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Conserved domains on  [gi|1737829014|emb|VVE24206|]
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ABC transporter ATP-binding protein [Pandoraea sputorum]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11438110)

ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ATP transporter complex responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of substrates including nitrate and sulfonates; similar to aliphatic sulfonates import ATP-binding protein SsuB

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
32-287 5.64e-135

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


:

Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 382.13  E-value: 5.64e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAF 111
Cdd:COG1116     7 ALELRGVSKRF--PTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDE 191
Cdd:COG1116    85 VFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 192 PFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDLPH-RDnpIERRKQAGMN 270
Cdd:COG1116   165 PFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRpRD--RELRTSPEFA 242
                         250
                  ....*....|....*..
gi 1737829014 271 EYVAHLMELLKVGRDDH 287
Cdd:COG1116   243 ALRAEILDLLREEAERA 259
 
Name Accession Description Interval E-value
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
32-287 5.64e-135

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 382.13  E-value: 5.64e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAF 111
Cdd:COG1116     7 ALELRGVSKRF--PTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDE 191
Cdd:COG1116    85 VFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 192 PFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDLPH-RDnpIERRKQAGMN 270
Cdd:COG1116   165 PFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRpRD--RELRTSPEFA 242
                         250
                  ....*....|....*..
gi 1737829014 271 EYVAHLMELLKVGRDDH 287
Cdd:COG1116   243 ALRAEILDLLREEAERA 259
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
33-254 9.80e-127

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: 359.86  E-value: 9.80e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFM 112
Cdd:cd03293     1 LEVRNVSKTY--GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:cd03293    79 FQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 193 FSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDL 254
Cdd:cd03293   159 FSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
ABC_ATP_SaoA NF040729
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ...
33-281 4.16e-80

ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.


Pssm-ID: 468693 [Multi-domain]  Cd Length: 248  Bit Score: 242.34  E-value: 4.16e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFM 112
Cdd:NF040729    2 LKIQNISKTFINN--KKENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGPDRGFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:NF040729   80 FQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 193 FSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDLPHRDNpierRKQAGMNEY 272
Cdd:NF040729  160 LGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRDKGKILEDLKIDLPRPRN----RESEKYLEY 235

                  ....*....
gi 1737829014 273 VAHLMELLK 281
Cdd:NF040729  236 KDHLTNILK 244
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
53-257 7.93e-67

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 208.79  E-value: 7.93e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFMLQKDLLMPWRSIQKNVELGM 132
Cdd:PRK11248   16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAFGL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 133 QIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQML 212
Cdd:PRK11248   96 QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLW 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1737829014 213 ASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDLPHR 257
Cdd:PRK11248  176 QETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLNFARR 220
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
56-255 3.73e-61

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: 193.45  E-value: 3.73e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GPSQQVAFmlQKDLLMPWRSIQKNVELGMQ 133
Cdd:TIGR01184   3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepGPDRMVVF--QNYSLLPWLTVRENIALAVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 134 --IRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQM 211
Cdd:TIGR01184  81 rvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1737829014 212 LASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEI-TVDLP 255
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQIlEVPFP 205
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
54-194 2.28e-39

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 134.70  E-value: 2.28e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----QQVAFMLQKDLLMPWRSIQKNV 128
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDErkslrKEIGYVFQDPQLFPRLTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 129 ELGMQIRGRSKAERAEVAKALLARCHLKGFENH----YPHQLSGGMRQRAALARTLAVEPDVLLMDEPFS 194
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
52-236 3.80e-33

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 120.03  E-value: 3.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTlagkpvRGPSQQVAFMLQK---DLLMPWRSIQKnV 128
Cdd:NF040873    6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------RAGGARVAYVPQRsevPDSLPLTVRDL-V 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 129 ELGM-QIRGR----SKAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:NF040873   79 AMGRwARRGLwrrlTRDDRAAVDDAL-ERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1737829014 204 LQQDLAQmLASEGKTALMITHDLaEAIALSDRV 236
Cdd:NF040873  158 IIALLAE-EHARGATVVVVTHDL-ELVRRADPC 188
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
24-197 6.66e-25

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 104.44  E-value: 6.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  24 PAAAPLPFAIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV- 102
Cdd:NF033858  258 PADDDDEPAIEARGLTMRF------GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVd 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 103 ------RgpsQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAAL 176
Cdd:NF033858  332 agdiatR---RRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSL 408
                         170       180
                  ....*....|....*....|...
gi 1737829014 177 ArtLAV--EPDVLLMDEPFSALD 197
Cdd:NF033858  409 A--VAVihKPELLILDEPTSGVD 429
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
32-192 5.18e-17

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 80.94  E-value: 5.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGP------ 105
Cdd:NF033858    1 VARLEGVSHRY------GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADArhrrav 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 106 SQQVAFMLQ---KDlLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAV 182
Cdd:NF033858   75 CPRIAYMPQglgKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIH 153
                         170
                  ....*....|
gi 1737829014 183 EPDVLLMDEP 192
Cdd:NF033858  154 DPDLLILDEP 163
GguA NF040905
sugar ABC transporter ATP-binding protein;
34-285 3.84e-14

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 72.13  E-value: 3.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  34 EYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYaPS---EGQVTLAGKPVR----GPS 106
Cdd:NF040905    3 EMRGITKTF------PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRfkdiRDS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 QQVAFML--QKDLLMPWRSIQKNVELGMQIRGRSKAERAEV---AKALLARCHLKgfENhyPHQLSG----GMRQRAALA 177
Cdd:NF040905   76 EALGIVIihQELALIPYLSIAENIFLGNERAKRGVIDWNETnrrARELLAKVGLD--ES--PDTLVTdigvGKQQLVEIA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 178 RTLAVEPDVLLMDEPFSAL-DAQTKMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEeiTVDLpH 256
Cdd:NF040905  152 KALSKDVKLLILDEPTAALnEEDSAALL--DLLLELKAQGITSIIISHKLNEIRRVADSITVL--RDGRTIE--TLDC-R 224
                         250       260
                  ....*....|....*....|....*....
gi 1737829014 257 RDNPIERRKQAGMneyvahlmellkVGRD 285
Cdd:NF040905  225 ADEVTEDRIIRGM------------VGRD 241
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
32-253 5.32e-11

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 62.45  E-value: 5.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLnMGAGLYAPSEGQV---------------- 95
Cdd:NF000106   13 AVEVRGLVKHF------GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRpwrf*twcanrralrr 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  96 TLAG-KPVRGPSQQvAFMLQKDLLMpwrsiqknveLGMQIRGRSKAERAEvAKALLARCHLKGFENHYPHQLSGGMRQRA 174
Cdd:NF000106   86 TIG*hRPVR*GRRE-SFSGRENLYM----------IGR*LDLSRKDARAR-ADELLERFSLTEAAGRAAAKYSGGMRRRL 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 175 ALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLaSEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:NF000106  154 DLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDR--GRVIADGKVD 229
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
64-239 8.87e-11

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: 58.92  E-value: 8.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   64 GEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGkpvrgpsqqvafmlqkdllmpwrsiqknvelgmqirgrskaerA 143
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------------------------------------------G 38
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  144 EVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQD-----LAQMLASEGKT 218
Cdd:smart00382  39 EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKNLT 118
                          170       180
                   ....*....|....*....|....*.
gi 1737829014  219 ALMITHDL-----AEAIALSDRVFVM 239
Cdd:smart00382 119 VILTTNDEkdlgpALLRRRFDRRIVL 144
GguA NF040905
sugar ABC transporter ATP-binding protein;
166-251 1.72e-10

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 60.96  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 166 LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKM----VLQQdlaqmLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:NF040905  405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYeiytIINE-----LAAEGKGVIVISSELPELLGMCDRIYVMNE 479
                          90
                  ....*....|
gi 1737829014 242 rpGTIIEEIT 251
Cdd:NF040905  480 --GRITGELP 487
 
Name Accession Description Interval E-value
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
32-287 5.64e-135

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 382.13  E-value: 5.64e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAF 111
Cdd:COG1116     7 ALELRGVSKRF--PTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDE 191
Cdd:COG1116    85 VFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 192 PFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDLPH-RDnpIERRKQAGMN 270
Cdd:COG1116   165 PFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRpRD--RELRTSPEFA 242
                         250
                  ....*....|....*..
gi 1737829014 271 EYVAHLMELLKVGRDDH 287
Cdd:COG1116   243 ALRAEILDLLREEAERA 259
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
33-254 9.80e-127

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: 359.86  E-value: 9.80e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFM 112
Cdd:cd03293     1 LEVRNVSKTY--GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:cd03293    79 FQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 193 FSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDL 254
Cdd:cd03293   159 FSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
32-247 1.68e-83

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 254.64  E-value: 1.68e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQ-- 108
Cdd:COG3842     5 ALELENVSKRY------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlPPEKrn 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:COG3842    79 VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII 247
Cdd:COG3842   159 LDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND--GRIE 215
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
47-257 6.76e-82

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 247.47  E-value: 6.76e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  47 GKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFMLQKDLLMPWRSIQK 126
Cdd:COG4525    16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVFQKDALLPWLNVLD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 NVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQ 206
Cdd:COG4525    96 NVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQE 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 207 DLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDLPHR 257
Cdd:COG4525   176 LLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELDFSRR 226
ABC_ATP_SaoA NF040729
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ...
33-281 4.16e-80

ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.


Pssm-ID: 468693 [Multi-domain]  Cd Length: 248  Bit Score: 242.34  E-value: 4.16e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFM 112
Cdd:NF040729    2 LKIQNISKTFINN--KKENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGPDRGFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:NF040729   80 FQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 193 FSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDLPHRDNpierRKQAGMNEY 272
Cdd:NF040729  160 LGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRDKGKILEDLKIDLPRPRN----RESEKYLEY 235

                  ....*....
gi 1737829014 273 VAHLMELLK 281
Cdd:NF040729  236 KDHLTNILK 244
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
33-248 9.63e-78

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: 235.11  E-value: 9.63e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQ--V 109
Cdd:cd03259     1 LELKGLSKTY------GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvPPERrnI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:cd03259    75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:cd03259   155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNE--GRIVQ 211
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
33-253 7.02e-70

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 219.63  E-value: 7.02e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGK------PVRgpS 106
Cdd:COG1118     3 IEVRNISKRFGSFT------LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftnlPPR--E 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 QQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDV 186
Cdd:COG1118    75 RRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 187 LLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:COG1118   155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ--GRIEQVGTPD 219
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
33-241 1.76e-67

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: 209.27  E-value: 1.76e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNrqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS------ 106
Cdd:cd03255     1 IELKNLSKTYGG--GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelaa 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 ---QQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:cd03255    79 frrRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLaEAIALSDRVFVMSE 241
Cdd:cd03255   159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRD 215
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
53-257 7.93e-67

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 208.79  E-value: 7.93e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFMLQKDLLMPWRSIQKNVELGM 132
Cdd:PRK11248   16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAFGL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 133 QIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQML 212
Cdd:PRK11248   96 QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLW 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1737829014 213 ASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDLPHR 257
Cdd:PRK11248  176 QETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLNFARR 220
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
32-250 6.70e-66

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 205.28  E-value: 6.70e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----- 106
Cdd:COG1136     4 LLELRNLTKSY--GTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerela 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 ----QQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAV 182
Cdd:COG1136    82 rlrrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 183 EPDVLLMDEPFSALDAQT-KMVLQQdLAQMLASEGKTALMITHDLaEAIALSDRVFVMSErpGTIIEEI 250
Cdd:COG1136   162 RPKLILADEPTGNLDSKTgEEVLEL-LRELNRELGTTIVMVTHDP-ELAARADRVIRLRD--GRIVSDE 226
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
33-246 4.32e-64

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: 200.93  E-value: 4.32e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG---PSQQV 109
Cdd:cd03300     1 IELENVSKFY------GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlppHKRPV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:cd03300    75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTI 246
Cdd:cd03300   155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNK--GKI 209
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
32-241 1.99e-63

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 203.38  E-value: 1.99e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-------RG 104
Cdd:COG3839     3 SLELENVSKSY------GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlppkdRN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 105 psqqVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:COG3839    77 ----IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 185 DVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:COG3839   153 KVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND 209
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
33-248 2.64e-62

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: 196.75  E-value: 2.64e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GPSQ--- 107
Cdd:cd03295     1 IEFENVTKRYGGGK-----KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqDPVElrr 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHL--KGFENHYPHQLSGGMRQRAALARTLAVEPD 185
Cdd:cd03295    76 KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPP 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 186 VLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:cd03295   156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN--GEIVQ 216
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
33-250 5.47e-62

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 198.01  E-value: 5.47e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG--PS---- 106
Cdd:COG1125     2 IEFENVTKRYPDGT-----VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDldPVelrr 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 ------QQVAfmlqkdlLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHL--KGFENHYPHQLSGGMRQRAALAR 178
Cdd:COG1125    77 rigyviQQIG-------LFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVAR 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 179 TLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTII-----EEI 250
Cdd:COG1125   150 ALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM--REGRIVqydtpEEI 224
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
17-253 5.70e-62

