.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   25 GEQVAILGPSGAGKSTLLNLIAGFLAPA---SGTLLIAGedHTLTPPSRRPVSMLFQENNLF-------SHLNVQQNIGL 94
Cdd:TIGR00955  51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNG--MPIDAKEMRAISAYVQQDDLFiptltvrEHLMFQAHLRM 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   95 GLNpgltLNASQREKR-DAIARQMGIES-------LMARLPGeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:TIGR00955 129 PRR----VTKKEKRERvDEVLQALGLRKcantrigVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 877977460  167 EMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:TIGR00955 204 SVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
15-163 1.19e-20

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 85.87  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   15 PMRFTLAVerGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRrpvsmlfQENNLF-SHLNvqqnig 93
Cdd:TIGR01189  18 GLSFTLNA--GEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-------HENILYlGHLP------ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   94 lGLNPGLT-----------LNASQREKRDAIArQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDP 162
Cdd:TIGR01189  83 -GLKPELSalenlhfwaaiHGGAQRTIEDALA-AVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160

                  .
gi 877977460  163 A 163
Cdd:TIGR01189 161 A 161
galliderm_ABC TIGR03740
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ...
19-216 1.72e-20

gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.


Pssm-ID: 163452 [Multi-domain]  Cd Length: 223  Bit Score: 86.30  E-value: 1.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLglnp 98
Cdd:TIGR03740  20 SLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDG--HPWTRKDLHKIGSLIESPPLYENLTARENLKV---- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   99 gLTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIcR 177
Cdd:TIGR03740  94 -HTTLLGLPDSRiDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQELRELIRSF-P 171
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 877977460  178 ERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDE 216
Cdd:TIGR03740 172 EQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
19-217 4.92e-20

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 86.68  E-value: 4.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtLTPPS-------RRPVSMLFQENnlFSHLNVQQN 91
Cdd:PRK15079  41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKD--LLGMKddewravRSDIQMIFQDP--LASLNPRMT 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  92 IG-------LGLNPGLTlNASQREKRDAIARQMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:PRK15079 117 IGeiiaeplRTYHPKLS-RQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 877977460 164 LRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK15079 196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
18-207 5.15e-20

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: 84.79  E-value: 5.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTL---TPPSRRPVSMLFQENNLFS-HLNV---QQ 90
Cdd:COG4778   30 VSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVdlaQASPREILALRRRTIGYVSqFLRViprVS 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  91 NIGLGLNPGLTLNASQREKRD---AIARQMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:COG4778  110 ALDVVAEPLLERGVDREEARArarELLARLNLpERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRA 189
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 877977460 167 EMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:COG4778  190 VVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
19-209 9.82e-20

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: 84.08  E-value: 9.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLtppsRRPVSMLFQENNLFSHlNVQQNi 92
Cdd:cd03244   24 SFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskiglHDL----RSRISIIPQDPVLFSG-TIRSN- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 glgLNPgltLNASQREKRDAIARQMGIESLMARLPGEL-----------SGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:cd03244   98 ---LDP---FGEYSDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEATASVD 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 877977460 162 PALRQEMLTLVSDICRERqlTLLMVSHSVE---DAARIaprsIVVADGRIA 209
Cdd:cd03244  172 PETDALIQKTIREAFKDC--TVLTIAHRLDtiiDSDRI----LVLDKGRVV 216
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
19-212 1.06e-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: 84.12  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedhtltppsrRPVSMLFqennlfshlnvqqnIGLGLNP 98
Cdd:cd03220   42 SFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----------RVSSLLG--------------LGGGFNP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  99 GLT-----------LNASQREKRDAIARqmgIESLmARLP-------GELSGGQRQRV--ALARCLvrEQPVLLLDEPFS 158
Cdd:cd03220   98 ELTgreniylngrlLGLSRKEIDEKIDE---IIEF-SELGdfidlpvKTYSSGMKARLafAIATAL--EPDILLIDEVLA 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 877977460 159 ALDPALRQEMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03220  172 VGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
hmuV PRK13547
heme ABC transporter ATP-binding protein;
19-212 1.98e-19

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 84.11  E-value: 1.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFL--------APASGTLLIAGEDHTLTPPSR--RPVSMLFQENNLFSHLNV 88
Cdd:PRK13547  21 SLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEPLAAIDAPRlaRLRAVLPQAAQPAFAFSA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  89 QQNIGLGLNP-GLTLNASQREKRDAIARQM---GIESLMARLPGELSGGQRQRVALARCLVREQP---------VLLLDE 155
Cdd:PRK13547 101 REIVLLGRYPhARRAGALTHRDGEIAWQALalaGATALVGRDVTTLSGGELARVQFARVLAQLWPphdaaqpprYLLLDE 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 156 PFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:PRK13547 181 PTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
19-197 4.69e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 83.16  E-value: 4.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIaGFLAPASGTLLIAG----------EDHTLTPPSRRPVSMLFQENNLFShLNV 88
Cdd:PRK14258  27 SMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGrveffnqniyERRVNLNRLRRQVSMVHPKPNLFP-MSV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  89 QQNIGLGL-----NPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:PRK14258 105 YDNVAYGVkivgwRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPI 184
                        170       180       190
                 ....*....|....*....|....*....|....
gi 877977460 164 LRQEMLTLVSDICRERQLTLLMVSHSVEDAARIA 197
Cdd:PRK14258 185 ASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLS 218
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
18-188 5.05e-19

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: 85.22  E-value: 5.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVE-----RGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLliageDHTLTppsrrpVSMLFQENNLFSHLNVQQNI 92
Cdd:COG1245  354 FSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----DEDLK------ISYKPQYISPDYDGTVEEFL 422
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLNPGLTLNASQREkrdaIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:COG1245  423 RSANTDDFGSSYYKTE----IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498
                        170
                 ....*....|....*.
gi 877977460 173 SDICRERQLTLLMVSH 188
Cdd:COG1245  499 RRFAENRGKTAMVVDH 514
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
19-197 5.24e-19

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 82.91  E-value: 5.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLL-------NLIAGFLAPASgtllIAGEDHTLTPPS------RRPVSMLFQENNLFSH 85
Cdd:PRK14243  30 WLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRVEGK----VTFHGKNLYAPDvdpvevRRRIGMVFQKPNPFPK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  86 lNVQQNIGLG-------------LNPGLTLNASQREKRDAIaRQMGIEslmarlpgeLSGGQRQRVALARCLVREQPVLL 152
Cdd:PRK14243 106 -SIYDNIAYGaringykgdmdelVERSLRQAALWDEVKDKL-KQSGLS---------LSGGQQQRLCIARAIAVQPEVIL 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 877977460 153 LDEPFSALDP--ALRQE--MLTLVsdicreRQLTLLMVSHSVEDAARIA 197
Cdd:PRK14243 175 MDEPCSALDPisTLRIEelMHELK------EQYTIIIVTHNMQQAARVS 217
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
20-228 9.02e-19

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 84.30  E-value: 9.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-------------RRpvsmlfqENNLFSHL 86
Cdd:COG1129  273 FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdairagiayvpedRK-------GEGLVLDL 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  87 NVQQNIGLG----LNPGLTLNasqREKRDAIARQMgIESLMARLP------GELSGGQRQRVALARCLVREQPVLLLDEP 156
Cdd:COG1129  346 SIRENITLAsldrLSRGGLLD---RRRERALAEEY-IKRLRIKTPspeqpvGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 877977460 157 FSALDPALRQEMLTLVSDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRIawqgkTDELLSGQASASALL 228
Cdd:COG1129  422 TRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI-----VGELDREEATEEAIM 487
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
19-221 1.07e-18

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 83.34  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtlTPP----SRRPVSMLFQENNLFSHLNVQQNIgl 94
Cdd:PRK13536  61 SFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP---VPArarlARARIGVVPQFDNLDLEFTVRENL-- 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  95 gLNPGLTLNASQREKRDAIArqmgieSLM--ARLP-------GELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:PRK13536 136 -LVFGRYFGMSTREIEAVIP------SLLefARLEskadarvSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR 208
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460 166 QemltLVSDICRE---RQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQ 221
Cdd:PRK13536 209 H----LIWERLRSllaRGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
20-207 2.26e-18

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: 79.82  E-value: 2.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedhtltppsrrPVSMLFQENNLFShLNVQQNI--GLGLN 97
Cdd:cd03250   26 LEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQEPWIQN-GTIRENIlfGKPFD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  98 PgltlnasQREKR--DAIARQMGIESLMARLP---GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:cd03250   94 E-------ERYEKviKACALEPDLEILPDGDLteiGEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHI 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 877977460 169 LTLVsdICRERQL--TLLMVSHSVE---DAARIaprsIVVADGR 207
Cdd:cd03250  167 FENC--ILGLLLNnkTRILVTHQLQllpHADQI----VVLDNGR 204
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
19-219 3.54e-18

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 82.83  E-value: 3.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKS-TLLNLIAGFLAPA----SGTLLIAGED--HTLTPPSRR----PVSMLFQENnlFSHLN 87
Cdd:PRK15134  29 SLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESllHASEQTLRGvrgnKIAMIFQEP--MVSLN 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  88 VQQNIG------LGLNPGLTLNASQREKRDAIARqMGIESLMARL---PGELSGGQRQRVALARCLVREQPVLLLDEPFS 158
Cdd:PRK15134 107 PLHTLEkqlyevLSLHRGMRREAARGEILNCLDR-VGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 159 ALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK15134 186 ALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFS 246
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
19-219 9.68e-18

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: 81.39  E-value: 9.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGF--LAPASGTLLI----------------AGE------------------- 61
Cdd:TIGR03269  20 SFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskVGEpcpvcggtlepeevdfwnl 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   62 DHTLTPPSRRPVSMLFQEN-NLFSHLNVQQNIglgLNpglTLNASQREKRDAIAR------QMGIESLMARLPGELSGGQ 134
Cdd:TIGR03269 100 SDKLRRRIRKRIAIMLQRTfALYGDDTVLDNV---LE---ALEEIGYEGKEAVGRavdlieMVQLSHRITHIARDLSGGE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  135 RQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKT 214
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTP 253

                  ....*
gi 877977460  215 DELLS 219
Cdd:TIGR03269 254 DEVVA 258
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
17-163 2.65e-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: 77.15  E-value: 2.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE-DHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLg 95
Cdd:cd03231   18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRF- 96
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460  96 lnpgLTLNASQREKRDAIArQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:cd03231   97 ----WHADHSDEQVEEALA-RVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
10-161 2.94e-17

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 77.15  E-value: 2.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  10 LYHHLpmrfTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSrrpvsmlFQENNLF-SHLNv 88
Cdd:PRK13538  16 LFSGL----SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------YHQDLLYlGHQP- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  89 qqniglGLNPGLT----LNASQR----EKRDAIA---RQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPF 157
Cdd:PRK13538  84 ------GIKTELTalenLRFYQRlhgpGDDEALWealAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157

                 ....
gi 877977460 158 SALD 161
Cdd:PRK13538 158 TAID 161
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
20-226 3.02e-17

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 78.20  E-value: 3.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKS----TLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMlfqennlfshlnVQQNIGLG 95
Cdd:PRK10418  24 LTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIAT------------IMQNPRSA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LNPGLTLNASQREKRDAIARQMGIESLMARL---------------PGELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:PRK10418  92 FNPLHTMHTHARETCLALGKPADDATLTAALeavglenaarvlklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 161 DPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASA 226
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
20-207 3.94e-17

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: 79.48  E-value: 3.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPAS--GTLLIAGED---HTLTPPSRRPVSMLFQENNLFSHLNVQQNIGL 94
Cdd:TIGR02633  22 LEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPlkaSNIRDTERAGIVIIHQELTLVPELSVAENIFL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   95 G----LNPGLTLNASQREKRDAIARQMGIESL-MARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:TIGR02633 102 GneitLPGGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILL 181
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 877977460  170 TLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:TIGR02633 182 DIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
19-206 6.36e-17

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 79.06  E-value: 6.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHT-LTP--PSRRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:PRK09700  25 NLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNkLDHklAAQLGIGIIYQELSVIDELTVLENLYIG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LNP-----GLTLN--ASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPAlRQEM 168
Cdd:PRK09700 105 RHLtkkvcGVNIIdwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK-EVDY 183
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 877977460 169 LTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADG 206
Cdd:PRK09700 184 LFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
20-207 1.25e-16

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 78.03  E-value: 1.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTppSRRP-----VSMLFQENNLFSHLNVQQNIGL 94
Cdd:PRK11288  25 FDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFA--STTAalaagVAIIYQELHLVPEMTVAENLYL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  95 GLNPG----LTLNASQREKRDAIARqMGIE-SLMARLpGELSGGQRQRVALARCLVREQPVLLLDEPFSALDpALRQEML 169
Cdd:PRK11288 103 GQLPHkggiVNRRLLNYEAREQLEH-LGVDiDPDTPL-KYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS-AREIEQL 179
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 877977460 170 TLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:PRK11288 180 FRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
19-207 1.60e-16

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 78.05  E-value: 1.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGfLAPA---SGTLLIAGED---HTLTPPSRRPVSMLFQENNLFSHLNVQQNI 92
Cdd:PRK13549  25 SLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEElqaSNIRDTERAGIAIIHQELALVKELSVLENI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLNP---GLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:PRK13549 104 FLGNEItpgGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLL 183
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 877977460 170 TLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:PRK13549 184 DIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGR 220
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
1-219 1.86e-16

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 76.20  E-value: 1.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDITWLYHHLPMR--FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS----RRPVS 74
Cdd:PRK13638   1 MLATSDLWFRYQDEPVLkgLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllalRQQVA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  75 MLFQ--ENNLFsHLNVQQNIGLGL-NPGLTLNASQREKRDAIA-------RQMGIESLmarlpgelSGGQRQRVALARCL 144
Cdd:PRK13638  81 TVFQdpEQQIF-YTDIDSDIAFSLrNLGVPEAEITRRVDEALTlvdaqhfRHQPIQCL--------SHGQKKRVAIAGAL 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 145 VREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
25-208 2.01e-16

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 77.59  E-value: 2.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-----RRPVSMLFQENnlFSHLNVQQNIGLGLNPG 99
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqalRRDIQFIFQDP--YASLDPRQTVGDSIMEP 427
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 LT----LNASQREKRDA-IARQMGIESLMA-RLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVS 173
Cdd:PRK10261 428 LRvhglLPGKAAAARVAwLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLL 507
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 877977460 174 DICRERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:PRK10261 508 DLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
18-188 2.41e-16

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 77.54  E-value: 2.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPsRRPvsmLFQENNLFSHLnvqqniglgLN 97
Cdd:COG4178  382 LSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLP-QRP---YLPLGTLREAL---------LY 448
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  98 PGLTLNASQREKRDAIaRQMGIESLMARL------PGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:COG4178  449 PATAEAFSDAELREAL-EAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL 527
                        170
                 ....*....|....*..
gi 877977460 172 VSDICRErqLTLLMVSH 188
Cdd:COG4178  528 LREELPG--TTVISVGH 542
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
18-161 3.88e-16

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 76.77  E-value: 3.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVE-----RGEQVAILGPSGAGKSTLLNLIAGFLAPASG----TLLIAGEDHTLTPPSRRPVSMLFQENNlfshlnv 88
Cdd:PRK13409 353 FSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGevdpELKISYKPQYIKPDYDGTVEDLLRSIT------- 425
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460  89 qqniglglnPGLTLNASQREkrdaIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:PRK13409 426 ---------DDLGSSYYKSE----IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
5-234 1.01e-15

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 74.15  E-value: 1.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   5 IDITWLYHHLPMR-FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhtltpPSRRPVsmlfqENNLF 83
Cdd:PRK15056  12 VTVTWRNGHTALRdASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ------PTRQAL-----QKNLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  84 SHLNVQQNI--------------GLGLNPGLTLNASQREKR---DAIARqMGIESLMARLPGELSGGQRQRVALARCLVR 146
Cdd:PRK15056  81 AYVPQSEEVdwsfpvlvedvvmmGRYGHMGWLRRAKKRDRQivtAALAR-VDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 147 EQPVLLLDEPFSALDPALRQEMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVaDGRIAWQGKTDELLSGQASASA 226
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFTAENLELA 237

                 ....*...
gi 877977460 227 LLGIKSHI 234
Cdd:PRK15056 238 FSGVLRHV 245
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
14-161 2.82e-15

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: 74.44  E-value: 2.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  14 LPMrftlaVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGtlliageDHTlTPPSRRPVSMLFQENNLFSHLN--VQQN 91
Cdd:COG1245   93 LPV-----PKKGKVTGILGPNGIGKSTALKILSGELKPNLG-------DYD-EEPSWDEVLKRFRGTELQDYFKklANGE 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  92 IGLGLNP---------------GLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEP 156
Cdd:COG1245  160 IKVAHKPqyvdlipkvfkgtvrELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239

                 ....*
gi 877977460 157 FSALD 161
Cdd:COG1245  240 SSYLD 244
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
12-195 3.16e-15

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 74.39  E-value: 3.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  12 HHLPMRF---------TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedHTLTP---PSRRPVSMLFQE 79
Cdd:NF033858 270 RGLTMRFgdftavdhvSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG--QPVDAgdiATRRRVGYMSQA 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  80 NNLFSHLNVQQNiglglnpgLTLNA-------SQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVL 151
Cdd:NF033858 348 FSLYGELTVRQN--------LELHArlfhlpaAEIAARvAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELL 419
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 877977460 152 LLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAAR 195
Cdd:NF033858 420 ILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER 463
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
19-189 3.78e-15

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: 70.65  E-value: 3.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGfLAPA-SGTLLIAGEDHTLTPPsRRPVsmlfqennlfshlnvqqniglgLN 97
Cdd:cd03223   21 SFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWgSGRIGMPEGEDLLFLP-QRPY----------------------LP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  98 PGlTLnasqrekRDAIARQMGIEslmarlpgeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLtlvsDICR 177
Cdd:cd03223   77 LG-TL-------REQLIYPWDDV---------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY----QLLK 135
                        170
                 ....*....|..
gi 877977460 178 ERQLTLLMVSHS 189
Cdd:cd03223  136 ELGITVISVGHR 147
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
19-209 4.05e-15

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: 71.29  E-value: 4.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFShlnvqQNIGLGL 96
Cdd:cd03369   28 SFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEdlRSSLTIIPQDPTLFS-----GTIRSNL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 NPgltLNA-SQREKRDAIARQMGIESlmarlpgeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRqemlTLVSDI 175
Cdd:cd03369  103 DP---FDEySDEEIYGALRVSEGGLN--------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATD----ALIQKT 167
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 877977460 176 CRE--RQLTLLMVSH---SVEDAARIaprsIVVADGRIA 209
Cdd:cd03369  168 IREefTNSTILTIAHrlrTIIDYDKI----LVMDAGEVK 202
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
19-228 8.20e-15