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 203.98  E-value: 5.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  17 ADARHAQPAAAPLpfaIEYRGVTRRFKNRqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVT 96
Cdd:COG1123   248 GRAAPAAAAAEPL---LEVRNLSKRYPVR-GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIL 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  97 LAGKPVRGPSQQVAFMLQKDL----------LMPWRSIQKNVELGMQIRGR-SKAERAEVAKALLARCHL-KGFENHYPH 164
Cdd:COG1123   324 FDGKDLTKLSRRSLRELRRRVqmvfqdpyssLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPH 403
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 165 QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpG 244
Cdd:COG1123   404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD--G 481

                  ....*....
gi 1737829014 245 TIIEEITVD 253
Cdd:COG1123   482 RIVEDGPTE 490
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
53-278 2.19e-61

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: 195.55  E-value: 2.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS---------QQVAFMLQKDLLMPWRS 123
Cdd:cd03294    39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelrelrrKKISMVFQSFALLPHRT 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:cd03294   119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 204 LQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTII-----EEITVdlphrdNPierrkqagMNEYVAHLME 278
Cdd:cd03294   199 MQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIM--KDGRLVqvgtpEEILT------NP--------ANDYVREFFR 262
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
56-255 3.73e-61

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: 193.45  E-value: 3.73e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GPSQQVAFmlQKDLLMPWRSIQKNVELGMQ 133
Cdd:TIGR01184   3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepGPDRMVVF--QNYSLLPWLTVRENIALAVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 134 --IRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQM 211
Cdd:TIGR01184  81 rvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1737829014 212 LASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEI-TVDLP 255
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQIlEVPFP 205
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
33-253 9.86e-61

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 192.59  E-value: 9.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----QQ 108
Cdd:COG1131     1 IEVRGLTKRYGDK------TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPaevrRR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:COG1131    75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:COG1131   155 LDEPTSGLDPEARRELWELLRE-LAAEGKTVLLSTHYLEEAERLCDRVAIIDK--GRIVADGTPD 216
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
32-241 2.24e-60

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: 191.78  E-value: 2.24e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS---QQ 108
Cdd:cd03296     2 SIEVRNVSKRF------GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPvqeRN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQIRGR----SKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:cd03296    76 VGFVFQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 185 DVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:cd03296   156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNK 212
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
53-250 5.68e-60

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


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 195.32  E-value: 5.68e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGE-FVsLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ---------VAFMLQKDLLMPWR 122
Cdd:COG4175    42 GVNDASFDVEEGEiFV-IMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKelrelrrkkMSMVFQHFALLPHR 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 SIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKM 202
Cdd:COG4175   121 TVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRR 200
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 203 VLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTII-----EEI 250
Cdd:COG4175   201 EMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIM--KDGRIVqigtpEEI 251
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
33-247 5.92e-60

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: 190.24  E-value: 5.92e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKnrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----Q 107
Cdd:COG1122     1 IELENLSFSYP-----GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlrelrR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQkD----LLMPwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:COG1122    76 KVGLVFQ-NpddqLFAP--TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII 247
Cdd:COG1122   153 PEVLVLDEPTAGLDPRGRRELLELLKR-LNKEGKTVIIVTHDLDLVAELADRVIVLDD--GRIV 213
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
41-241 1.88e-58

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: 185.75  E-value: 1.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  41 RFKN---RQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGP-----SQQVAFM 112
Cdd:cd03225     1 ELKNlsfSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLslkelRRKVGLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQK---DLLMPwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:cd03225    81 FQNpddQFFGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:cd03225   159 DEPTAGLDPAGRRELLELLKK-LKAEGKTIIIVTHDLDLLLELADRVIVLED 209
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
33-249 5.67e-56

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: 180.01  E-value: 5.67e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNrqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFM 112
Cdd:cd03257     2 LEVKNLSVSFPT--GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLM----------PWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHL---KGFENHYPHQLSGGMRQRAALART 179
Cdd:cd03257    80 RRKEIQMvfqdpmsslnPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 180 LAVEPDVLLMDEPFSALDAQTK---MVLQQDLAQMLaseGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:cd03257   160 LALNPKLLIADEPTSALDVSVQaqiLDLLKKLQEEL---GLTLLFITHDLGVVAKIADRVAVMYA--GKIVEE 227
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
36-239 8.50e-56

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274496 [Multi-domain]  Cd Length: 353  Bit Score: 183.70  E-value: 8.50e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  36 RGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-RGPSQQVAF--M 112
Cdd:TIGR03265   8 DNIRKRF------GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDItRLPPQKRDYgiV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:TIGR03265  82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1737829014 193 FSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVM 208
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
33-241 9.08e-55

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: 175.45  E-value: 9.08e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ---- 108
Cdd:cd03229     1 LELKNVSKRY------GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElppl 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 ---VAFMLQKDLLMPWRSIQKNVELGmqirgrskaeraevakallarchlkgfenhyphqLSGGMRQRAALARTLAVEPD 185
Cdd:cd03229    75 rrrIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 186 VLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:cd03229   121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
32-258 9.60e-55

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: 177.69  E-value: 9.60e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQ---- 107
Cdd:COG1124     1 MLEVRNLSVSY--GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkafr 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 -QVAFMLQ--KDLLMPWRSIQKNVELGMQIRGRskAERAEVAKALLARCHL-KGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:COG1124    79 rRVQMVFQdpYASLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILE 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVDLPHRD 258
Cdd:COG1124   157 PELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN--GRIVEELTVADLLAG 229
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
32-261 3.59e-54

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


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 175.94  E-value: 3.59e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----- 106
Cdd:COG1127     5 MIEVRNLTKSF------GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekely 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 ---QQVAFMLQKDLL---MpwrSIQKNVELGMQIRGR-SKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALART 179
Cdd:COG1127    79 elrRRIGMLFQGGALfdsL---TVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 180 LAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD-LPHRD 258
Cdd:COG1127   156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLAD--GKIIAEGTPEeLLASD 233

                  ...
gi 1737829014 259 NPI 261
Cdd:COG1127   234 DPW 236
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
33-239 4.39e-53

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: 172.05  E-value: 4.39e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--RGPSQQ-V 109
Cdd:cd03301     1 VELENVTKRFGNV------TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdLPPKDRdI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAE----VAKALlarcHLKGFENHYPHQLSGGMRQRAALARTLAVEPD 185
Cdd:cd03301    75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDErvreVAELL----QIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 186 VLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:cd03301   151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM 204
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
33-249 5.03e-53

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 172.87  E-value: 5.03e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAfM 112
Cdd:COG1126     2 IEIENLHKSF------GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDIN-K 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDL--------LMPWRSIQKNVELG-MQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:COG1126    75 LRRKVgmvfqqfnLFPHLTVLENVTLApIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 184 PDVLLMDEPFSALDAQ-TKMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:COG1126   155 PKVMLFDEPTSALDPElVGEVL--DVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDG--GRIVEE 217
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
33-248 5.44e-53

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 176.45  E-value: 5.44e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ---V 109
Cdd:PRK11432    7 VVLKNITKRF------GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQqrdI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:PRK11432   81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:PRK11432  161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNK--GKIMQ 217
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
49-253 6.34e-53

glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 130254 [Multi-domain]  Cd Length: 363  Bit Score: 176.58  E-value: 6.34e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS---------QQVAFMLQKDLLM 119
Cdd:TIGR01186   4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSpvelrevrrKKIGMVFQQFALF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 120 PWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQ 199
Cdd:TIGR01186  84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 200 TKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEEITVD 253
Cdd:TIGR01186 164 IRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIM--KAGEIVQVGTPD 215
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
33-248 8.87e-53

sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 172.29  E-value: 8.87e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-RGPSQ--QV 109
Cdd:TIGR00968   1 IEIANISKRF------GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDAtRVHARdrKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:TIGR00968  75 GFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:TIGR00968 155 DEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSN--GKIEQ 211
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
30-256 2.03e-50

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 166.78  E-value: 2.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  30 PFAIEyrGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVtLAGK-PVRGPSQQ 108
Cdd:PRK11247   12 PLLLN--AVSKRYGER------TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTaPLAEARED 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARChlkgfeNHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:PRK11247   83 TRLMFQDARLLPWKKVIDNVGLGLKGQWRDAALQALAAVGLADRA------NEWPAALSGGQKQRVALARALIHRPGLLL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVDLPH 256
Cdd:PRK11247  157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEE--GKIGLDLTVDLPR 222
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
32-242 3.53e-50

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 165.65  E-value: 3.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAF 111
Cdd:COG1121     6 AIELENLTVSYGGR------PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKdllmpwRSIQKN--------VELGMQ-----IRGRSKAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALAR 178
Cdd:COG1121    80 VPQR------AEVDWDfpitvrdvVLMGRYgrrglFRRPSRADREAVDEAL-ERVGLEDLADRPIGELSGGQQQRVLLAR 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 179 TLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSER 242
Cdd:COG1121   153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRE-LRREGKTILVVTHDLGAVREYFDRVLLLNRG 215
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
54-248 1.09e-49

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: 164.43  E-value: 1.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS---QQVAFMLQKDLLMPWRSIQKNVEL 130
Cdd:cd03299    15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPpekRDISYVPQNYALFPHMTVYKNIAY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 131 GMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQ 210
Cdd:cd03299    95 GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1737829014 211 MLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIE 248
Cdd:cd03299   175 IRKEFGVTVLHVTHDFEEAWALADKVAIM--LNGKLIQ 210
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
49-247 1.25e-49

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: 164.45  E-value: 1.25e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----QQVAFMLQ--------- 114
Cdd:COG1120    12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSrrelaRRIAYVPQeppapfglt 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 115 -KDLLM----PWRSIqknvelgmqIRGRSKAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:COG1120    92 vRELVAlgryPHLGL---------FGRPSAEDREAVEEAL-ERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII 247
Cdd:COG1120   162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKD--GRIV 217
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
33-239 1.46e-49

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: 163.08  E-value: 1.46e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS------ 106
Cdd:cd03262     1 IEIKNLHKSFGDFH------VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKkninel 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 -QQVAFMLQKDLLMPWRSIQKNVELG-MQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:cd03262    75 rQKVGMVFQQFNLFPHLTVLENITLApIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 185 DVLLMDEPFSALDAQT-KMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:cd03262   155 KVMLFDEPTSALDPELvGEVL--DVMKDLAEEGMTMVVVTHEMGFAREVADRVIFM 208
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
32-253 3.02e-49

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: 170.47  E-value: 3.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknrqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPS---EGQVTLAGKPVRGPS-- 106
Cdd:COG1123     4 LLEVRDLSVRY----PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSea 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 ---QQVAFMLQ--KDLLMPWRsIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLA 181
Cdd:COG1123    80 lrgRRIGMVFQdpMTQLNPVT-VGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 182 VEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEEITVD 253
Cdd:COG1123   159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM--DDGRIVEDGPPE 228
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
33-261 6.21e-49

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


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 162.29  E-value: 6.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQ----- 107
Cdd:cd03261     1 IELRGLTKSF------GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelyr 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 ---QVAFMLQKDLLMPWRSIQKNVELGMQIRGR-SKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:cd03261    75 lrrRMGMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQ---DLAQMLaseGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD-LPHRDN 259
Cdd:cd03261   155 PELLLYDEPTAGLDPIASGVIDDlirSLKKEL---GLTSIMVTHDLDTAFAIADRIAVLYD--GKIVAEGTPEeLRASDD 229

                  ..
gi 1737829014 260 PI 261
Cdd:cd03261   230 PL 231
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
33-227 7.77e-49

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 161.76  E-value: 7.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQVAF 111
Cdd:COG2884     2 IRFENVSKRYPGGR-----EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQK------DL-LMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:COG2884    77 LRRRigvvfqDFrLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1737829014 185 DVLLMDEPFSALDAQTKM-VLqqDLAQMLASEGKTALMITHDLA 227
Cdd:COG2884   157 ELLLADEPTGNLDPETSWeIM--ELLEEINRRGTTVLIATHDLE 198
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
33-281 1.28e-48

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: 1.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR----GPSQQ 108
Cdd:COG4555     2 IEVENLSKKYGKVP------ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkeprEARRQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:COG4555    76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVDlphrdnpiERRKQAG 268
Cdd:COG4555   156 LDEPTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHK--GKVVAQGSLD--------ELREEIG 224
                         250
                  ....*....|...
gi 1737829014 269 MNEYVAHLMELLK 281
Cdd:COG4555   225 EENLEDAFVALIG 237
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
33-252 1.37e-48