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 73.24  E-value: 8.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-----HtltppsRRPVS-----M---LfqENNLFSH 85
Cdd:NF033858  21 SLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDmadarH------RRAVCpriayMpqgL--GKNLYPT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  86 LNVQQNI-------GLGlnpgltlnASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPF 157
Cdd:NF033858  93 LSVFENLdffgrlfGQD--------AAERRRRiDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 158 SALDPALRQEMLTLVSDICRER-QLTLLMVSHSVEDAARIaprSIVVA--DGRIAWQGKTDELLSGQASAS------ALL 228
Cdd:NF033858 165 TGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEEAERF---DWLVAmdAGRVLATGTPAELLARTGADTleaafiALL 241
PLN03211 PLN03211
ABC transporter G-25; Provisional
25-173 8.49e-15

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 72.99  E-value: 8.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPGLTLNA 104
Cdd:PLN03211  94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKSL 173
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 105 SQREK---RDAIARQMGIESLMARLPGE-----LSGGQRQRVALARCLVREQPVLLLDEPFSALDP-ALRQEMLTLVS 173
Cdd:PLN03211 174 TKQEKilvAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDAtAAYRLVLTLGS 251
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
12-208 8.63e-15

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 72.74  E-value: 8.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  12 HHLpmrfTLAVERGEQVAILGPSGAGKSTLLNLIAGflapasgtlliageDH------TLTPPSRRPVS----------M 75
Cdd:PRK10938 277 HNL----SWQVNPGEHWQIVGPNGAGKSTLLSLITG--------------DHpqgysnDLTLFGRRRGSgetiwdikkhI 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  76 LFQENNLfsHLNVQQNI--------GLGLNPGLTLNASQREKRdaIARQ----MGIESLMARLP-GELSGGQrQRVAL-A 141
Cdd:PRK10938 339 GYVSSSL--HLDYRVSTsvrnvilsGFFDSIGIYQAVSDRQQK--LAQQwldiLGIDKRTADAPfHSLSWGQ-QRLALiV 413
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 142 RCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAAR-IAPRSIVVADGRI 208
Cdd:PRK10938 414 RALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPAcITHRLEFVPDGDI 481
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
18-228 9.56e-15

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 72.64  E-value: 9.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPP--SRRPVSMLFQENN----LFSHLNVQQN 91
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrdAIRAGIMLCPEDRkaegIIPVHSVADN 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  92 IGLG-----LNPGLTLNAsQREKRDAiARQmgIESLMARLP------GELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:PRK11288 352 INISarrhhLRAGCLINN-RWEAENA-DRF--IRSLNIKTPsreqliMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 161 DPALRQEMLTLVSDICrERQLTLLMVSHSVEDAARIAPRSIVVADGRIAwqgktDELLSGQASASALL 228
Cdd:PRK11288 428 DVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRIA-----GELAREQATERQAL 489
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
18-217 1.52e-14

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 71.29  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVerGEQVAILGPSGAGKSTLLNLIAGFLAP---ASGTLLIAGEDhTLTPPSRR-------PVSMLFQENnlFSHLN 87
Cdd:PRK09473  37 FSLRA--GETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGRE-ILNLPEKElnklraeQISMIFQDP--MTSLN 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  88 VQQNIG------LGLNPGLTLNASQREK---RDAI----ARQMgieslMARLPGELSGGQRQRVALARCLVREQPVLLLD 154
Cdd:PRK09473 112 PYMRVGeqlmevLMLHKGMSKAEAFEESvrmLDAVkmpeARKR-----MKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460 155 EPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
16-218 1.86e-14

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 72.05  E-value: 1.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  16 MRFTLavERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTllIAGEDHTLTPPS----RRPVSMLFQENNLFSHlNVQQN 91
Cdd:PRK10789 334 VNFTL--KPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD--IRFHDIPLTKLQldswRSRLAVVSQTPFLFSD-TVANN 408
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  92 IGLGlNPgltlNASQREKRDAiARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:PRK10789 409 IALG-RP----DATQQEIEHV-ARLASVHDDILRLPqgydtevGErgvmLSGGQKQRISIARALLLNAEILILDDALSAV 482
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 161 DPALRQEMLTLVSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELL 218
Cdd:PRK10789 483 DGRTEHQILHNLRQWGEGR--TVIISAHrlsALTEASEI----LVMQHGHIAQRGNHDQLA 537
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
18-188 2.19e-14

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: 67.86  E-value: 2.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAgedhtltppsrrpvsmlfqENNLFSHLnvqqniglgln 97
Cdd:cd03221   19 ISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------STVKIGYF----------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  98 pgltlnaSQrekrdaiarqmgieslmarlpgeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPalrqEMLTLVSDICR 177
Cdd:cd03221   69 -------EQ-----------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL----ESIEALEEALK 114
                        170
                 ....*....|.
gi 877977460 178 ERQLTLLMVSH 188
Cdd:cd03221  115 EYPGTVILVSH 125
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
1-188 2.93e-14

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 68.82  E-value: 2.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   1 MLKLIDITWLYHHLPM--RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtltppSRRPVSMLFQ 78
Cdd:PRK13540   1 MLDVIELDFDYHDQPLlqQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS------IKKDLCTYQK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  79 ENNLFSHLNvqqniglGLNPGLTLN---------ASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQP 149
Cdd:PRK13540  75 QLCFVGHRS-------GINPYLTLRenclydihfSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAK 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 877977460 150 VLLLDEPFSALDpalRQEMLTLVSDICRERQL--TLLMVSH 188
Cdd:PRK13540 148 LWLLDEPLVALD---ELSLLTIITKIQEHRAKggAVLLTSH 185
PLN03232 PLN03232
ABC transporter C family member; Provisional
18-224 5.43e-14

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 70.78  E-value: 5.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHT---LTPpSRRPVSMLFQENNLFShlnvqQNIGL 94
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfgLTD-LRRVLSIIPQSPVLFS-----GTVRF 1328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   95 GLNP-------GLTLNASQREKRDAIARQ-MGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDpaLRQ 166
Cdd:PLN03232 1329 NIDPfsehndaDLWEALERAHIKDVIDRNpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD--VRT 1406
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460  167 EmlTLVSDICRE--RQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLSGQASA 224
Cdd:PLN03232 1407 D--SLIQRTIREefKSCTMLVIAHrlnTIIDCDKI----LVLSSGQVLEYDSPQELLSRDTSA 1463
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
17-219 6.59e-14

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 69.77  E-value: 6.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFL----APASGTLLIAGED-HTLTPPSRRP-----VSMLFQENnlFSHL 86
Cdd:PRK11022  25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDlQRISEKERRNlvgaeVAMIFQDP--MTSL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  87 NVQQNIGLGLNPGLTLN-----ASQREKRDAIARQMGIESLMARL---PGELSGGQRQRVALARCLVREQPVLLLDEPFS 158
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVHqggnkKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 159 ALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
17-188 9.72e-14

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 67.68  E-value: 9.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLapasgtlliagedhtltppSRRPVSMLF--QENNLFSHLNVQQNIGL 94
Cdd:COG2401   48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL-------------------KGTPVAGCVdvPDNQFGREASLIDAIGR 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  95 GLNPGltlnasqrekrDAIAR--QMGIES--LMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT 170
Cdd:COG2401  109 KGDFK-----------DAVELlnAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
                        170
                 ....*....|....*...
gi 877977460 171 LVSDICRERQLTLLMVSH 188
Cdd:COG2401  178 NLQKLARRAGITLVVATH 195
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1-219 1.15e-13

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 70.04  E-value: 1.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460     1 MLKLIDITWLYHHLPM----RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhTLTPPSRRPVSML 76
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSpavdRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKS-ILTNISDVHQNMG 2015
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    77 F--QENNLFSHLNVQQNIGLGLNpgltLNASQREKRDAIA----RQMGIESLMARLPGELSGGQRQRVALARCLVREQPV 150
Cdd:TIGR01257 2016 YcpQFDAIDDLLTGREHLYLYAR----LRGVPAEEIEKVAnwsiQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460   151 LLLDEPFSALDPALRQEMLTLVSDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKS 2159
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
20-228 1.23e-13

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: 68.34  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhtltppsrrpVSMLFQennlFSHL---NVQQNIGLGL 96
Cdd:cd03291   58 LKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQ----FSWImpgTIKENIIFGV 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 npgltlnaSQREKR-DAIARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:cd03291  123 --------SYDEYRyKSVVKACQLEEDITKFPekdntvlGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 165 RQEMLTlvSDICR-ERQLTLLMVSHSVEDaARIAPRSIVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:cd03291  195 EKEIFE--SCVCKlMANKTRILVTSKMEH-LKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
20-212 1.36e-13

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 67.78  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLA--PASGTLLIAGEDHTLTPP---SRRPVSMLFQ---Ennlfshlnvqqn 91
Cdd:COG0396   21 LTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPderARAGIFLAFQypvE------------ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  92 IglglnPGLT--------LNASQREKRDAIARQMGIESLMARL------------PGeLSGGQRQRVALARCLVREQPVL 151
Cdd:COG0396   89 I-----PGVSvsnflrtaLNARRGEELSAREFLKLLKEKMKELgldedfldryvnEG-FSGGEKKRNEILQMLLLEPKLA 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 152 LLDEPFSALD-PALRqemltLVSDIC---RERQLTLLMVSHSvedaAR----IAP-RSIVVADGRIAWQG 212
Cdd:COG0396  163 ILDETDSGLDiDALR-----IVAEGVnklRSPDRGILIITHY----QRildyIKPdFVHVLVDGRIVKSG 223
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
12-188 1.37e-13