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: 161.21  E-value: 1.37e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--------RG 104
Cdd:cd03258     2 IELKNVSKVFGDT--GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsgkelRK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 105 PSQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:cd03258    80 ARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 185 DVLLMDEPFSALDAQ-TKMVLQ--QDLAQMLaseGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITV 252
Cdd:cd03258   160 KVLLCDEATSALDPEtTQSILAllRDINREL---GLTIVLITHEMEVVKRICDRVAVMEK--GEVVEEGTV 225
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
33-246 2.21e-48

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 165.12  E-value: 2.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQ--V 109
Cdd:PRK09452   15 VELRGISKSF------DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvPAENrhV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:PRK09452   89 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTI 246
Cdd:PRK09452  169 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRI 223
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
32-250 6.06e-48

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 163.33  E-value: 6.06e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS---QQ 108
Cdd:PRK10851    2 SIEIANIKKSFGRTQ------VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHardRK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQI-----RGRSKAERAEVAKaLLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:PRK10851   76 VGFVFQHYALFRHMTVFDNIAFGLTVlprreRPNAAAIKAKVTQ-LLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQDLAQmLASEGK-TALMITHDLAEAIALSDRVFVMSErpgTIIEEI 250
Cdd:PRK10851  155 PQILLLDEPFGALDAQVRKELRRWLRQ-LHEELKfTSVFVTHDQEEAMEVADRVVVMSQ---GNIEQA 218
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
33-252 7.82e-48

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 162.55  E-value: 7.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--------RG 104
Cdd:COG1135     2 IELENLSKTF--PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalserelRA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 105 PSQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:COG1135    80 ARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 185 DVLLMDEPFSALDAQ-TKMVLQ--QDLAQMLaseGKTALMITHDLA--EAIAlsDRVFVMSErpGTIIEEITV 252
Cdd:COG1135   160 KVLLCDEATSALDPEtTRSILDllKDINREL---GLTIVLITHEMDvvRRIC--DRVAVLEN--GRIVEQGPV 225
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
33-248 2.78e-47

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: 157.73  E-value: 2.78e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLY-----APSEGQVTLAGKPVRGPSQ 107
Cdd:cd03260     1 IELRDLNVYYGDKH------ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 -------QVAFMLQKDLLMPwRSIQKNVELGMQIRG-RSKAERAEVAKALLARCHLKGFENH--YPHQLSGGMRQRAALA 177
Cdd:cd03260    75 dvlelrrRVGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLA 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 178 RTLAVEPDVLLMDEPFSALDAQTKMVLqQDLAQMLASEgKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:cd03260   154 RALANEPEVLLLDEPTSALDPISTAKI-EELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLN--GRLVE 220
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
22-240 3.81e-47

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 161.93  E-value: 3.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  22 AQPAAAPLpfaIEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGK- 100
Cdd:PRK11607   12 TRKALTPL---LEIRNLTKSFDGQH------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVd 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 101 -----PVRGPsqqVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAA 175
Cdd:PRK11607   83 lshvpPYQRP---INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 176 LARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMS 240
Cdd:PRK11607  160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
33-246 6.51e-47

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 156.13  E-value: 6.51e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQGkgemtaVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----Q 107
Cdd:COG4619     1 LELEGLSFRVGGKPI------LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppewrR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLmpWR-SIQKNVELGMQIRGRSKAEraEVAKALLARCHL-KGFENHYPHQLSGGMRQRAALARTLAVEPD 185
Cdd:COG4619    75 QVAYVPQEPAL--WGgTVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPD 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 186 VLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTI 246
Cdd:COG4619   151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTL--EAGRL 209
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
33-239 1.37e-46

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: 154.09  E-value: 1.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----QQ 108
Cdd:cd03230     1 IEVRNLSKRYGKK------TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPeevkRR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPwrsiqknvelgmqirgrskaeraevakallarcHLKGFENHYphqLSGGMRQRAALARTLAVEPDVLL 188
Cdd:cd03230    75 IGYLPEEPSLYE---------------------------------NLTVRENLK---LSGGMKQRLALAQALLHDPELLI 118
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:cd03230   119 LDEPTSGLDPESRREFWELLRE-LKKEGKTILLSSHILEEAERLCDRVAIL 168
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
69-240 1.64e-46

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: 158.81  E-value: 1.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  69 LIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--RGPSQQ-VAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEV 145
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVtnVPPHLRhINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 146 AKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHD 225
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
                         170
                  ....*....|....*
gi 1737829014 226 LAEAIALSDRVFVMS 240
Cdd:TIGR01187 161 QEEAMTMSDRIAIMR 175
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
64-241 3.29e-46

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: 154.76  E-value: 3.29e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  64 GEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG-------KPVRGPSQQ--VAFMLQKDLLMPWRSIQKNVELGMqi 134
Cdd:cd03297    23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQrkIGLVFQQYALFPHLNVRENLAFGL-- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 135 RGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAS 214
Cdd:cd03297   101 KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKN 180
                         170       180
                  ....*....|....*....|....*..
gi 1737829014 215 EGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:cd03297   181 LNIPVIFVTHDLSEAEYLADRIVVMED 207
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
61-262 5.07e-46

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 154.53  E-value: 5.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG--PSQQ-VAFMLQKDLLMPWRSIQKNVELGMQIRGR 137
Cdd:COG3840    22 IAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlpPAERpVSMLFQENNLFPHLTVAQNIGLGLRPGLK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 138 -SKAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAqtkmVLQQD----LAQML 212
Cdd:COG3840   102 lTAEQRAQVEQAL-ERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP----ALRQEmldlVDELC 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1737829014 213 ASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVDLPHRDNPIE 262
Cdd:COG3840   177 RERGLTVLMVTHDPEDAARIADRVLLVAD--GRIAADGPTAALLDGEPPP 224
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
52-239 1.22e-45

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: 153.07  E-value: 1.22e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFMLQKdllmpwRSIQKN---- 127
Cdd:cd03235    13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQR------RSIDRDfpis 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 128 ----VELGMQIRGR-----SKAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:cd03235    87 vrdvVLMGLYGHKGlfrrlSKADKAKVDEAL-ERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1737829014 199 QTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:cd03235   166 KTQEDIYELLRE-LRREGMTILVVTHDLGLVLEYFDRVLLL 205
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
32-249 2.34e-45

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: 152.97  E-value: 2.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKP---------- 101
Cdd:COG4181     8 IIELRGLTKTV--GTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDlfaldedara 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 102 -VRGpsQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAEraEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTL 180
Cdd:COG4181    86 rLRA--RHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 181 AVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAiALSDRVFVMSErpGTIIEE 249
Cdd:COG4181   162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRA--GRLVED 227
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
36-253 1.20e-44

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 153.67  E-value: 1.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  36 RGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAP---SEGQVTLAGKPVRGPSQ----- 107
Cdd:COG0444     5 RNLKVYF--PTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkelrk 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 ----QVAFMLQKDL--LMPWRSIQKNVELGMQI-RGRSKAERAEVAKALLARCHLKGFENH---YPHQLSGGMRQRAALA 177
Cdd:COG0444    83 irgrEIQMIFQDPMtsLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRldrYPHELSGGMRQRVMIA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 178 RTLAVEPDVLLMDEPFSALD----AQtkmVLQ--QDLAQMLaseGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEIT 251
Cdd:COG0444   163 RALALEPKLLIADEPTTALDvtiqAQ---ILNllKDLQREL---GLAILFITHDLGVVAEIADRVAVMYA--GRIVEEGP 234

                  ..
gi 1737829014 252 VD 253
Cdd:COG0444   235 VE 236
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
33-239 2.62e-44

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: 148.30  E-value: 2.62e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQGKgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----Q 107
Cdd:cd03228     1 IEFKNVSFSYPGRPKP----VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDleslrK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPwRSIQKNVelgmqirgrskaeraevakallarchlkgfenhyphqLSGGMRQRAALARTLAVEPDVL 187
Cdd:cd03228    77 NIAYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPIL 118
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 188 LMDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAeAIALSDRVFVM 239
Cdd:cd03228   119 ILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLS-TIRDADRIIVL 167
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
33-249 4.36e-44

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 149.86  E-value: 4.36e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS------ 106
Cdd:PRK09493    2 IEFKNVSKHF------GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKvderli 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 -QQVAFMLQKDLLMPWRSIQKNVELG-MQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:PRK09493   76 rQEAGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 185 DVLLMDEPFSALDAQTKM-VLQqdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:PRK09493  156 KLMLFDEPTSALDPELRHeVLK--VMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDK--GRIAED 217
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
36-249 4.54e-44

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: 150.19  E-value: 4.54e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  36 RGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQVA---- 110
Cdd:COG0411     8 RGLTKRF------GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlPPHRIArlgi 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 111 ---FmlQKDLLMPWRSIQKNVELGMQIRGRS-------------KAERAEVAKA--LLARCHLKGFENHYPHQLSGGMRQ 172
Cdd:COG0411    82 artF--QNPRLFPELTVLENVLVAAHARLGRgllaallrlprarREEREARERAeeLLERVGLADRADEPAGNLSYGQQR 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 173 RAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:COG0411   160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF--GRVIAE 234
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
24-239 1.37e-43

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 151.04  E-value: 1.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  24 PAAAPLpfaIEYRGVTRRFKNRQG-----KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLA 98
Cdd:COG4608     2 AMAEPL---LEVRDLKKHFPVRGGlfgrtVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  99 GKPVRGPSQQVAFMLQKDLLM----------PWRSIQKNVELGMQIRG-RSKAERAEVAKALLARCHLK-GFENHYPHQL 166
Cdd:COG4608    79 GQDITGLSGRELRPLRRRMQMvfqdpyaslnPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRpEHADRYPHEF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 167 SGGMRQRAALARTLAVEPDVLLMDEPFSALD----AQtkmV------LQQDLaqmlaseGKTALMITHDLAEAIALSDRV 236
Cdd:COG4608   159 SGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQ---VlnlledLQDEL-------GLTYLFISHDLSVVRHISDRV 228

                  ...
gi 1737829014 237 FVM 239
Cdd:COG4608   229 AVM 231
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
32-249 2.43e-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: 156.92  E-value: 2.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknrqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GPS--- 106
Cdd:COG2274   473 DIELENVSFRY----PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqiDPAslr 548
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 QQVAFMLQKDLLMPwRSIQKNVELgmqirGRSKAERAEVAKAL-LARCHlkGFENHYPH-----------QLSGGMRQRA 174
Cdd:COG2274   549 RQIGVVLQDVFLFS-GTIRENITL-----GDPDATDEEIIEAArLAGLH--DFIEALPMgydtvvgeggsNLSGGQRQRL 620
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 175 ALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAseGKTALMITHDLAeAIALSDRVFVMSErpGTIIEE 249
Cdd:COG2274   621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLS-TIRLADRIIVLDK--GRIVED 690
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
34-241 2.77e-43

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: 145.08  E-value: 2.77e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  34 EYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRgpsqqvafml 113
Cdd:cd00267     1 EIENLSFRYGGR------TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA---------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 114 qkdllmpwrsiqknvelgmqiRGRSKAERAEVAkallarchlkgfenhYPHQLSGGMRQRAALARTLAVEPDVLLMDEPF 193
Cdd:cd00267    65 ---------------------KLPLEELRRRIG---------------YVPQLSGGQRQRVALARALLLNPDLLLLDEPT 108
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1737829014 194 SALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:cd00267   109 SGLDPASRERLLELLRE-LAEEGRTVIIVTHDPELAELAADRVIVLKD 155
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
36-253 7.79e-43

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: 146.43  E-value: 7.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  36 RGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQVA---- 110
Cdd:cd03219     4 RGLTKRF------GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlPPHEIArlgi 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 111 ---FmlQKDLLMPWRSIQKNVELGMQIRGRS--------KAERAEVAKA--LLARCHLKGFENHYPHQLSGGMRQRAALA 177
Cdd:cd03219    78 grtF--QIPRLFPELTVLENVMVAAQARTGSglllararREEREARERAeeLLERVGLADLADRPAGELSYGQQRRLEIA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 178 RTLAVEPDVLLMDEPFSALDAQtkmvLQQDLAQM---LASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:cd03219   156 RALATDPKLLLLDEPAAGLNPE----ETEELAELireLRERGITVLLVEHDMDVVMSLADRVTVLDQ--GRVIAEGTPD 228
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
47-247 8.10e-43

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: 144.50  E-value: 8.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  47 GKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----QQVAFMLQkdllmpw 121
Cdd:cd03214     8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSpkelaRKIAYVPQ------- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 rsiqknvelgmqirgrskaeraevakaLLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTK 201
Cdd:cd03214    81 ---------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1737829014 202 MVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII 247
Cdd:cd03214   134 IELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKD--GRIV 177
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
33-241 1.89e-42

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: 145.19  E-value: 1.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKnrQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQ----- 107
Cdd:TIGR02211   2 LKCENLGKRYQ--EGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSnerak 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 ----QVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:TIGR02211  80 lrnkKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQ 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 184 PDVLLMDEPFSALDAQT-KMVLqqDLAQMLASEGKTALMI-THDLaEAIALSDRVFVMSE 241
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNaKIIF--DLMLELNRELNTSFLVvTHDL-ELAKKLDRVLEMKD 216
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
17-249 1.03e-41