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


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 67.78  E-value: 1.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  12 HHLPMrftlaVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGtlliageDHTlTPPSRRPVSMLFQENNL---FSHL-- 86
Cdd:cd03236   18 HRLPV-----PREGQVLGLVGPNGIGKSTALKILAGKLKPNLG-------KFD-DPPDWDEILDEFRGSELqnyFTKLle 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  87 -----------------NVQQNIGLGLNpgltlNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQP 149
Cdd:cd03236   85 gdvkvivkpqyvdlipkAVKGKVGELLK-----KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDAD 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 877977460 150 VLLLDEPFSALDPALRQEMLTLVSDICRERQlTLLMVSH 188
Cdd:cd03236  160 FYFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEH 197
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
21-178 1.97e-13

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 69.07  E-value: 1.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  21 AVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGtlliageDHTlTPPSRRPVSMLFQENNLFSHLN--VQQNIGLGLNP 98
Cdd:PRK13409  95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLG-------DYE-EEPSWDEVLKRFRGTELQNYFKklYNGEIKVVHKP 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  99 -----------G----LTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDpa 163
Cdd:PRK13409 167 qyvdlipkvfkGkvreLLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD-- 244
                        170
                 ....*....|....*
gi 877977460 164 LRQEMltLVSDICRE 178
Cdd:PRK13409 245 IRQRL--NVARLIRE 257
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
18-212 2.26e-13

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 66.40  E-value: 2.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLA--PASGTLLIAGEDHTLTPP---SRRPVSMLFQENNLFshlnvqqni 92
Cdd:cd03217   19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPeerARLGIFLAFQYPPEI--------- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 glglnPGLTLNASQREKRDAiarqmgieslmarlpgeLSGGQRQRVALARCLVREQPVLLLDEPFSALD-PALRqemltL 171
Cdd:cd03217   90 -----PGVKNADFLRYVNEG-----------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDiDALR-----L 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 877977460 172 VSDIC---RERQLTLLMVSHSVEDAARIAP-RSIVVADGRIAWQG 212
Cdd:cd03217  143 VAEVInklREEGKSVLIITHYQRLLDYIKPdRVHVLYDGRIVKSG 187
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
19-217 3.47e-13

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 68.34  E-value: 3.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKS----TLLNLI--AGFLAPASGTLL-------IAGEDHTLTPPSR---RPVSMLFQENnl 82
Cdd:PRK10261  36 SFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLrrrsrqvIELSEQSAAQMRHvrgADMAMIFQEP-- 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  83 FSHLNVQQNIGLGLNPGLTLN-ASQREKRDAIARQM-------GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLD 154
Cdd:PRK10261 114 MTSLNPVFTVGEQIAESIRLHqGASREEAMVEAKRMldqvripEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIAD 193
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460 155 EPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK10261 194 EPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
19-191 4.62e-13

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: 65.82  E-value: 4.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASG------TLLIAGEDHTLTPPSRRPVSMLFQENNLFShLNVQQNI 92
Cdd:cd03290   21 NIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLLN-ATVEENI 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGlNPgltLNaSQREKR--DAIARQMGIESL-------MARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:cd03290  100 TFG-SP---FN-KQRYKAvtDACSLQPDIDLLpfgdqteIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
                        170       180
                 ....*....|....*....|....*....
gi 877977460 164 LRQEMLTL-VSDICRERQLTLLMVSHSVE 191
Cdd:cd03290  175 LSDHLMQEgILKFLQDDKRTLVLVTHKLQ 203
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
19-209 4.97e-13

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 67.50  E-value: 4.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPP-------------SRRpvsmlfqENNLFSH 85
Cdd:PRK09700 283 SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgmayiteSRR-------DNGFFPN 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  86 LNVQQNIGL-------GLNPGLTLNASQREKRDAIARQ--MGIE-SLMARLPGELSGGQRQRVALARCLVREQPVLLLDE 155
Cdd:PRK09700 356 FSIAQNMAIsrslkdgGYKGAMGLFHEVDEQRTAENQRelLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 877977460 156 PFSALDPALRQEMLTLVSDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRIA 209
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLT 488
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
19-160 7.19e-13

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 67.34  E-value: 7.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPP--SRRP-VSMLFQENNLFSHLNVQQNIGLG 95
Cdd:PRK10762  24 ALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPksSQEAgIGIIHQELNLIPQLTIAENIFLG 103
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460  96 LNP----GLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:PRK10762 104 REFvnrfGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
20-219 8.94e-13

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 66.96  E-value: 8.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLliageDHTLTPPSR-------RPVSMLFQENN--LFShlNVQQ 90
Cdd:PRK10938  24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER-----QSQFSHITRlsfeqlqKLVSDEWQRNNtdMLS--PGED 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  91 NIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT 170
Cdd:PRK10938  97 DTGRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 877977460 171 LVSDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK10938 177 LLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
99-217 1.01e-12

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 66.30  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  99 GLTLNASQREKR---DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:NF000106 111 GR*LDLSRKDARaraDELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM 190
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 877977460 176 CRERQlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:NF000106 191 VRDGA-TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
17-219 1.25e-12

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 65.98  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFlapASGTLLIAGEDH--------TLTPPSRRP-----VSMLFQENNlf 83
Cdd:PRK15093  25 RVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTADRMrfddidllRLSPRERRKlvghnVSMIFQEPQ-- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  84 SHLNVQQNIGLGLN---PGLTLNAS--QR---EKRDAIA--RQMGIE---SLMARLPGELSGGQRQRVALARCLVREQPV 150
Cdd:PRK15093 100 SCLDPSERVGRQLMqniPGWTYKGRwwQRfgwRKRRAIEllHRVGIKdhkDAMRSFPYELTEGECQKVMIAIALANQPRL 179
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460 151 LLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK15093 180 LIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVT 248
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
25-161 1.29e-12

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: 66.50  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAgedhtltpPSRRpVSMLFQENNLFSHLNVQQNIGLGLNPGL---- 100
Cdd:TIGR03719  31 GAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ--------PGIK-VGYLPQEPQLDPTKTVRENVEEGVAEIKdald 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  101 -----------------TLNASQREKRDAIA--------RQMGIESLMARLP------GELSGGQRQRVALARCLVREQP 149
Cdd:TIGR03719 102 rfneisakyaepdadfdKLAAEQAELQEIIDaadawdldSQLEIAMDALRCPpwdadvTKLSGGERRRVALCRLLLSKPD 181
                         170
                  ....*....|..
gi 877977460  150 VLLLDEPFSALD 161
Cdd:TIGR03719 182 MLLLDEPTNHLD 193
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
19-227 2.19e-12

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: 65.62  E-value: 2.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAG-FLAPASGTLLIAGEDHTLTPPS---RRPVSMLFQE---NNLFSHLNVQQN 91
Cdd:TIGR02633 280 SFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRNPAqaiRAGIAMVPEDrkrHGIVPILGVGKN 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   92 IGLGlnpglTLNA-SQREKRDAIARQMGIESLMARLP----------GELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:TIGR02633 360 ITLS-----VLKSfCFKMRIDAAAELQIIGSAIQRLKvktaspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460  161 DPALRQEMLTLVSDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASAL 227
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVLAAAL 500
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
18-188 2.27e-12

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 65.74  E-value: 2.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGT------LLIAGEDH---TLTPPSrrpvsmlfqennlfshlNV 88
Cdd:PRK11147 338 FSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRihcgtkLEVAYFDQhraELDPEK-----------------TV 400
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  89 QQNIGLGlNPGLTLNASQRE------------KRdaiarqmgieslmARLPGE-LSGGQRQRVALARCLVREQPVLLLDE 155
Cdd:PRK11147 401 MDNLAEG-KQEVMVNGRPRHvlgylqdflfhpKR-------------AMTPVKaLSGGERNRLLLARLFLKPSNLLILDE 466
                        170       180       190
                 ....*....|....*....|....*....|...
gi 877977460 156 PFSALDpalrQEMLTLVSDICRERQLTLLMVSH 188
Cdd:PRK11147 467 PTNDLD----VETLELLEELLDSYQGTVLLVSH 495
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
15-188 2.49e-12

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 65.76  E-value: 2.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  15 PMRFTLavERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHLNVQQni 92
Cdd:PRK10522 341 PINLTI--KRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAVFTDFHLFDQLLGPE-- 416
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLNPGLTLNASQR-EKRDAIARQMGIESLMarlpgELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK10522 417 GKPANPALVEKWLERlKMAHKLELEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQV 491
                        170
                 ....*....|....*..
gi 877977460 172 VSDICRERQLTLLMVSH 188
Cdd:PRK10522 492 LLPLLQEMGKTIFAISH 508
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
22-175 3.47e-12

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 63.33  E-value: 3.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  22 VERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdHTLTPPSRRPVSMLFQENNLFSHLNVQQNigLGLNPGLT 101
Cdd:PRK13543  34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK-TATRGDRSRFMAYLGHLPGLKADLSTLEN--LHFLCGLH 110
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 877977460 102 LNASQREKRDAIArQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPalrqEMLTLVSDI 175
Cdd:PRK13543 111 GRRAKQMPGSALA-IVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL----EGITLVNRM 179
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
17-219 4.23e-12

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 64.54  E-value: 4.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAP----ASGTLLIAGEDHT-LTPPSRRPV-----SMLFQENNlfSHL 86
Cdd:COG4170   25 RVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLkLSPRERRKIigreiAMIFQEPS--SCL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  87 NVQQNIGLGLN---PGLTLNAS--QR---EKRDAIA--RQMGI---ESLMARLPGELSGGQRQRVALARCLVReQPVLLL 153
Cdd:COG4170  103 DPSAKIGDQLIeaiPSWTFKGKwwQRfkwRKKRAIEllHRVGIkdhKDIMNSYPHELTEGECQKVMIAMAIAN-QPRLLI 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 154 -DEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG4170  182 aDEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILK 248
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
70-221 4.86e-12

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 65.05  E-value: 4.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   70 RRPVSMLFQENNLFShLNVQQNIGLGLNpgltlNASqREKRDAIARQMGIESLMARLPGE-----------LSGGQRQRV 138
Cdd:PTZ00265 1295 RNLFSIVSQEPMLFN-MSIYENIKFGKE-----DAT-REDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRI 1367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  139 ALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARiaPRSIVVADGR------IAWQG 212
Cdd:PTZ00265 1368 AIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR--SDKIVVFNNPdrtgsfVQAHG 1445

                  ....*....
gi 877977460  213 KTDELLSGQ 221
Cdd:PTZ00265 1446 THEELLSVQ 1454
PLN03073 PLN03073
ABC transporter F family; Provisional
27-209 6.37e-12

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 64.50  E-value: 6.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  27 QVAILGPSGAGKSTLLNLIAGFLAPASGTLLiagedhtLTPPSRRPVsmlfqennlFSHLNVqQNIGLGLNPGLTLN--- 103
Cdd:PLN03073 537 RIAMVGPNGIGKSTILKLISGELQPSSGTVF-------RSAKVRMAV---------FSQHHV-DGLDLSSNPLLYMMrcf 599
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 104 -ASQREKRDAIARQMGIESLMARLPG-ELSGGQRQRVALARCLVREQPVLLLDEPFSALD----PALRQEMLTLvsdicr 177
Cdd:PLN03073 600 pGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDldavEALIQGLVLF------ 673
                        170       180       190
                 ....*....|....*....|....*....|..
gi 877977460 178 erQLTLLMVSHSVEDAARIAPRSIVVADGRIA 209
Cdd:PLN03073 674 --QGGVLMVSHDEHLISGSVDELWVVSEGKVT 703
PLN03130 PLN03130
ABC transporter C family member; Provisional
20-219 9.08e-12

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 64.37  E-value: 9.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAgedhtltppsRRPVSMLFQENNLFShLNVQQNIGLGLnpg 99
Cdd:PLN03130  638 LDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVI----------RGTVAYVPQVSWIFN-ATVRDNILFGS--- 703
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  100 lTLNASQREKR-DAIARQMGIESLmarlPG-----------ELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:PLN03130  704 -PFDPERYERAiDVTALQHDLDLL----PGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQ 778
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460  168 mltlVSDICRERQL---TLLMVS---HSVEDAARIaprsIVVADGRIAWQGKTDELLS 219
Cdd:PLN03130  779 ----VFDKCIKDELrgkTRVLVTnqlHFLSQVDRI----ILVHEGMIKEEGTYEELSN 828
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
17-161 9.45e-12

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: 63.80  E-value: 9.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIaGEDHTLT--PPSRrpvsmlfqeNNLFSHLNVQQNIGL 94
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAyvDQSR---------DALDPNKTVWEEISG 409
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460   95 GLNPgLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:TIGR03719 410 GLDI-IKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
19-228 1.21e-11

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 63.78  E-value: 1.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhTLTPPSRRPVSMLFQENNLFshlnvqqniglglnp 98
Cdd:TIGR01271  446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRI-SFSPQTSWIMPGTIKDNIIF--------------- 509
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    99 GLTLNasqrEKR-DAIARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:TIGR01271  510 GLSYD----EYRyTSVIKACQLEEDIALFPekdktvlGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460   167 EMLTlvSDICR-ERQLTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:TIGR01271  586 EIFE--SCLCKlMSNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
19-228 1.24e-11

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 63.81  E-value: 1.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdHTLTPPSRRPVSMLFQENNLFSH-LN---VQQNI-G 93
Cdd:TIGR00957  658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVPQQAWIQNDSLRENILFGKaLNekyYQQVLeA 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    94 LGLNPGLTLNASQreKRDAIARQmGIEslmarlpgeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVs 173
Cdd:TIGR00957  737 CALLPDLEILPSG--DRTEIGEK-GVN---------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHV- 803
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460   174 dICRERQL---TLLMVSHSVEdaarIAPRS---IVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:TIGR00957  804 -IGPEGVLknkTRILVTHGIS----YLPQVdviIVMSGGKISEMGSYQELLQRDGAFAEFL 859
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
19-188 1.39e-11

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 62.44  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLiagedhtlTPPSRRpVSMLFQENNLFSHLNVQQNIGLGLNP 98
Cdd:PRK09544  24 SLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLR-IGYVPQKLYLDTTLPLTVNRFLRLRP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  99 GLtlnasqrEKRD---AIARQMGIESLMARLPgELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:PRK09544  95 GT-------KKEDilpALKRVQAGHLIDAPMQ-KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQL 166
                        170
                 ....*....|...
gi 877977460 176 CRERQLTLLMVSH 188
Cdd:PRK09544 167 RRELDCAVLMVSH 179
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
18-212 1.96e-11

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: 61.12  E-value: 1.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPA---SGTLLIAGED-HTLTPPSRRPVSMLFQENNLFSHLNVQQnig 93
Cdd:cd03233   26 FSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPyKEFAEKYPGEIIYVSEEDVHFPTLTVRE--- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 lglnpglTLNASQREKRDAIARqmGIeslmarlpgelSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVS 173
Cdd:cd03233  103 -------TLDFALRCKGNEFVR--GI-----------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIR 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 877977460 174 DICRERQLTLLM-VSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03233  163 TMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQIYYG 202
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
25-161 2.75e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 62.44  E-value: 2.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGtlliageDHTLTPPSRrpVSMLFQENNLFSHLNVQQNIGLGLnpGLTLNA 104
Cdd:PRK11819  33 GAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------EARPAPGIK--VGYLPQEPQLDPEKTVRENVEEGV--AEVKAA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 105 SQR------------EKRDAIARQMG-----IESL----------MA----RLP------GELSGGQRQRVALARCLVRE 147
Cdd:PRK11819 102 LDRfneiyaayaepdADFDALAAEQGelqeiIDAAdawdldsqleIAmdalRCPpwdakvTKLSGGERRRVALCRLLLEK 181
                        170
                 ....*....|....
gi 877977460 148 QPVLLLDEPFSALD 161
Cdd:PRK11819 182 PDMLLLDEPTNHLD 195
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
19-207 4.62e-11

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 61.67  E-value: 4.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED---HTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:PRK10982  18 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfKSSKEALENGISMVHQELNLVLQRSVMDNMWLG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  96 LNPGLTLNASQREK-RD--AIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK10982  98 RYPTKGMFVDQDKMyRDtkAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTII 177
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 877977460 173 SDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:PRK10982 178 RKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
18-208 4.68e-11

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 61.58  E-value: 4.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHT-LTPPSRRPVSMLF-----QENNLFSHLNVQQN 91
Cdd:COG3845  277 VSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITgLSPRERRRLGVAYipedrLGRGLVPDMSVAEN 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  92 IGLG------LNPGLTLNasqREKRDAIARQMgIESLMARLPGE------LSGGQRQRVALARCLVREQPVLLLDEPFSA 159
Cdd:COG3845  357 LILGryrrppFSRGGFLD---RKAIRAFAEEL-IEEFDVRTPGPdtparsLSGGNQQKVILARELSRDPKLLIAAQPTRG 432
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 877977460 160 LDP----ALRQEMLTLvsdicRERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:COG3845  433 LDVgaieFIHQRLLEL-----RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
19-209 7.01e-11

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 61.22  E-value: 7.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHT-LTP-----------PSRRPVSMLFQENNLfsHL 86
Cdd:PRK15439 283 SLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINaLSTaqrlarglvylPEDRQSSGLYLDAPL--AW 360
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  87 NV----QQNIGLGLNPGltlnasqREKR--DAIARQMGIESLMARLP-GELSGGQRQRVALARCLVREQPVLLLDEPFSA 159
Cdd:PRK15439 361 NVcaltHNRRGFWIKPA-------RENAvlERYRRALNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 877977460 160 LDPALRQEMLTLVSDICrERQLTLLMVSHSVEDAARIAPRSIVVADGRIA 209
Cdd:PRK15439 434 VDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
GguA NF040905
sugar ABC transporter ATP-binding protein;
19-207 8.49e-11

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 60.96  E-value: 8.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGfLAPA---SGTLLIAGED---HTLTPPSRRPVSMLFQENNLFSHLNVQQNI 92
Cdd:NF040905  21 NLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVcrfKDIRDSEALGIVIIHQELALIPYLSIAENI 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLNPG----LTLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:NF040905 100 FLGNERAkrgvIDWNETNRRARELLAK-VGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAAL 178
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 877977460 169 LTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:NF040905 179 LDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGR 216
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
28-221 9.37e-11