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: 151.06  E-value: 1.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  17 ADARHAQPAAAPLPFAIEYRGVTRRFKNRQgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVT 96
Cdd:COG4988   321 AAPAGTAPLPAAGPPSIELEDVSFSYPGGR-----PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  97 LAGKPVRGPS-----QQVAFMLQKDLLMPWrSIQKNVELgmqirGRSKAERAEVAKAlLARCHLKGFENHYPH------- 164
Cdd:COG4988   396 INGVDLSDLDpaswrRQIAWVPQNPYLFAG-TIRENLRL-----GRPDASDEELEAA-LEAAGLDEFVAALPDgldtplg 468
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 165 ----QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmlASEGKTALMITHDLAeAIALSDRVFVMs 240
Cdd:COG4988   469 eggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR--LAKGRTVILITHRLA-LLAQADRILVL- 544

                  ....*....
gi 1737829014 241 eRPGTIIEE 249
Cdd:COG4988   545 -DDGRIVEQ 552
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
17-249 3.29e-41

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 149.93  E-value: 3.29e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  17 ADARHAQPAAaPLPFAIEYRGVTRRFKNRQgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVT 96
Cdd:COG1132   325 PDPPGAVPLP-PVRGEIEFENVSFSYPGDR-----PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  97 LAGKPVRGPSQ-----QVAFMLQKDLLMPwRSIQKNvelgmqIR-GRSKAERAEVAKAL-LARCH--LKGFENHYPHQ-- 165
Cdd:COG1132   399 IDGVDIRDLTLeslrrQIGVVPQDTFLFS-GTIREN------IRyGRPDATDEEVEEAAkAAQAHefIEALPDGYDTVvg 471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 166 -----LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAseGKTALMITHDLAeAIALSDRVFVMS 240
Cdd:COG1132   472 ergvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLS-TIRNADRILVLD 548

                  ....*....
gi 1737829014 241 ErpGTIIEE 249
Cdd:COG1132   549 D--GRIVEQ 555
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
54-242 3.49e-41

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 141.47  E-value: 3.49e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAP---SEGQVTLAGKPV-RGPSQQ--VAFMLQKDLLMPWRSIQKN 127
Cdd:COG4136    17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLtALPAEQrrIGILFQDDLLFPHLSVGEN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 128 VELGMQiRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQD 207
Cdd:COG4136    97 LAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREF 175
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1737829014 208 LAQMLASEGKTALMITHDlAEAIALSDRVFVMSER 242
Cdd:COG4136   176 VFEQIRQRGIPALLVTHD-EEDAPAAGRVLDLGNW 209
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
33-240 4.97e-40

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: 138.79  E-value: 4.97e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFM 112
Cdd:cd03263     1 LQIRNLTKTYKK----GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 L----QKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:cd03263    77 LgycpQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAEAIALSDRVFVMS 240
Cdd:cd03263   157 LDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMS 206
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
32-249 2.20e-39

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 137.96  E-value: 2.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTL------AGKP---- 101
Cdd:PRK11264    3 AIEVKNLVKKFHGQ------TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSlsqq 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 102 ---VRGPSQQVAFMLQKDLLMPWRSIQKNVELG-MQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALA 177
Cdd:PRK11264   77 kglIRQLRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 178 RTLAVEPDVLLMDEPFSALDAQtkmVLQQDLAQM--LASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:PRK11264  157 RALAMRPEVILFDEPTSALDPE---LVGEVLNTIrqLAQEKRTMVIVTHEMSFARDVADRAIFMDQ--GRIVEQ 225
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
54-194 2.28e-39

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 134.70  E-value: 2.28e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----QQVAFMLQKDLLMPWRSIQKNV 128
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDErkslrKEIGYVFQDPQLFPRLTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 129 ELGMQIRGRSKAERAEVAKALLARCHLKGFENH----YPHQLSGGMRQRAALARTLAVEPDVLLMDEPFS 194
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
49-242 4.37e-39

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: 136.07  E-value: 4.37e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----QQVAFMLQKDLLMPWRSI 124
Cdd:COG4133    13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARedyrRRLAYLGHADGLKPELTV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 125 QKNVELGMQIRGRSKAERAevAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVL 204
Cdd:COG4133    93 RENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1737829014 205 QQDLAQMLAsEGKTALMITHDLAEaiALSDRVFVMSER 242
Cdd:COG4133   171 AELIAAHLA-RGGAVLLTTHQPLE--LAAARVLDLGDF 205
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
33-247 5.12e-39

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: 134.48  E-value: 5.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSqqvafm 112
Cdd:cd03216     1 LELRGITKRF------GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 lqkdllmPWRSIQKNVELgmqirgrskaeraeVakallarchlkgfenhypHQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:cd03216    69 -------PRDARRAGIAM--------------V------------------YQLSVGERQMVEIARALARNARLLILDEP 109
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 193 FSAL-DAQTKMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTII 247
Cdd:cd03216   110 TAALtPAEVERLF--KVIRRLRAQGVAVIFISHRLDEVFEIADRVTVL--RDGRVV 161
PhnT TIGR03258
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ...
49-241 5.77e-39

2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.


Pssm-ID: 132302 [Multi-domain]  Cd Length: 362  Bit Score: 140.13  E-value: 5.77e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPS--EGQVTLAGKPV-RGPSQQ--VAFMLQKDLLMPWRS 123
Cdd:TIGR03258  16 GANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDLtHAPPHKrgLALLFQNYALFPHLK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:TIGR03258  96 VEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDANIRAN 175
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1737829014 204 LQQDLAQMLASEGK-TALMITHDLAEAIALSDRVFVMSE 241
Cdd:TIGR03258 176 MREEIAALHEELPElTILCVTHDQDDALTLADKAGIMKD 214
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
56-239 9.97e-39

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: 135.31  E-value: 9.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG------KPVRGPsqqVAFMLQKDLLMPWRSIQKNVE 129
Cdd:cd03298    16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaaPPADRP---VSMLFQENNLFAHLTVEQNVG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 130 LGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLA 209
Cdd:cd03298    93 LGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
                         170       180       190
                  ....*....|....*....|....*....|
gi 1737829014 210 QMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:cd03298   173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFL 202
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
21-248 1.28e-38

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


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 142.60  E-value: 1.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  21 HAQPAAAPLPFAIEYRGVTRRFKNrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGK 100
Cdd:COG4987   322 PAEPAPAPGGPSLELEDVSFRYPG----AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGV 397
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 101 PVRGPS-----QQVAFMLQKDLLMPwRSIQKNVELgmqirGRSKAERAEVAKAlLARCHLKGFENHYPH----------- 164
Cdd:COG4987   398 DLRDLDeddlrRRIAVVPQRPHLFD-TTLRENLRL-----ARPDATDEELWAA-LERVGLGDWLAALPDgldtwlgeggr 470
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 165 QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmlASEGKTALMITHDLAeAIALSDRVFVMSErpG 244
Cdd:COG4987   471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE--ALAGRTVLLITHRLA-GLERMDRILVLED--G 545

                  ....
gi 1737829014 245 TIIE 248
Cdd:COG4987   546 RIVE 549
heterocyst_DevA TIGR02982
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...
47-225 1.34e-38

ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.


Pssm-ID: 274374 [Multi-domain]  Cd Length: 220  Bit Score: 135.15  E-value: 1.34e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  47 GKGEM--TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQ--------QVAFMLQKD 116
Cdd:TIGR02982  12 GHGSLrkQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKkqlvqlrrRIGYIFQAH 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 117 LLMPWRSIQKNVELGMQI-RGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSA 195
Cdd:TIGR02982  92 NLLGFLTARQNVQMALELqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAA 171
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1737829014 196 LDAQT-KMVLqqDLAQMLASE-GKTALMITHD 225
Cdd:TIGR02982 172 LDSKSgRDVV--ELMQKLAKEqGCTILMVTHD 201
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
33-249 1.41e-38

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: 135.74  E-value: 1.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQgkgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR-----GPSQ 107
Cdd:cd03249     1 IEFKNVSFRYPSRP---DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRdlnlrWLRS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPwRSIQKNVELGmqIRGRSKAERAEVAKalLARCH--LKGFENHY-----PH--QLSGGMRQRAALAR 178
Cdd:cd03249    78 QIGLVSQEPVLFD-GTIAENIRYG--KPDATDEEVEEAAK--KANIHdfIMSLPDGYdtlvgERgsQLSGGQKQRIAIAR 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 179 TLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmlASEGKTALMITHDLAeAIALSDRVFVMSerPGTIIEE 249
Cdd:cd03249   153 ALLRNPKILLLDEATSALDAESEKLVQEALDR--AMKGRTTIVIAHRLS-TIRNADLIAVLQ--NGQVVEQ 218
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
13-249 2.01e-37

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 138.66  E-value: 2.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  13 AEAYADARHAQPAAAPLpfaIEYRGVTRRFKNRQG-----KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLlnmGAGL 87
Cdd:COG4172   259 AEPRGDPRPVPPDAPPL---LEARDLKVWFPIKRGlfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTL---GLAL 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  88 YA--PSEGQVTLAGKPVRGPSQQVAFMLQKDL----------LMPWRSIQKNVELGMQI--RGRSKAERAEVAKALLARC 153
Cdd:COG4172   333 LRliPSEGEIRFDGQDLDGLSRRALRPLRRRMqvvfqdpfgsLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEV 412
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 154 HLK-GFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDaqtkMVLQQDLAQMLAS----EGKTALMITHDLAE 228
Cdd:COG4172   413 GLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQILDLLRDlqreHGLAYLFISHDLAV 488
                         250       260
                  ....*....|....*....|.
gi 1737829014 229 AIALSDRVFVMSErpGTIIEE 249
Cdd:COG4172   489 VRALAHRVMVMKD--GKVVEQ 507
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
32-248 2.03e-37

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 135.74  E-value: 2.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTrrfKNRQGKGEmtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--RGPSQQ- 108
Cdd:PRK11650    3 GLKLQAVR---KSYDGKTQ--VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVneLEPADRd 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAER----AEVAKALlarcHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:PRK11650   78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIeervAEAARIL----ELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 185 DVLLMDEPFSALDAQTK--MVLQ-QDLAQMLaseGKTALMITHDLAEAIALSDRVFVMS----ERPGTIIE 248
Cdd:PRK11650  154 AVFLFDEPLSNLDAKLRvqMRLEiQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNggvaEQIGTPVE 221
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
33-252 2.11e-37

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 135.31  E-value: 2.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQV--------TLAGKPVRG 104
Cdd:PRK11153    2 IELKNISKVF--PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgqdltALSEKELRK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 105 PSQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:PRK11153   80 ARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 185 DVLLMDEPFSALDAQ-TKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITV 252
Cdd:PRK11153  160 KVLLCDEATSALDPAtTRSILEL-LKDINRELGLTIVLITHEMDVVKRICDRVAVIDA--GRLVEQGTV 225
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
32-239 1.45e-36

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: 129.63  E-value: 1.45e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFKNRQGKgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GPS--- 106
Cdd:cd03245     2 RIEFRNVSFSYPNQEIP----ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPAdlr 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 QQVAFMLQkDLLMPWRSIQKNVELGMQIrgrskAERAEVAKAL-------LARCHLKGF-----ENHYphQLSGGMRQRA 174
Cdd:cd03245    78 RNIGYVPQ-DVTLFYGTLRDNITLGAPL-----ADDERILRAAelagvtdFVNKHPNGLdlqigERGR--GLSGGQRQAV 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 175 ALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAseGKTALMITHDLAeAIALSDRVFVM 239
Cdd:cd03245   150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVM 211
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
33-225 1.52e-36

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


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 129.45  E-value: 1.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNrqgkgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQVAF 111
Cdd:cd03292     1 IEFINVTKTYPN-----GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 M-------LQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:cd03292    76 LrrkigvvFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1737829014 185 DVLLMDEPFSALDAQTK---MVLQQDLAQMlaseGKTALMITHD 225
Cdd:cd03292   156 TILIADEPTGNLDPDTTweiMNLLKKINKA----GTTVVVATHA 195
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
53-253 1.76e-36

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 134.39  E-value: 1.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS---------QQVAFMLQKDLLMPWRS 123
Cdd:PRK10070   43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelrevrrKKIAMVFQSFALMPHMT 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:PRK10070  123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1737829014 204 LQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:PRK10070  203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN--GEVVQVGTPD 250
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
33-253 2.30e-36

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: 129.41  E-value: 2.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQV--- 109
Cdd:cd03265     1 IEVENLVKKY------GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVrrr 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 -AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:cd03265    75 iGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:cd03265   155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDH--GRIIAEGTPE 217
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
33-257 4.24e-36