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 60.89  E-value: 9.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  28 VAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedHTLTPPS----RRPVSMLFQENNLFSHlNVQQNIGLG--LNPGLT 101
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG--RPLSSLShsvlRQGVAMVQQDPVVLAD-TFLANVTLGrdISEEQV 446
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 102 LNASQREKRDAIARQM--GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ---EMLTLVsdic 176
Cdd:PRK10790 447 WQALETVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQaiqQALAAV---- 522
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 877977460 177 rERQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLSGQ 221
Cdd:PRK10790 523 -REHTTLVVIAHrlsTIVEADTI----LVLHRGQAVEQGTHQQLLAAQ 565
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
24-202 2.07e-10

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: 57.38  E-value: 2.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    24 RGEQVAILGPSGAGKSTLLNLIAGFLAPASGT-LLIAGEDHTLTPPSRRpvsmlfqennlfshlnvqqniglglnpgltl 102
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQL------------------------------- 49
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   103 nasqrekrdaiarqmgIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD-----ICR 177
Cdd:smart00382  50 ----------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKS 113
                          170       180
                   ....*....|....*....|....*
gi 877977460   178 ERQLTLLMVSHSVEDAARIAPRSIV 202
Cdd:smart00382 114 EKNLTVILTTNDEKDLGPALLRRRF 138
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
4-161 2.44e-10

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 59.96  E-value: 2.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   4 LIDIT--WL---YHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE----------------- 61
Cdd:PRK11147   3 LISIHgaWLsfsDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivarlqqdpprnvegt 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  62 -----------------------DHTLTPPSRRPVSMLFQENNLFSHLN-------VQQNIG-LGLNPGLTLNasqrekr 110
Cdd:PRK11147  83 vydfvaegieeqaeylkryhdisHLVETDPSEKNLNELAKLQEQLDHHNlwqlenrINEVLAqLGLDPDAALS------- 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 877977460 111 daiarqmgieslmarlpgELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:PRK11147 156 ------------------SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
PLN03130 PLN03130
ABC transporter C family member; Provisional
26-224 3.98e-10

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 59.37  E-value: 3.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   26 EQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHT---LTPpSRRPVSMLFQENNLFShlnvqQNIGLGLNPGLTL 102
Cdd:PLN03130 1266 EKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfgLMD-LRKVLGIIPQAPVLFS-----GTVRFNLDPFNEH 1339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  103 N------ASQREK-RDAIARQ-MGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD---PALRQEMLtl 171
Cdd:PLN03130 1340 NdadlweSLERAHlKDVIRRNsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDvrtDALIQKTI-- 1417
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460  172 vsdicRE--RQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLSGQASA 224
Cdd:PLN03130 1418 -----REefKSCTMLIIAHrlnTIIDCDRI----LVLDAGRVVEFDTPENLLSNEGSA 1466
PLN03232 PLN03232
ABC transporter C family member; Provisional
20-217 4.80e-10

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 59.22  E-value: 4.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAgedhtltppsRRPVSMLFQENNLFShLNVQQNIGLGLNpg 99
Cdd:PLN03232  638 LEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVI----------RGSVAYVPQVSWIFN-ATVRENILFGSD-- 704
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  100 ltlNASQREKR--DAIARQMGIESLMARLPGEL-------SGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEmlt 170
Cdd:PLN03232  705 ---FESERYWRaiDVTALQHDLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ--- 778
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 877977460  171 lVSDICRERQL---TLLMVSHSVEDAARIaPRSIVVADGRIAWQGKTDEL 217
Cdd:PLN03232  779 -VFDSCMKDELkgkTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAEL 826
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
3-219 8.89e-10

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 57.98  E-value: 8.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   3 KLIDITW-----LYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhtltppsrrpVSMLF 77
Cdd:PRK13545  23 KLKDLFFrskdgEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  78 QENNLFSHLNVQQNIGL-GLNPGLTlnasqREKRDAIARQM----GIESLMARLPGELSGGQRQRVALARCLVREQPVLL 152
Cdd:PRK13545  92 ISSGLNGQLTGIENIELkGLMMGLT-----KEKIKEIIPEIiefaDIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILV 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 153 LDEPFSALDPALRQEMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13545 167 IDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
19-219 1.71e-09

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: 57.65  E-value: 1.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLtppsRRPVSMLFQENNLFShlnvqQNI 92
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNiakiglHDL----RFKITIIPQDPVLFS-----GSL 1376
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    93 GLGLNPgltlnASQREKRDA-IARQMG-IESLMARLP----------GE-LSGGQRQRVALARCLVREQPVLLLDEPFSA 159
Cdd:TIGR00957 1377 RMNLDP-----FSQYSDEEVwWALELAhLKTFVSALPdkldhecaegGEnLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460   160 LD---PALRQEMLTLVSDICrerqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLS 219
Cdd:TIGR00957 1452 VDletDNLIQSTIRTQFEDC-----TVLTIAHrlnTIMDYTRV----IVLDKGEVAEFGAPSNLLQ 1508
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
18-161 2.32e-09

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 56.67  E-value: 2.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAveRGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIaGEDhtltppsrrpVSMLFQE---NNLFSHLNVQQNIGL 94
Cdd:PRK11819 345 FSLP--PGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GET----------VKLAYVDqsrDALDPNKTVWEEISG 411
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460  95 GLNpglTLNASQRE--KRDAIAR--------QmgieslmaRLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:PRK11819 412 GLD---IIKVGNREipSRAYVGRfnfkggdqQ--------KKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
21-227 2.49e-09

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 56.86  E-value: 2.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  21 AVERGEQVAILGPSGAGKSTLLNLIAG-FLAPASGTLLIAGEDHTLTPPS---RRPVSMLFQE---NNLFSHLNVQQNIG 93
Cdd:PRK13549 284 SLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVKIRNPQqaiAQGIAMVPEDrkrDGIVPVMGVGKNIT 363
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  94 LGlnpglTLNASQREKR-DAIARQMGIESLMARLP----------GELSGGQRQRVALARCLVREQPVLLLDEPFSALDP 162
Cdd:PRK13549 364 LA-----ALDRFTGGSRiDDAAELKTILESIQRLKvktaspelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 163 ALRQEMLTLVSDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASAL 227
Cdd:PRK13549 439 GAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNLTQEQVMEAAL 502
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
2-155 2.51e-09

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: 56.73  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   2 LKLIDITWLYHHL--PMRFT-----LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhTLTPPS----R 70
Cdd:COG4615  328 LELRGVTYRYPGEdgDEGFTlgpidLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ--PVTADNreayR 405
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  71 RPVSMLFQENNLFSHLnvqqnigLGLnpgltlnasQREKRDAIARQmgiesLMARL--------------PGELSGGQRQ 136
Cdd:COG4615  406 QLFSAVFSDFHLFDRL-------LGL---------DGEADPARARE-----LLERLeldhkvsvedgrfsTTDLSQGQRK 464
                        170
                 ....*....|....*....
gi 877977460 137 RVALARCLVREQPVLLLDE 155
Cdd:COG4615  465 RLALLVALLEDRPILVFDE 483
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
18-222 4.53e-09

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 56.05  E-value: 4.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIA--------GEDHTltppsrrpvSMLFQENNLFSHLnvq 89
Cdd:PRK15064 338 LNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenanigyyAQDHA---------YDFENDLTLFDWM--- 405
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  90 qniglglnpgltlnaSQ--REKRDaiaRQMgIESLMARL----------PGELSGGQRQRVALARCLVREQPVLLLDEP- 156
Cdd:PRK15064 406 ---------------SQwrQEGDD---EQA-VRGTLGRLlfsqddikksVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPt 466
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 877977460 157 -------FSALDPALrqEMLtlvsdicrerQLTLLMVSHSVEDAARIAPRSI-VVADGRIAWQGKTDELLSGQA 222
Cdd:PRK15064 467 nhmdmesIESLNMAL--EKY----------EGTLIFVSHDREFVSSLATRIIeITPDGVVDFSGTYEEYLRSQG 528
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
22-203 1.11e-08

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: 52.96  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  22 VERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTlliagEDHTLTPPSRRPvsmlfqennlfshlnvqQNIglglnpglt 101
Cdd:cd03222   22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN-----DEWDGITPVYKP-----------------QYI--------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 102 lnasqrekrdaiarqmgieslmarlpgELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQL 181
Cdd:cd03222   71 ---------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
                        170       180
                 ....*....|....*....|..
gi 877977460 182 TLLMVSHSVEDAARIAPRSIVV 203
Cdd:cd03222  124 TALVVEHDLAVLDYLSDRIHVF 145
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
17-188 1.58e-08

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: 54.37  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGfLAPASGTlliagedhTLTPPSrrpvsmlfqENNLFsHLNVQQNIGLG- 95
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGE-LWPVYGG--------RLTKPA---------KGKLF-YVPQRPYMTLGt 530
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   96 -----LNPGLTLNASQREKRDA--------------IARQMGIESlMARLPGELSGGQRQRVALARCLVREQPVLLLDEP 156
Cdd:TIGR00954 531 lrdqiIYPDSSEDMKRRGLSDKdleqildnvqlthiLEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
                         170       180       190
                  ....*....|....*....|....*....|..
gi 877977460  157 FSALDPALRQEMLTLvsdiCRERQLTLLMVSH 188
Cdd:TIGR00954 610 TSAVSVDVEGYMYRL----CREFGITLFSVSH 637
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
16-161 2.08e-08

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 54.26  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   16 MRFTLavERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIaGEDHTLTPPS----RRPVSMLFQENNLFSHlNVQQN 91
Cdd:PTZ00265  404 LNFTL--TEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII-NDSHNLKDINlkwwRSKIGVVSQDPLLFSN-SIKNN 479
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   92 IGLGL--------------------NPGLTLNASQREK---------------------------RDA----IARQMGIE 120
Cdd:PTZ00265  480 IKYSLyslkdlealsnyynedgndsQENKNKRNSCRAKcagdlndmsnttdsneliemrknyqtiKDSevvdVSKKVLIH 559
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 877977460  121 SLMARLP-----------GELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:PTZ00265  560 DFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
19-191 6.86e-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: 52.61  E-value: 6.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    19 TLAVERGEQVAILGPSGAGKSTLLNLIAGfLAPASGTLLIAGE--DHTLTPPSRRPVSMLFQENNLFSHlNVQQNiglgL 96
Cdd:TIGR01271 1239 SFSVEGGQRVGLLGRTGSGKSTLLSALLR-LLSTEGEIQIDGVswNSVTLQTWRKAFGVIPQKVFIFSG-TFRKN----L 1312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    97 NPGLTLNASQREKrdaIARQMGIESLMARLPGEL-----------SGGQRQRVALARCLVREQPVLLLDEPFSALDPA-- 163
Cdd:TIGR01271 1313 DPYEQWSDEEIWK---VAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVtl 1389
                          170       180       190
                   ....*....|....*....|....*....|
gi 877977460   164 --LRQEMLTLVSDiCrerqlTLLMVSHSVE 191
Cdd:TIGR01271 1390 qiIRKTLKQSFSN-C-----TVILSEHRVE 1413
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
18-228 7.68e-08

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 52.31  E-value: 7.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  18 FTLavERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-------------RRP----VSMLFQEN 80
Cdd:PRK10762 273 FTL--RKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglangivyisedRKRdglvLGMSVKEN 350
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  81 NLFSHLNVQQNIGLGLNpgltlNASQREKRDAIARQMGIES-LMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSA 159
Cdd:PRK10762 351 MSLTALRYFSRAGGSLK-----HADEQQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460 160 LDPALRQEMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIawqgkTDELLSGQASASALL 228
Cdd:PRK10762 426 VDVGAKKEIYQLINQF-KAEGLSIILVSSEMPEVLGMSDRILVMHEGRI-----SGEFTREQATQEKLM 488
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
25-233 7.83e-08

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: 51.45  E-value: 7.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLtppsRRPVSMLFQENNLFShlnvqQNIGLGLNP 98
Cdd:cd03288   47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDisklplHTL----RSRLSIILQDPILFS-----GSIRFNLDP 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  99 GLTLNASQREKRDAIARqmgIESLMARLPGEL-----------SGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:cd03288  118 ECKCTDDRLWEALEIAQ---LKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 168 MLTLVSDICRERQ-LTLLMVSHSVEDAARIaprsIVVADGRIAWQGKTDELLSGQASASALLgIKSH 233
Cdd:cd03288  195 LQKVVMTAFADRTvVTIAHRVSTILDADLV----LVLSRGILVECDTPENLLAQEDGVFASL-VRTD 256
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
25-216 1.22e-07

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 52.03  E-value: 1.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    25 GEQVAILGPSGAGKSTLLNLIA----GFLAPASGTLLIAGED-HTLTPPSRRPVSMLFQENNLFSHLNVQQNI------- 92
Cdd:TIGR00956   87 GELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITpEEIKKHYRGDVVYNAETDVHFPHLTVGETLdfaarck 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460    93 GLGLNP-GLTLNASQREKRDAIARQMGIESLMARLPGE-----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:TIGR00956  167 TPQNRPdGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATAL 246
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 877977460   167 EMLTLVSDICRERQLTLLM-VSHSVEDAARIAPRSIVVADGRIAWQGKTDE 216
Cdd:TIGR00956  247 EFIRALKTSANILDTTPLVaIYQCSQDAYELFDKVIVLYEGYQIYFGPADK 297
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
24-191 1.83e-07

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


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 49.63  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  24 RGEQVAILGPSGAGKSTLLNliAGFlaPASGTLLIAGedhTLTPPSRRPVSMLFQENNLFshlnvqqNIGLGLnpgLTLN 103
Cdd:cd03238   20 LNVLVVVTGVSGSGKSTLVN--EGL--YASGKARLIS---FLPKFSRNKLIFIDQLQFLI-------DVGLGY---LTLG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 104 asqrekrdaiarqmgieslmaRLPGELSGGQRQRVALARCLVREQP--VLLLDEPFSALDPalrQEMLTLVSDICRERQL 181
Cdd:cd03238   83 ---------------------QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ---QDINQLLEVIKGLIDL 138
                        170
                 ....*....|..
gi 877977460 182 --TLLMVSHSVE 191
Cdd:cd03238  139 gnTVILIEHNLD 150
PTZ00243 PTZ00243
ABC transporter; Provisional
19-212 1.91e-07

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 51.32  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLiagedhtltppSRRPVSMLFQENNLFShLNVQQNIgLGLNP 98
Cdd:PTZ00243  680 SVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQAWIMN-ATVRGNI-LFFDE 746
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   99 gltlnasQREKR--DAIaRQMGIESLMARLPG-----------ELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:PTZ00243  747 -------EDAARlaDAV-RVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 877977460  166 QEmltLVSDIC--RERQLTLLMVSHSVEDAARiAPRSIVVADGRIAWQG 212
Cdd:PTZ00243  819 ER---VVEECFlgALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSG 863
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
21-161 2.12e-07

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


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 49.55  E-value: 2.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  21 AVERGEQVAILGPSGAGKSTLLNLIAG--FLAPASGTLLIAGedhtltppsrRPVSMLFQENNLFSHlnvQQNIglgLNP 98
Cdd:cd03232   29 YVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILING----------RPLDKNFQRSTGYVE---QQDV---HSP 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460  99 GLTLnasqrekrdaiarqmgIESLM--ARLPGeLSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:cd03232   93 NLTV----------------REALRfsALLRG-LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
19-166 2.24e-07

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: 50.24  E-value: 2.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLApASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHlNVQQNiglgL 96
Cdd:cd03289   24 SFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQkwRKAFGVIPQKVFIFSG-TFRKN----L 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  97 NPGLTLNASQREKrdaIARQMGIESLMARLPGEL-----------SGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:cd03289   98 DPYGKWSDEEIWK---VAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 174

                 .
gi 877977460 166 Q 166
Cdd:cd03289  175 Q 175
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
29-194 2.88e-07

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


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 49.53  E-value: 2.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  29 AILGPSGAGKSTLLNLI--AGF-LAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNlfshlnvqqniglglnpGLTLNAS 105
Cdd:cd03240   26 LIVGQNGAGKTTIIEALkyALTgELPPNSKGGAHDPKLIREGEVRAQVKLAFENAN-----------------GKKYTIT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 106 QREK--RDAI-ARQMGIESLMARLPGELSGGQRQ------RVALARCLVREQPVLLLDEPFSALDPA-LRQEMLTLVSDI 175
Cdd:cd03240   89 RSLAilENVIfCHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLAEIIEER 168
                        170       180
                 ....*....|....*....|.
gi 877977460 176 CRERQLTLLMVSH--SVEDAA 194
Cdd:cd03240  169 KSQKNFQLIVITHdeELVDAA 189
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
24-209 3.65e-07

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 50.11  E-value: 3.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  24 RGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE---DHTLTPPSRRPVSMLFQE---NNLFSHLNVQ-----QNI 92
Cdd:PRK10982 273 KGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKkinNHNANEAINHGFALVTEErrsTGIYAYLDIGfnsliSNI 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLNPgLTLNASQREKRDAiarQMGIESLMARLP------GELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:PRK10982 353 RNYKNK-VGLLDNSRMKSDT---QWVIDSMRVKTPghrtqiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKF 428
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 877977460 167 EMLTLVSDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRIA 209
Cdd:PRK10982 429 EIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLVA 470
PTZ00243 PTZ00243
ABC transporter; Provisional
25-217 1.59e-06

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 48.62  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLtppsRRPVSMLFQENNLFSHlNVQQNiglgLNP 98
Cdd:PTZ00243 1336 REKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREigayglREL----RRQFSMIPQDPVLFDG-TVRQN----VDP 1406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   99 glTLNASQRE---------KRDAIARQM-GIESLMARLPGELSGGQRQRVALARCLV-REQPVLLLDEPFSALDPAL-RQ 166
Cdd:PTZ00243 1407 --FLEASSAEvwaalelvgLRERVASESeGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALdRQ 1484
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 877977460  167 EMLTLVSDICRERQLTLLMVSHSVEDAARIaprsIVVADGRIAWQGKTDEL 217
Cdd:PTZ00243 1485 IQATVMSAFSAYTVITIAHRLHTVAQYDKI----IVMDHGAVAEMGSPREL 1531
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
19-218 1.38e-05

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 44.81  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhtltppsrrpVSMLFQENNLFSHLNVQQNIGLGLnp 98
Cdd:PRK13546  44 SLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGIENIEFKM-- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  99 gLTLNASQREKRDAIARQMGIESLmarlpGEL--------SGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT 170
Cdd:PRK13546 111 -LCMGFKRKEIKAMTPKIIEFSEL-----GEFiyqpvkkySSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 877977460 171 LVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELL 218
Cdd:PRK13546 185 KIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
25-188 2.42e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 44.78  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAgEDHTLTPPSRRPVSMLFQENNLFSHLNvqqniglglnpGLTLNA 104
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA-KGIKLGYFAQHQLEFLRADESPLQHLA-----------RLAPQE 405
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 105 SQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIcrerQLTLL 184
Cdd:PRK10636 406 LEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF----EGALV 481