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: 129.22  E-value: 4.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNrqGKgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQV--------TLAGKPVRG 104
Cdd:cd03256     1 IEVENLSKTYPN--GK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinKLKGKALRQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 105 PSQQVAFMLQKDLLMPWRSIQKNVELGM--------QIRGR-SKAERaEVAKALLARCHLKGFENHYPHQLSGGMRQRAA 175
Cdd:cd03256    76 LRRQIGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLfPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 176 LARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII-----EEI 250
Cdd:cd03256   155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD--GRIVfdgppAEL 232

                  ....*..
gi 1737829014 251 TVDLPHR 257
Cdd:cd03256   233 TDEVLDE 239
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
33-250 4.48e-36

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: 128.10  E-value: 4.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV---RGPSQQV 109
Cdd:cd03268     1 LKTNDLTKTYGKKR------VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqknIEALRRI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVakalLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:cd03268    75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 190 DEPFSALDAQTKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEI 250
Cdd:cd03268   151 DEPTNGLDPDGIKELRE-LILSLRDQGITVLISSHLLSEIQKVADRIGIINK--GKLIEEG 208
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
56-241 8.87e-36

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: 131.38  E-value: 8.87e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV----RG---PSQQ--VAFMLQKDLLMPWRSIQK 126
Cdd:COG4148    17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsaRGiflPPHRrrIGYVFQEARLFPHLSVRG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 NVELGMQ--IRGRSKAERAEVAK-----ALLARchlkgfenhYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQ 199
Cdd:COG4148    97 NLLYGRKraPRAERRISFDEVVEllgigHLLDR---------RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1737829014 200 TKMVLQQDLAQmLASEGKT-ALMITHDLAEAIALSDRVFVMSE 241
Cdd:COG4148   168 RKAEILPYLER-LRDELDIpILYVSHSLDEVARLADHVVLLEQ 209
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
49-239 2.13e-35

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 130.53  E-value: 2.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG--PSQQ-VAFMLQKDLLMPWRSIQ 125
Cdd:PRK11000   14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvpPAERgVGMVFQSYALYPHLSVA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 126 KNVELGMQIRGRSKAE---RAEVAKALLARCHLKgfeNHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKM 202
Cdd:PRK11000   94 ENMSFGLKLAGAKKEEinqRVNQVAEVLQLAHLL---DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1737829014 203 VLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:PRK11000  171 QMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVL 207
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
49-286 2.27e-35

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: 129.05  E-value: 2.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV----RGPSQQVAFMLQK----DLLMP 120
Cdd:TIGR01188   4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvrepRKVRRSIGIVPQYasvdEDLTG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 121 WrsiqKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT 200
Cdd:TIGR01188  84 R----ENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 201 KMVLqQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITV-DLPHR----------DNPIERRKQAGM 269
Cdd:TIGR01188 160 RRAI-WDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDH--GRIIAEGTPeELKRRlgkdtlesrpRDIQSLKVEVSM 236
                         250
                  ....*....|....*....
gi 1737829014 270 --NEYVAHLMELLKVGRDD 286
Cdd:TIGR01188 237 liAELGETGLGLLAVTVDS 255
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
49-248 2.87e-35

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 127.05  E-value: 2.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG-----------KPVRGPSQQVAFMLQKDL 117
Cdd:PRK11124   13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdKAIRELRRNVGMVFQQYN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 118 LMPWRSIQKN-VELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSAL 196
Cdd:PRK11124   93 LWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 197 DAQ-TKMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:PRK11124  173 DPEiTAQIV--SIIRELAETGITQVIVTHEVEVARKTASRVVYMEN--GHIVE 221
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
33-249 5.31e-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: 126.19  E-value: 5.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----Q 107
Cdd:cd03251     1 VEFKNVTFRY----PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlaslrR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQkDLLMPWRSIQKNVELgmqirGRSKAERAEVAKAL-LARCH--LKGFENHYPH-------QLSGGMRQRAALA 177
Cdd:cd03251    77 QIGLVSQ-DVFLFNDTVAENIAY-----GRPGATREEVEEAArAANAHefIMELPEGYDTvigergvKLSGGQRQRIAIA 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 178 RTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLasEGKTALMITHDLAeAIALSDRVFVMSErpGTIIEE 249
Cdd:cd03251   151 RALLKDPPILILDEATSALDTESERLVQAALERLM--KNRTTFVIAHRLS-TIENADRIVVLED--GKIVER 217
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
52-241 6.16e-35

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 126.77  E-value: 6.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQVAFML-----QKDLLMPWRSIQ 125
Cdd:COG4559    15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwSPWELARRRavlpqHSSLAFPFTVEE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 126 KnVELGMQIRGRSKAERAEVAKALLARCHLKGFEN-HYPhQLSGGMRQRAALARTLA-------VEPDVLLMDEPFSALD 197
Cdd:COG4559    95 V-VALGRAPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1737829014 198 -AQTKMVLQqdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:COG4559   173 lAHQHAVLR--LARQLARRGGGVVAVLHDLNLAAQYADRILLLHQ 215
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
61-241 1.03e-34

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 125.46  E-value: 1.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG--PSQQVAFML-QKDLLMPWRSIQKNVELGMQIRGR 137
Cdd:PRK10771   22 VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTtpPSRRPVSMLfQENNLFSHLTVAQNIGLGLNPGLK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 138 SKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGK 217
Cdd:PRK10771  102 LNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQL 181
                         170       180
                  ....*....|....*....|....
gi 1737829014 218 TALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK10771  182 TLLMVSHSLEDAARIAPRSLVVAD 205
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
32-241 1.38e-34

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 125.65  E-value: 1.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQVA 110
Cdd:PRK13548    2 MLEARNLSVRLGGR------TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 111 FML-----QKDLLMPWrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLA---- 181
Cdd:PRK13548   76 RRRavlpqHSSLSFPF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwe 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 182 --VEPDVLLMDEPFSALD-AQTKMVLQqdLAQMLASEGKTA-LMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK13548  155 pdGPPRWLLLDEPTSALDlAHQHHVLR--LARQLAHERGLAvIVVLHDLNLAARYADRIVLLHQ 216
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
32-272 1.68e-34

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 126.38  E-value: 1.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-RGPSQQVA 110
Cdd:COG4152     1 MLELKGLTKRF------GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLdPEDRRRIG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 111 FMLQKdllmpwRSIQKNVELGMQI------RGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP 184
Cdd:COG4152    75 YLPEE------RGLYPKMKVGEQLvylarlKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 185 DVLLMDEPFSALD--AQTKMVlqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVDlphrdnpiE 262
Cdd:COG4152   149 ELLILDEPFSGLDpvNVELLK---DVIRELAAKGTTVIFSSHQMELVEELCDRIVIINK--GRKVLSGSVD--------E 215
                         250
                  ....*....|
gi 1737829014 263 RRKQAGMNEY 272
Cdd:COG4152   216 IRRQFGRNTL 225
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
58-241 2.54e-34

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: 123.82  E-value: 2.54e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  58 SIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG--PSQQ-VAFMLQKDLLMPWRSIQKNVELGMQI 134
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGlaPYQRpVSMLFQENNLFAHLTVRQNIGLGLHP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 135 RGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAS 214
Cdd:TIGR01277  98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
                         170       180
                  ....*....|....*....|....*..
gi 1737829014 215 EGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQ 204
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
53-249 3.56e-34

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: 123.87  E-value: 3.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----QQVAFMLQKDLLMPwRSIQKN 127
Cdd:cd03254    18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkslrSMIGVVLQDTFLFS-GTIMEN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 128 VELgmqirGRSKAERAEVAKAL-LARCHL------KGFE---NHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD 197
Cdd:cd03254    97 IRL-----GRPNATDEEVIEAAkEAGAHDfimklpNGYDtvlGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 198 AQTKMVLQQDLAQMLasEGKTALMITHDLAeAIALSDRVFVMSErpGTIIEE 249
Cdd:cd03254   172 TETEKLIQEALEKLM--KGRTSIIIAHRLS-TIKNADKILVLDD--GKIIEE 218
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
33-239 7.95e-34

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: 122.39  E-value: 7.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR-GPSQQVAF 111
Cdd:cd03269     1 LEVENVTKRF------GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiAARNRIGY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDE 191
Cdd:cd03269    75 LPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1737829014 192 PFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:cd03269   155 PFSGLDPVNVELLKDVIRE-LARAGKTVILSTHQMELVEELCDRVLLL 201
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
49-249 8.01e-34

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 123.20  E-value: 8.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG-----------KPVRGPSQQVAFMLQKDL 117
Cdd:COG4161    13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkpseKAIRLLRQKVGMVFQQYN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 118 LMPWRSIQKN-VELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSAL 196
Cdd:COG4161    93 LWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 197 DAQ-TKMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:COG4161   173 DPEiTAQVV--EIIRELSQTGITQVIVTHEVEFARKVASQVVYMEK--GRIIEQ 222
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
24-248 1.01e-33

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 123.22  E-value: 1.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  24 PAAAPLPFAIEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLL---N-MGAgLYaPS---EGQVT 96
Cdd:COG1117     3 APASTLEPKIEVRNLNVYYGDKQ------ALKDINLDIPENKVTALIGPSGCGKSTLLrclNrMND-LI-PGarvEGEIL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  97 LAGKPVRGPS-------QQVAFMLQKDLLMPWrSIQKNVELGMQIRG-RSKAERAEVAKALLARCHL----KGFENHYPH 164
Cdd:COG1117    75 LDGEDIYDPDvdvvelrRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGiKSKSELDEIVEESLRKAALwdevKDRLKKSAL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 165 QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQ-TKMVlqQDLAQMLASEgKTALMITHDLAEAIALSDRVFVMSErp 243
Cdd:COG1117   154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIsTAKI--EELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYL-- 228

                  ....*
gi 1737829014 244 GTIIE 248
Cdd:COG1117   229 GELVE 233
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
33-278 1.60e-33

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 123.59  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKP--------VRg 104
Cdd:PRK13635    6 IRVEHISFRYPD----AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdVR- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 105 psQQVAFMLQK-DLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:PRK13635   81 --RQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAiALSDRVFVMSE-------------RPGTIIEEI 250
Cdd:PRK13635  159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKgeileegtpeeifKSGHMLQEI 237
                         250       260
                  ....*....|....*....|....*...
gi 1737829014 251 TVDLPHRDNPIERRKQAGMNEYVAHLME 278
Cdd:PRK13635  238 GLDVPFSVKLKELLKRNGILLPNTYLTM 265
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
32-253 3.56e-33

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 126.67  E-value: 3.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----- 106
Cdd:COG1129     4 LLEMRGISKSF------GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprdaq 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 -QQVAFMLQKDLLMPWRSIQKNVELGMQIRGRS----KAERAEvAKALLAR--CHLKgfenhyPHQ----LSGGMRQRAA 175
Cdd:COG1129    78 aAGIAIIHQELNLVPNLSVAENIFLGREPRRGGlidwRAMRRR-ARELLARlgLDID------PDTpvgdLSVAQQQLVE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 176 LARTLAVEPDVLLMDEPFSALDAQ-TKMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTII-----EE 249
Cdd:COG1129   151 IARALSRDARVLILDEPTASLTEReVERLF--RIIRRLKAQGVAIIYISHRLDEVFEIADRVTVL--RDGRLVgtgpvAE 226

                  ....
gi 1737829014 250 ITVD 253
Cdd:COG1129   227 LTED 230
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
52-236 3.80e-33

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 120.03  E-value: 3.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTlagkpvRGPSQQVAFMLQK---DLLMPWRSIQKnV 128
Cdd:NF040873    6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------RAGGARVAYVPQRsevPDSLPLTVRDL-V 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 129 ELGM-QIRGR----SKAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:NF040873   79 AMGRwARRGLwrrlTRDDRAAVDDAL-ERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1737829014 204 LQQDLAQmLASEGKTALMITHDLaEAIALSDRV 236
Cdd:NF040873  158 IIALLAE-EHARGATVVVVTHDL-ELVRRADPC 188
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
24-239 4.36e-33

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


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 127.02  E-value: 4.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  24 PAAAPLPFAIEYRGVTRRFKnrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR 103
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYP-----GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA 387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 104 GPSQ-----QVAFMLQKDLLMPwRSIQKNVELgmqirGRSKAERAEVAKAlLARCHLKGFENHYP-----------HQLS 167
Cdd:TIGR02857 388 DADAdswrdQIAWVPQHPFLFA-GTIAENIRL-----ARPDASDAEIREA-LERAGLDEFVAALPqgldtpigeggAGLS 460
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 168 GGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmlASEGKTALMITHDLAeAIALSDRVFVM 239
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA--LAQGRTVLLVTHRLA-LAALADRIVVL 529
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
32-241 6.29e-33

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 122.61  E-value: 6.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----Q 107
Cdd:PRK13537    7 PIDFRNVEKRY------GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRArharQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVL 187
Cdd:PRK13537   81 RVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 188 LMDEPFSALDAQTKMVLQQDLAQMLASeGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK13537  161 VLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEE 213
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
30-285 1.18e-32

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 125.14  E-value: 1.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  30 PFAIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQV 109
Cdd:COG3845     3 PPALELRGITKRF------GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 A-----------FMLQKDLlmpwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFE---NHYPHQLSGGMRQRAA 175
Cdd:COG3845    77 AialgigmvhqhFMLVPNL-----TVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDvdpDAKVEDLSVGEQQRVE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 176 LARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEEITVdlp 255
Cdd:COG3845   152 ILKALYRGARILILDEPTAVLTPQEADELFEILRR-LAAEGKSIIFITHKLREVMAIADRVTVL--RRGKVVGTVDT--- 225
                         250       260       270
                  ....*....|....*....|....*....|
gi 1737829014 256 hrdnpierrKQAGMNEyVAHLMellkVGRD 285
Cdd:COG3845   226 ---------AETSEEE-LAELM----VGRE 241
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
33-251 1.25e-32

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 120.58  E-value: 1.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFkNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-RGPSQQVAF 111
Cdd:COG1101     2 LELKNLSKTF-NPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYKRAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 ML----QkDLLM---PWRSIQKNVELGMQiRGRS--------KAERAEVaKALLARCHLkGFENHYPHQ---LSGGMRQR 173
Cdd:COG1101    81 YIgrvfQ-DPMMgtaPSMTIEENLALAYR-RGKRrglrrgltKKRRELF-RELLATLGL-GLENRLDTKvglLSGGQRQA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 174 AALARTLAVEPDVLLMDEPFSALDAQT-KMVLqqDLAQMLASEGK-TALMITHDLAEAIALSDRVFVMSErpGTIIEEIT 251
Cdd:COG1101   157 LSLLMATLTKPKLLLLDEHTAALDPKTaALVL--ELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMHE--GRIILDVS 232
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
36-239 1.89e-32

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 122.00  E-value: 1.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  36 RGVTRRFKNRQG--KGEMT--AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAF 111
Cdd:PRK11308    9 IDLKKHYPVKRGlfKPERLvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKDLLM----------PWRSIQKNVELGMQIRGR-SKAERAEVAKALLARCHLKG-FENHYPHQLSGGMRQRAALART 179
Cdd:PRK11308   89 LLRQKIQIvfqnpygslnPRKKVGQILEEPLLINTSlSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARA 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 180 LAVEPDVLLMDEPFSALD----AQT---KMVLQQDLaqmlaseGKTALMITHDLA--EAIAlsDRVFVM 239
Cdd:PRK11308  169 LMLDPDVVVADEPVSALDvsvqAQVlnlMMDLQQEL-------GLSYVFISHDLSvvEHIA--DEVMVM 228
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
33-253 2.00e-32

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 119.80  E-value: 2.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-RGPSQQVAF 111
Cdd:COG4604     2 IEIKNVSKRY------GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVaTTPSRELAK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLqkdllmpwrSI--QKNVeLGMQI--------------RGRSKAE-RAEVAKAlLARCHLKGFENHYPHQLSGGMRQRA 174
Cdd:COG4604    76 RL---------AIlrQENH-INSRLtvrelvafgrfpysKGRLTAEdREIIDEA-IAYLDLEDLADRYLDELSGGQRQRA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 175 ALARTLAVEPDVLLMDEPFSALD---AQTKMVLQQDLAQMLaseGKTALMITHDLAEAIALSDRVFVMseRPGTIIEEIT 251
Cdd:COG4604   145 FIAMVLAQDTDYVLLDEPLNNLDmkhSVQMMKLLRRLADEL---GKTVVIVLHDINFASCYADHIVAM--KDGRVVAQGT 219

                  ..
gi 1737829014 252 VD 253
Cdd:COG4604   220 PE 221
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
33-252 2.01e-32

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: 120.30  E-value: 2.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNR---QGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GPSQ 107
Cdd:TIGR02769   3 LEVRDVTHTYRTGglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqlDRKQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFmlQKDLLM----------PWRSIQKNVELGMQ-IRGRSKAERAEVAKALLARCHLKG-FENHYPHQLSGGMRQRAA 175
Cdd:TIGR02769  83 RRAF--RRDVQLvfqdspsavnPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRIN 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 176 LARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITV 252
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK--GQIVEECDV 235
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
49-249 2.30e-32

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: 118.69  E-value: 2.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQ-----VAFMLQKDLLMPWR 122
Cdd:cd03224    11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlPPHEraragIGYVPEGRRIFPEL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 SIQKNVELGMQIRGRSKAERA-EVAKALLARchLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALdaQTK 201
Cdd:cd03224    91 TVEENLLLGAYARRRAKRKARlERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL--APK 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1737829014 202 MVLQ-QDLAQMLASEGKTALMITHDLAEAIALSDRVFVMsERpGTIIEE 249
Cdd:cd03224   167 IVEEiFEAIRELRDEGVTILLVEQNARFALEIADRAYVL-ER-GRVVLE 213
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
47-240 2.77e-32

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 119.73  E-value: 2.77e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  47 GKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-----RGPSQQVAFMLQKDLLMPW 121
Cdd:PRK11231   11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsmlssRQLARRLALLPQHHLTPEG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 RSIQKNVELG----MQIRGR-SKAERAEVAKAlLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSAL 196
Cdd:PRK11231   91 ITVRELVAYGrspwLSLWGRlSAEDNARVNQA-MEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1737829014 197 DAQTKMVLqQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMS 240
Cdd:PRK11231  170 DINHQVEL-MRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLA 212
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
59-242 3.34e-32

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: 118.41  E-value: 3.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  59 IGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFMLQK-----DLLMPWRSIQKNVELGM- 132
Cdd:TIGR03771   1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQRhefawDFPISVAHTVMSGRTGHi 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 133 -QIRGRSKAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLqQDLAQM 211
Cdd:TIGR03771  81 gWLRRPCVADFAAVRDAL-RRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL-TELFIE 158
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1737829014 212 LASEGKTALMITHDLAEAIALSDRVFVMSER 242
Cdd:TIGR03771 159 LAGAGTAILMTTHDLAQAMATCDRVVLLNGR 189
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
33-249 3.41e-32

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: 118.87  E-value: 3.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTrrFKNRQGKgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQvafM 112
Cdd:cd03253     1 IEFENVT--FAYDPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLD---S 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLM-PWRSIQKNVELGMQIR-GRSKAERAEV-AKALLARCH--LKGFENHYPHQ-------LSGGMRQRAALARTL 180
Cdd:cd03253    73 LRRAIGVvPQDTVLFNDTIGYNIRyGRPDATDEEViEAAKAAQIHdkIMRFPDGYDTIvgerglkLSGGEKQRVAIARAI 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 181 AVEPDVLLMDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAEaIALSDRVFVMSErpGTIIEE 249
Cdd:cd03253   153 LKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLST-IVNADKIIVLKD--GRIVER 216
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
33-253 5.12e-32

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 118.41  E-value: 5.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV---------- 102
Cdd:cd03218     1 LRAENLSKRYGKRK------VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItklpmhkrar 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 103 RG----PSQQVAFmlqKDLlmpwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALAR 178
Cdd:cd03218    75 LGigylPQEASIF---RKL-----TVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIAR 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 179 TLAVEPDVLLMDEPFSALDAQTKMVLQQdLAQMLASEGkTALMIT-HDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:cd03218   147 ALATNPKFLLLDEPFAGVDPIAVQDIQK-IIKILKDRG-IGVLITdHNVRETLSITDRAYIIYE--GKVLAEGTPE 218
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
46-225 7.41e-32

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 117.96  E-value: 7.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  46 QGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG---------PSQQVAFMLQKD 116
Cdd:PRK10584   18 QGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeearaklRAKHVGFVFQSF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 117 LLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSAL 196
Cdd:PRK10584   98 MLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
                         170       180
                  ....*....|....*....|....*....
gi 1737829014 197 DAQTKMVLQQDLAQMLASEGKTALMITHD 225
Cdd:PRK10584  178 DRQTGDKIADLLFSLNREHGTTLILVTHD 206
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
53-289 1.02e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 118.64  E-value: 1.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR-------GPSQQVAFMLQK---DLLMPwr 122
Cdd:PRK13639   17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkksllEVRKTVGIVFQNpddQLFAP-- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 SIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD---AQ 199
Cdd:PRK13639   95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgAS 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 200 TKMVLQQDLAQmlasEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVDLPHRDnpIERRKQAGMN-EYVAHLME 278
Cdd:PRK13639  175 QIMKLLYDLNK----EGITIIISTHDVDLVPVYADKVYVMSD--GKIIKEGTPKEVFSD--IETIRKANLRlPRVAHLIE 246
                         250
                  ....*....|.
gi 1737829014 279 LLKvgRDDHLG 289
Cdd:PRK13639  247 ILN--KEDNLP 255
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
52-269 1.84e-30

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 115.17  E-value: 1.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG--PSQQVAFmlQKDLLM---------- 119
Cdd:PRK10419   26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnRAQRKAF--RRDIQMvfqdsisavn 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 120 PWRSIQKNVELGMQ-IRGRSKAERAEVAKALLARCHLK-GFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD 197
Cdd:PRK10419  104 PRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 198 aqtkMVLQQDLAQMLAS---EGKTA-LMITHDLAEAIALSDRVFVMSErpGTIIEEITV-DLPHRDNPIERRKQAGM 269
Cdd:PRK10419  184 ----LVLQAGVIRLLKKlqqQFGTAcLFITHDLRLVERFCQRVMVMDN--GQIVETQPVgDKLTFSSPAGRVLQNAV 254
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
36-249 1.98e-30

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 114.36  E-value: 1.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  36 RGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV----------RGp 105
Cdd:COG1137     7 ENLVKSYGKR------TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkrarLG- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 106 sqqVAFMLQ-----KDLlmpwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTL 180
Cdd:COG1137    80 ---IGYLPQeasifRKL-----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 181 AVEPDVLLMDEPF------SALDAQtKMVLQqdlaqmLASEGkTALMIT-HDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:COG1137   152 ATNPKFILLDEPFagvdpiAVADIQ-KIIRH------LKERG-IGVLITdHNVRETLGICDRAYIISE--GKVLAE 217
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
44-241 2.61e-30

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: 113.12  E-value: 2.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  44 NRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-RGPSQQVAFMLQKD----LL 118
Cdd:cd03226     6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkAKERRKSIGYVMQDvdyqLF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 119 MpwrsiqKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:cd03226    86 T------DSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1737829014 199 QtKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:cd03226   160 K-NMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLAN 201
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
45-249 6.84e-30

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: 117.86  E-value: 6.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  45 RQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKS----TLLNMGAGLYAPSEGQVTLAGKP-----------VRGpsQQV 109
Cdd:COG4172    17 GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDllglserelrrIRG--NRI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDL--LMPWRSIQKNVELGMQI-RGRSKAERAEVAKALLARCHLKGFE---NHYPHQLSGGMRQRAALARTLAVE 183
Cdd:COG4172    95 AMIFQEPMtsLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQRVMIAMALANE 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 184 PDVLLMDEPFSALD----AQtkmVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEE 249
Cdd:COG4172   175 PDLLIADEPTTALDvtvqAQ---ILDL-LKDLQRELGMALLLITHDLGVVRRFADRVAVM--RQGEIVEQ 238
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
18-249 1.12e-29

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 114.54  E-value: 1.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  18 DARHAQPAAAPlPFAIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTL 97
Cdd:PRK13536   28 EAKASIPGSMS-TVAIDLAGVSKSY------GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  98 AGKPV----RGPSQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQR 173
Cdd:PRK13536  101 LGVPVparaRLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRR 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 174 AALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAsEGKTALMITHDLAEAIALSDRVFVMSE-------RPGTI 246
Cdd:PRK13536  181 LTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAgrkiaegRPHAL 259

                  ...
gi 1737829014 247 IEE 249
Cdd:PRK13536  260 IDE 262
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
33-239 1.13e-29

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: 110.38  E-value: 1.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GPS---Q 107
Cdd:cd03246     1 LEVENVSFRY----PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwDPNelgD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPwRSIQKNVelgmqirgrskaeraevakallarchlkgfenhyphqLSGGMRQRAALARTLAVEPDVL 187
Cdd:cd03246    77 HVGYLPQDDELFS-GSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRIL 118
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 188 LMDEPFSALDAQTKMVLQQDLAQMLASeGKTALMITHDLaEAIALSDRVFVM 239
Cdd:cd03246   119 VLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRP-ETLASADRILVL 168
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
33-251 1.27e-29