                 ....
gi 877977460 185 MVSH 188
Cdd:PRK10636 482 VVSH 485
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
29-202 2.49e-05

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 43.80  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  29 AILGPSGAGKSTLLNLIagflapasgTLLIAGEdhTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGL-----NPGLTLN 103
Cdd:cd03279   32 LICGPTGAGKSTILDAI---------TYALYGK--TPRYGRQENLRSVFAPGEDTAEVSFTFQLGGKKyrverSRGLDYD 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 104 ASqreKRDAIARQMGIESLMARLPGELSGGQRQRVALARCL--------VREQPV--LLLDEPFSALDPALRQEMLTLVS 173
Cdd:cd03279  101 QF---TRIVLLPQGEFDRFLARPVSTLSGGETFLASLSLALalsevlqnRGGARLeaLFIDEGFGTLDPEALEAVATALE 177
                        170       180
                 ....*....|....*....|....*....
gi 877977460 174 DICRERQLtLLMVSHSVEDAARIAPRSIV 202
Cdd:cd03279  178 LIRTENRM-VGVISHVEELKERIPQRLEV 205
ycf16 CHL00131
sulfate ABC transporter protein; Validated
20-71 3.94e-05

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 43.48  E-value: 3.94e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGFlaPA----SGTLLIAGEDHTLTPPSRR 71
Cdd:CHL00131  28 LSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILFKGESILDLEPEER 81
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
24-47 6.46e-05

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 42.39  E-value: 6.46e-05
                         10        20
                 ....*....|....*....|....
gi 877977460  24 RGEQVAILGPSGAGKSTLLNLIAG 47
Cdd:cd01854   84 KGKTSVLVGQSGVGKSTLLNALLP 107
PLN03140 PLN03140
ABC transporter G family member; Provisional
15-218 1.58e-04

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 42.53  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   15 PMRFTLavergeqvaILGPSGAGKSTLLNLIAGFLAPasgTLLIAGE----DHTLTPPSRRPVSMLFQENNL-FSHLNVQ 89
Cdd:PLN03140  190 PSRMTL---------LLGPPSSGKTTLLLALAGKLDP---SLKVSGEitynGYRLNEFVPRKTSAYISQNDVhVGVMTVK 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460   90 QNI-------GLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGE--------------------------------L 130
Cdd:PLN03140  258 ETLdfsarcqGVGTRYDLLSELARREKDAGIFPEAEVDLFMKATAMEgvksslitdytlkilgldickdtivgdemirgI 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  131 SGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMvshsveDAARIAPRS-------IVV 203
Cdd:PLN03140  338 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLM------SLLQPAPETfdlfddiILL 411
                         250
                  ....*....|....*
gi 877977460  204 ADGRIAWQGKTDELL 218
Cdd:PLN03140  412 SEGQIVYQGPRDHIL 426
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
127-191 2.22e-04

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


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 41.61  E-value: 2.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460  127 PGELSGGQRQ---RVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVsDICRERQLTLLMVSHSVE 191
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELL-KELSRNGAQLILTTHSPL 300
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
19-188 3.29e-04

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 41.31  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE-----DHTLTPPSRRP-VSMLFQENNLFSHLNVQQNI 92
Cdd:PRK10636  21 TATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawVNQETPALPQPaLEYVIDGDREYRQLEAQLHD 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  93 GLGLNPGLTLnASQREKRDAIArQMGIESLMARLPGEL--------------SGGQRQRVALARCLVREQPVLLLDEPFS 158
Cdd:PRK10636 101 ANERNDGHAI-ATIHGKLDAID-AWTIRSRAASLLHGLgfsneqlerpvsdfSGGWRMRLNLAQALICRSDLLLLDEPTN 178
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 877977460 159 ALDpalrqemltLVSDICRERQL-----TLLMVSH 188
Cdd:PRK10636 179 HLD---------LDAVIWLEKWLksyqgTLILISH 204
PLN03073 PLN03073
ABC transporter F family; Provisional
131-191 3.77e-04

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 41.38  E-value: 3.77e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 131 SGGQRQRVALARCLVREQPVLLLDEPFSALDpalRQEMLTLVSDICRERQlTLLMVSHSVE 191
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPK-TFIVVSHARE 402
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
27-53 9.27e-04

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 37.98  E-value: 9.27e-04
                          10        20
                  ....*....|....*....|....*..
gi 877977460   27 QVAILGPSGAGKSTLLNLIAGFLAPAS 53
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVS 27
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
24-47 1.33e-03

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 38.29  E-value: 1.33e-03
                          10        20
                  ....*....|....*....|....
gi 877977460   24 RGEQVAILGPSGAGKSTLLNLIAG 47
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLP 128
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
130-194 1.34e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 1.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 130 LSGGQRQ------RVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVsdicrERQL----TLLMVSHSVE--DAA 194
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIM-----ERYLrkipQVIIVSHDEElkDAA 860
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
28-175 1.76e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 38.45  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  28 VAILGPSGAGKSTLLNLIA-GFLAPASGTllIAGEDHTLTPPSRRP-VSMLFQENNLFSHLNVQQNIGLGLnpgltLNAS 105
Cdd:COG0419   26 NLIVGPNGAGKSTILEAIRyALYGKARSR--SKLRSDLINVGSEEAsVELEFEHGGKRYRIERRQGEFAEF-----LEAK 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 106 QREKRDAIARQMGI---ESLMARL---------------------------------PGELSGGQRQRVALARcLVReqp 149
Cdd:COG0419   99 PSERKEALKRLLGLeiyEELKERLkeleealesaleelaelqklkqeilaqlsgldpIETLSGGERLRLALAD-LLS--- 174
                        170       180
                 ....*....|....*....|....*.
gi 877977460 150 vLLLDepFSALDPALRQEMLTLVSDI 175
Cdd:COG0419  175 -LILD--FGSLDEERLERLLDALEEL 197
PRK01889 PRK01889
GTPase RsgA; Reviewed
25-47 2.88e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 37.99  E-value: 2.88e-03
                         10        20
                 ....*....|....*....|...
gi 877977460  25 GEQVAILGPSGAGKSTLLNLIAG 47
Cdd:PRK01889 195 GKTVALLGSSGVGKSTLVNALLG 217
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
25-47 4.77e-03

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 36.70  E-value: 4.77e-03
                         10        20
                 ....*....|....*....|...
gi 877977460  25 GEQVAILGPSGAGKSTLLNLIAG 47
Cdd:cd04164    3 GIKVVIAGKPNVGKSSLLNALAG 25
PhnN COG3709
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
28-68 5.31e-03

Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];


Pssm-ID: 442923  Cd Length: 188  Bit Score: 36.71  E-value: 5.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 877977460  28 VAILGPSGAGKSTLLNLIAGFLAPASGtLLIA-----------GEDH-TLTPP 68
Cdd:COG3709    8 IYVVGPSGAGKDSLLAAARARLAADPR-LVFArryitrpadagGEDHdALSEA 59
PRK00098 PRK00098
GTPase RsgA; Reviewed
30-47 5.42e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 37.11  E-value: 5.42e-03
                         10
                 ....*....|....*...
gi 877977460  30 ILGPSGAGKSTLLNLIAG 47
Cdd:PRK00098 169 LAGQSGVGKSTLLNALAP 186
VirB4 COG3451
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
28-46 5.54e-03

Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 37.62  E-value: 5.54e-03
                         10
                 ....*....|....*....
gi 877977460  28 VAILGPSGAGKSTLLNLIA 46
Cdd:COG3451  207 TLILGPSGSGKSFLLKLLL 225
AAA_29 pfam13555
P-loop containing region of AAA domain;
19-53 5.72e-03

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 34.11  E-value: 5.72e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 877977460   19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPAS 53
Cdd:pfam13555  16 TIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
20-161 6.70e-03

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 36.69  E-value: 6.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  20 LAVERGEQVAILGPSGAGKSTLLNLIAGF--LAPASGTLLIAGEDHTLTPPSRRP---VSMLFQ--------ENNLFSHL 86
Cdd:PRK09580  22 LEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAgegIFMAFQypveipgvSNQFFLQT 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460  87 NVQQniglglnpglTLNASQREKRDAIARQMGIESLMARL--PGEL---------SGGQRQRVALARCLVREQPVLLLDE 155
Cdd:PRK09580 102 ALNA----------VRSYRGQEPLDRFDFQDLMEEKIALLkmPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILDE 171

                 ....*.
gi 877977460 156 PFSALD 161
Cdd:PRK09580 172 SDSGLD 177
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
129-162 7.41e-03

ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213240 [Multi-domain]  Cd Length: 251  Bit Score: 36.51  E-value: 7.41e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 877977460 129 ELSGGQRQRVAL----ARCLVREQPVLLLDEPFSALDP 162
Cdd:cd03273  166 ELSGGQRSLVALslilALLLFKPAPMYILDEVDAALDL 203
PRK13830 PRK13830
conjugal transfer protein TrbE; Provisional
15-46 7.75e-03

conjugal transfer protein TrbE; Provisional


Pssm-ID: 237525 [Multi-domain]  Cd Length: 818  Bit Score: 37.13  E-value: 7.75e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 877977460  15 PMRFTLAVERGEQVAILGPSGAGKSTLLNLIA 46
Cdd:PRK13830 446 PFRLNLHVDDVGHTLIFGPTGSGKSTLLALIA 477
 
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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