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 117.90  E-value: 1.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQgkgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----Q 107
Cdd:TIGR00958 479 IEFQDVSFSYPNRP---DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhhylhR 555
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPwRSIQKNVELGMQirgrsKAERAEV-AKALLARCH--LKGFENHY-----PH--QLSGGMRQRAALA 177
Cdd:TIGR00958 556 QVALVGQEPVLFS-GSVRENIAYGLT-----DTPDEEImAAAKAANAHdfIMEFPNGYdtevgEKgsQLSGGQKQRIAIA 629
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 178 RTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmlasEGKTALMITHDLAeAIALSDRVFVMSErpGTIIEEIT 251
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQLLQESRSR----ASRTVLLIAHRLS-TVERADQILVLKK--GSVVEMGT 696
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
41-239 1.52e-29

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: 114.44  E-value: 1.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  41 RFKNRQGKGEMtavsDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG-------KPVRGPSQQ--VAF 111
Cdd:TIGR02142   4 RFSKRLGDFSL----DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPPEKrrIGY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKDLLMPWRSIQKNVELGM-QIRGRSKAERAEVAKALLARCHLKGfenHYPHQLSGGMRQRAALARTLAVEPDVLLMD 190
Cdd:TIGR02142  80 VFQEARLFPHLSVRGNLRYGMkRARPSERRISFERVIELLGIGHLLG---RLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1737829014 191 EPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVL 205
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
53-241 3.10e-29

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: 109.44  E-value: 3.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFML---------QKDLLMPWRS 123
Cdd:cd03215    15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedrKREGLVLDLS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELgmqirgrskaeraevakallarchlkgfenhyPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:cd03215    95 VAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1737829014 204 LQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:cd03215   143 IYR-LIRELADAGKAVLLISSELDELLGLCDRILVMYE 179
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
43-252 4.52e-29

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 110.68  E-value: 4.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  43 KNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS---------QQVAFML 113
Cdd:PRK11629   14 RYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakaelrnQKLGFIY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 114 QKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPF 193
Cdd:PRK11629   94 QFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 194 SALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVfvmSERPGTIIEEITV 252
Cdd:PRK11629  174 GNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL---EMRDGRLTAELSL 229
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
33-258 7.66e-29

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: 115.20  E-value: 7.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRqgkgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----Q 107
Cdd:TIGR02203 331 VEFRNVTFRYPGR----DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTlaslrR 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQkDLLMPWRSIQKNVELGmqirGRSKAERAEVAKALLArCHLKGFENHYP---HQ--------LSGGMRQRAAL 176
Cdd:TIGR02203 407 QVALVSQ-DVVLFNDTIANNIAYG----RTEQADRAEIERALAA-AYAQDFVDKLPlglDTpigengvlLSGGQRQRLAI 480
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 177 ARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLasEGKTALMITHDLAeAIALSDRVFVMSErpGTIIEEIT-VDLP 255
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLM--QGRTTLVIAHRLS-TIEKADRIVVMDD--GRIVERGThNELL 555

                  ...
gi 1737829014 256 HRD 258
Cdd:TIGR02203 556 ARN 558
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
33-249 8.43e-29

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: 109.88  E-value: 8.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKnrqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----Q 107
Cdd:cd03252     1 ITFEHVRFRYK----PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADpawlrR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPwRSIQKNVELGMQirGRSKAERAEVAKalLARCHL------KGFENHYPHQ---LSGGMRQRAALAR 178
Cdd:cd03252    77 QVGVVLQENVLFN-RSIRDNIALADP--GMSMERVIEAAK--LAGAHDfiselpEGYDTIVGEQgagLSGGQRQRIAIAR 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 179 TLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAseGKTALMITHDLAeAIALSDRVFVMSErpGTIIEE 249
Cdd:cd03252   152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEK--GRIVEQ 217
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
49-249 1.07e-28

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 110.44  E-value: 1.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKP---VRGPSQQVAF-------MLQKDLL 118
Cdd:PRK10619   16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlVRDKDGQLKVadknqlrLLRTRLT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 119 MPWR--------SIQKNV-ELGMQIRGRSKAERAEVAKALLARCHLKG-FENHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:PRK10619   96 MVFQhfnlwshmTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 189 MDEPFSALDAQ-TKMVLQqdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:PRK10619  176 FDEPTSALDPElVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQ--GKIEEE 233
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
39-249 1.21e-28

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: 109.16  E-value: 1.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  39 TRRFKNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFmlQKDLl 118
Cdd:cd03220    23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGGF--NPEL- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 119 mpwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFEN----HYphqlSGGMRQRAALARTLAVEPDVLLMDEPFS 194
Cdd:cd03220   100 ----TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDlpvkTY----SSGMKARLAFAIATALEPDILLIDEVLA 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 195 ALDAQTKMVLQQDLAQMLaSEGKTALMITHDLAEAIALSDRVFVMsERpGTIIEE 249
Cdd:cd03220   172 VGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVL-EK-GKIRFD 223
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
19-253 1.26e-28

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 114.67  E-value: 1.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  19 ARHAQPAAAPLPF---AIEYRGVTRRFKNRQgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQV 95
Cdd:PRK13657  318 DVRDPPGAIDLGRvkgAVEFDDVSFSYDNSR-----QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  96 TLAGKPVRGPS-----QQVAFMLQKDLLMPwRSIQKNVELgmqirGRSKAERAEVAKAL-LARCH------LKGFENHYP 163
Cdd:PRK13657  393 LIDGTDIRTVTraslrRNIAVVFQDAGLFN-RSIEDNIRV-----GRPDATDEEMRAAAeRAQAHdfierkPDGYDTVVG 466
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 164 H---QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAeAIALSDRVFVMS 240
Cdd:PRK13657  467 ErgrQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLS-TVRNADRILVFD 543
                         250
                  ....*....|...
gi 1737829014 241 ErpGTIIEEITVD 253
Cdd:PRK13657  544 N--GRVVESGSFD 554
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
32-253 1.90e-28

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 109.02  E-value: 1.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFK----------------NRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQV 95
Cdd:COG1134     4 MIEVENVSKSYRlyhepsrslkelllrrRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  96 TLAGKpvrgpsqqVAFML------QKDLlmpwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFEN----HYphq 165
Cdd:COG1134    84 EVNGR--------VSALLelgagfHPEL-----TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDqpvkTY--- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 166 lSGGMRQRAALARTLAVEPDVLLMDEPFSALDA--QTKMvlqQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErp 243
Cdd:COG1134   148 -SSGMRARLAFAVATAVDPDILLVDEVLAVGDAafQKKC---LARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEK-- 221
                         250
                  ....*....|
gi 1737829014 244 GTIIEEITVD 253
Cdd:COG1134   222 GRLVMDGDPE 231
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
33-260 2.78e-28

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 108.92  E-value: 2.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQVAF 111
Cdd:PRK11300    6 LSVSGLMMRF------GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGHQIAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 M----------LQKD-------LLMPWRSIQKNVELGM----QIRgRSKAERAEVAKALLARCHLKGFENHYPHQLSGGM 170
Cdd:PRK11300   80 MgvvrtfqhvrLFREmtvienlLVAQHQQLKTGLFSGLlktpAFR-RAESEALDRAATWLERVGLLEHANRQAGNLAYGQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 171 RQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII--- 247
Cdd:PRK11300  159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQ--GTPLang 236
                         250
                  ....*....|....*
gi 1737829014 248 --EEItvdlphRDNP 260
Cdd:PRK11300  237 tpEEI------RNNP 245
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
33-239 2.79e-28

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: 108.22  E-value: 2.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQV--- 109
Cdd:cd03266     2 ITADALTKRFRDV--KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEArrr 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 -AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:cd03266    80 lGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:cd03266   160 LDEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVL 209
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
49-241 3.10e-28

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 111.86  E-value: 3.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-----RGPSQQVAFMLQKDLLMPWRS 123
Cdd:PRK09536   14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaRAASRRVASVPQDTSLSFEFD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQI-RGR----SKAERAEVAKAlLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:PRK09536   94 VRQVVEMGRTPhRSRfdtwTETDRAAVERA-MERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1737829014 199 QtKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK09536  173 N-HQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLAD 214
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
53-239 3.29e-28

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 110.57  E-value: 3.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFMLQKDLLM----PWRSIQKNV 128
Cdd:PRK15079   36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMifqdPLASLNPRM 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 129 ELGmQIRGR---------SKAERAEVAKALLARCHL-KGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD- 197
Cdd:PRK15079  116 TIG-EIIAEplrtyhpklSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDv 194
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1737829014 198 ---AQTKMVLQQDLAQMlaseGKTALMITHDLAEAIALSDRVFVM 239
Cdd:PRK15079  195 siqAQVVNLLQQLQREM----GLSLIFIAHDLAVVKHISDRVLVM 235
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
33-247 5.40e-28

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: 106.48  E-value: 5.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLN--MGAGLYAPSEGQVTLAGKPV--RGPSQQ 108
Cdd:cd03213     4 LSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNalAGRRTGLGVSGEVLINGRPLdkRSFRKI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQIRGrskaeraevakallarchlkgfenhyphqLSGGMRQRAALARTLAVEPDVLL 188
Cdd:cd03213    84 IGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLF 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 189 MDEPFSALDAQTK---MVLQQDLAQMlaseGKTALMITHDL-AEAIALSDRVFVMSerPGTII 247
Cdd:cd03213   135 LDEPTSGLDSSSAlqvMSLLRRLADT----GRTIICSIHQPsSEIFELFDKLLLLS--QGRVI 191
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
50-249 5.95e-28

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: 105.86  E-value: 5.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  50 EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGP----SQQVAFMLQKDLLMPwRSIQ 125
Cdd:cd03247    14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLekalSSLISVLNQRPYLFD-TTLR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 126 KNVelgmqirGRskaeraevakallarchlkgfenhyphQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQ 205
Cdd:cd03247    93 NNL-------GR---------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1737829014 206 QDLAQMLasEGKTALMITHDLAeAIALSDRVFVMSErpGTIIEE 249
Cdd:cd03247   139 SLIFEVL--KDKTLIWITHHLT-GIEHMDKILFLEN--GKIIMQ 177
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
33-236 6.05e-28

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 112.90  E-value: 6.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNrqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV---------R 103
Cdd:PRK10535    5 LELKDIRRSYPS--GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldadalaQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 104 GPSQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:PRK10535   83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAiALSDRV 236
Cdd:PRK10535  163 GQVILADEPTGALDSHSGEEVMAILHQ-LRDRGHTVIIVTHDPQVA-AQAERV 213
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
37-247 8.99e-28

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: 106.97  E-value: 8.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  37 GVTRRFKNrQGKgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGL---YAPSEGQVTLAGKPV-RGPSQQ-VAF 111
Cdd:cd03234     8 DVGLKAKN-WNK-YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRkPDQFQKcVAY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKDLLMPWRSIQKNVELGMQIRGR----SKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVL 187
Cdd:cd03234    86 VRQDDILLPGLTVRETLTYTAILRLPrkssDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 188 LMDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHD-LAEAIALSDRVFVMSErpGTII 247
Cdd:cd03234   166 ILDEPTSGLDSFTALNLVSTLSQ-LARRNRIVILTIHQpRSDLFRLFDRILLLSS--GEIV 223
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
49-244 1.28e-27

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 106.34  E-value: 1.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----QQVAFMLQKDLLMPwRS 123
Cdd:PRK10247   18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeiyrQQVSYCAQTPTLFG-DT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGRSKAERAEVAKalLARCHL------KGFEnhyphQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD 197
Cdd:PRK10247   97 VYDNLIFPWQIRNQQPDPAIFLDD--LERFALpdtiltKNIA-----ELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1737829014 198 AQTKMVLQQDLAQMLASEGKTALMITHDLAEaIALSDRVFVMSERPG 244
Cdd:PRK10247  170 ESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQPHAG 215
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
33-241 1.32e-27

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: 106.36  E-value: 1.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFK--NRQGKgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTL--AGKPV---RGP 105
Cdd:COG4778     5 LEVENLSKTFTlhLQGGK-RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlaQAS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 106 SQQVAFMLQKDL--------LMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKgfEN---HYPHQLSGGMRQRA 174
Cdd:COG4778    84 PREILALRRRTIgyvsqflrVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLP--ERlwdLPPATFSGGEQQRV 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 175 ALARTLAVEPDVLLMDEPFSALDAQTKMVLqQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:COG4778   162 NIARGFIADPPLLLLDEPTASLDAANRAVV-VELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTP 227
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
33-241 2.45e-27

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: 105.63  E-value: 2.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQgkgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-----RGPSQ 107
Cdd:cd03248    12 VKFQNVTFAYPTRP---DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsqyehKYLHS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPwRSIQKNVELGMQirGRSKAERAEVAKALLARCHLKGFENHYP-------HQLSGGMRQRAALARTL 180
Cdd:cd03248    89 KVSLVGQEPVLFA-RSLQDNIAYGLQ--SCSFECVKEAAQKAHAHSFISELASGYDtevgekgSQLSGGQKQRVAIARAL 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 181 AVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLasEGKTALMITHDLaEAIALSDRVFVMSE 241
Cdd:cd03248   166 IRNPQVLILDEATSALDAESEQQVQQALYDWP--ERRTVLVIAHRL-STVERADQILVLDG 223
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
32-255 3.06e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 106.61  E-value: 3.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFKNrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVrgpSQQVAF 111
Cdd:PRK13632    7 MIKVENVSFSYPN----SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKDLLMPWR---------SIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAV 182
Cdd:PRK13632   80 EIRKKIGIIFQnpdnqfigaTVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 183 EPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIaLSDRVFVMSE----RPGT---------IIEE 249
Cdd:PRK13632  160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEgkliAQGKpkeilnnkeILEK 238

                  ....*.
gi 1737829014 250 ITVDLP 255
Cdd:PRK13632  239 AKIDSP 244
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
53-253 3.17e-27

nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131817 [Multi-domain]  Cd Length: 230  Bit Score: 105.53  E-value: 3.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAP----SEGQVTLAGKPVRGP---SQQVAFMLQ--KDLLMPWRS 123
Cdd:TIGR02770   1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLsirGRHIATIMQnpRTAFNPLFT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGR-SKAERAEVAKALLARC--HLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT 200
Cdd:TIGR02770  81 MGNHAIETLRSLGKlSKQARALILEALEAVGlpDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 201 KMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDD--GRIVERGTVK 211
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
33-239 9.94e-27

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: 103.70  E-value: 9.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQGKGEMTaVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKpvrgpsqqVAFM 112
Cdd:cd03250     1 ISVEDASFTWDSGEQETSFT-LKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------IAYV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKdllmPW---RSIQKNVELGMQIRgrskAER-AEVAKAllarCHL-KGFENhYPHQ-----------LSGGMRQRAAL 176
Cdd:cd03250    72 SQE----PWiqnGTIRENILFGKPFD----EERyEKVIKA----CALePDLEI-LPDGdlteigekginLSGGQKQRISL 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 177 ARTLAVEPDVLLMDEPFSALDAQT-KMVLQQDLAQMLAsEGKTALMITHDLaEAIALSDRVFVM 239
Cdd:cd03250   139 ARAVYSDADIYLLDDPLSAVDAHVgRHIFENCILGLLL-NNKTRILVTHQL-QLLPHADQIVVL 200
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
3-226 1.02e-26

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: 108.99  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   3 RSIQLKDANVAEAYADArHAQPAAAPLPFAIEYRGVTRRFKnrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLN 82
Cdd:TIGR02868 306 RIVEVLDAAGPVAEGSA-PAAGAVGLGKPTLELRDLSAGYP-----GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLA 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  83 MGAGLYAPSEGQVTLAGKPVRGPSQQ-----VAFMLQKDLLMPwRSIQKNVELgmqirGRSKAERAEVAKAlLARCHLKG 157
Cdd:TIGR02868 380 TLAGLLDPLQGEVTLDGVPVSSLDQDevrrrVSVCAQDAHLFD-TTVRENLRL-----ARPDATDEELWAA-LERVGLAD 452
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 158 FENHYPH-----------QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmlASEGKTALMITHDL 226
Cdd:TIGR02868 453 WLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA--ALSGRTVVLITHHL 530
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
33-247 2.27e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 105.17  E-value: 2.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFkNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVT-------LAGKPVRGP 105
Cdd:PRK13651    3 IKVKNIVKIF-NKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdekNKKKTKEKE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 106 SQQVAFMLQKDLLMPWR-----------------------SIQKNVELGMQIRGRSKAERAEVAKALLarcHLKGFENHY 162
Cdd:PRK13651   82 KVLEKLVIQKTRFKKIKkikeirrrvgvvfqfaeyqlfeqTIEKDIIFGPVSMGVSKEEAKKRAAKYI---ELVGLDESY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 163 ----PHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQ-TKMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVF 237
Cdd:PRK13651  159 lqrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEIL--EIFDNLNKQGKTIILVTHDLDNVLEWTKRTI 236
                         250
                  ....*....|
gi 1737829014 238 VMSErpGTII 247
Cdd:PRK13651  237 FFKD--GKII 244
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
32-247 2.54e-26

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: 103.63  E-value: 2.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRfknRQGKgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQ-VTLAGKPVRGPSqqva 110
Cdd:COG1119     3 LLELRNVTVR---RGGK---TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGED---- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 111 fmlqkdllmpWRSIQKNV-----ELGMQIRGRSKAERA--------------------EVAKALLARCHLKGFENHYPHQ 165
Cdd:COG1119    73 ----------VWELRKRIglvspALQLRFPRDETVLDVvlsgffdsiglyreptdeqrERARELLELLGLAHLADRPFGT 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 166 LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGT 245
Cdd:COG1119   143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL--KDGR 220

                  ..
gi 1737829014 246 II 247
Cdd:COG1119   221 VV 222
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
49-253 2.77e-26

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: 103.14  E-value: 2.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQ-----VAFMLQKDLLMPWR 122
Cdd:COG0410    14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlPPHRiarlgIGYVPEGRRIFPSL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 SIQKNVELGMQIRGRSKAERAEVAK--ALLARchLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALdaQT 200
Cdd:COG0410    94 TVEENLLLGAYARRDRAEVRADLERvyELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL--AP 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 201 KMVlqQDLAQM---LASEGKTALMITHDLAEAIALSDRVFVMsERpGTIIEEITVD 253
Cdd:COG0410   170 LIV--EEIFEIirrLNREGVTILLVEQNARFALEIADRAYVL-ER-GRIVLEGTAA 221
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
53-281 5.52e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 103.77  E-value: 5.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVrGPSQQVAFMLQKDLLMPWR---------S 123
Cdd:PRK13636   21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRESVGMVFQdpdnqlfsaS 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:PRK13636  100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 204 LQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVDLPHRDNPIERRKQAGMNEyVAHLMELLK 281
Cdd:PRK13636  180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKE--GRVILQGNPKEVFAEKEMLRKVNLRLPR-IGHLMEILK 254
cbiO PRK13650
energy-coupling factor transporter ATPase;
33-241 6.28e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 103.27  E-value: 6.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQgkgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG-----KPVRGPSQ 107
Cdd:PRK13650    5 IEVKNLTFKYKEDQ---EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteENVWDIRH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQK-DLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDV 186
Cdd:PRK13650   82 KIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 187 LLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEaIALSDRVFVMSE 241
Cdd:PRK13650  162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKN 215
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
55-225 1.15e-25

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 105.92  E-value: 1.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  55 SDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAgkpvrgPSQQVAFMLQKDLLMPWRSIQKNVELGMQI 134
Cdd:COG0488    15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------KGLRIGYLPQEPPLDDDLTVLDTVLDGDAE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 135 RGRSKAERAEVAKAL---------LARCHLK--------------------GFENHYPHQ----LSGGMRQRAALARTLA 181
Cdd:COG0488    89 LRALEAELEELEAKLaepdedlerLAELQEEfealggweaearaeeilsglGFPEEDLDRpvseLSGGWRRRVALARALL 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1737829014 182 VEPDVLLMDEPFSALDAQTKMVLQqdlaQMLASEGKTALMITHD 225
Cdd:COG0488   169 SEPDLLLLDEPTNHLDLESIEWLE----EFLKNYPGTVLVVSHD 208
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
53-241 1.16e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 102.51  E-value: 1.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ-----VAFMLQK-DLLMPWRSIQK 126
Cdd:PRK13647   20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvrskVGLVFQDpDDQVFSSTVWD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 NVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQ 206
Cdd:PRK13647  100 DVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME 179
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1737829014 207 DLAQmLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK13647  180 ILDR-LHNQGKTVIVATHDVDLAAEWADQVIVLKE 213
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
53-251 1.32e-25

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 105.49  E-value: 1.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--RGPSQQVA---FMLQKD-----LLMPwR 122
Cdd:COG1129   267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVriRSPRDAIRagiAYVPEDrkgegLVLD-L 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 SIQKNVELGMQIRGR-----SKAERAEVAKALLARCHLKGfenHYPHQ----LSGGMRQRAALARTLAVEPDVLLMDEPF 193
Cdd:COG1129   346 SIRENITLASLDRLSrggllDRRRERALAEEYIKRLRIKT---PSPEQpvgnLSGGNQQKVVLAKWLATDPKVLILDEPT 422
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 194 SALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEIT 251
Cdd:COG1129   423 RGIDVGAKAEIYRLIRE-LAAEGKAVIVISSELPELLGLSDRILVMRE--GRIVGELD 477
cbiO PRK13640
energy-coupling factor transporter ATPase;
32-255 1.93e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 102.19  E-value: 1.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFKNrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQ--------VTLAGKPVR 103
Cdd:PRK13640    5 IVEFKHVSFTYPD----SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 104 GPSQQVAFMLQK-DLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAV 182
Cdd:PRK13640   81 DIREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 183 EPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAiALSDRVFVM-------SERPGTI------IEE 249
Cdd:PRK13640  161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLddgkllaQGSPVEIfskvemLKE 239

                  ....*.
gi 1737829014 250 ITVDLP 255
Cdd:PRK13640  240 IGLDIP 245
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
31-236 4.48e-25

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 100.30  E-value: 4.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  31 FAIEyrgvTRRFKNRQGKGEMtaVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLY-----APSEGQVTLAGKPVRGP 105
Cdd:PRK14267    3 FAIE----TVNLRVYYGSNHV--IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 106 S-------QQVAFMLQKDLLMPWRSIQKNVELGMQIRG--RSKAERAEVAKALLARCHL----KGFENHYPHQLSGGMRQ 172
Cdd:PRK14267   77 DvdpievrREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQ 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 173 RAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAEAIALSDRV 236
Cdd:PRK14267  157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYV 218
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
33-247 5.70e-25

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: 99.71  E-value: 5.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQGKG---------------EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTL 97
Cdd:cd03267     1 IEVSNLSKSYRVYSKEPgligslkslfkrkyrEVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  98 AGkpVRGPSQQVAFMLQKDLLMPWRS-------IQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGM 170
Cdd:cd03267    81 AG--LVPWKRRKKFLRRIGVVFGQKTqlwwdlpVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQ 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 171 RQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII 247
Cdd:cd03267   159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK--GRLL 233
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
24-197 6.66e-25

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 104.44  E-value: 6.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  24 PAAAPLPFAIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV- 102
Cdd:NF033858  258 PADDDDEPAIEARGLTMRF------GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVd 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 103 ------RgpsQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAAL 176
Cdd:NF033858  332 agdiatR---RRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSL 408
                         170       180
                  ....*....|....*....|...
gi 1737829014 177 ArtLAV--EPDVLLMDEPFSALD 197
Cdd:NF033858  409 A--VAVihKPELLILDEPTSGVD 429
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
57-248 7.63e-25

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 103.77  E-value: 7.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  57 VSIGIKAGEFVSLIGPSGCGKSTLLNMGAGlYAPSEGQVTLAGKPVRGPS-----QQVAFMLQKDLLmPWRSIQKNVELG 131
Cdd:PRK11174  369 LNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDpeswrKHLSWVGQNPQL-PHGTLRDNVLLG 446
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 132 mqirgRSKAERAEVaKALLARCHLKGFENHYPH-----------QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT 200
Cdd:PRK11174  447 -----NPDASDEQL-QQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1737829014 201 KMVLQQDLAQmlASEGKTALMITHDLaEAIALSDRVFVMseRPGTIIE 248
Cdd:PRK11174  521 EQLVMQALNA--ASRRQTTLMVTHQL-EDLAQWDQIWVM--QDGQIVQ 563
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
33-241 1.09e-24

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: 98.42  E-value: 1.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVsLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ---- 108
Cdd:cd03264     1 LQLENLTKRYGKKR------ALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlrrr 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:cd03264    74 IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:cd03264   154 VDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNK 204
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
49-234 1.26e-24

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 99.47  E-value: 1.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLL---NMGAGLY--APSEGQVTLAGKPVRGPS-------QQVAFMLQKD 116
Cdd:PRK14243   21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIpgFRVEGKVTFHGKNLYAPDvdpvevrRRIGMVFQKP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 117 LLMPwRSIQKNVELGMQIRGrSKAERAEVAKALLARCHL----KGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:PRK14243  101 NPFP-KSIYDNIAYGARING-YKGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1737829014 193 FSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAEAIALSD 234
Cdd:PRK14243  179 CSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSD 218
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
33-266 2.63e-24

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 98.68  E-value: 2.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRfknrqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFM 112
Cdd:PRK11831    8 VDMRGVSFT------RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLMPWRS--------IQKNVELGMQIRGRSKAE--RAEVAKALLArCHLKGFENHYPHQLSGGMRQRAALARTLAV 182
Cdd:PRK11831   82 VRKRMSMLFQSgalftdmnVFDNVAYPLREHTQLPAPllHSTVMMKLEA-VGLRGAAKLMPSELSGGMARRAALARAIAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 183 EPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERpgTIIEEITVDlPHRDNPIE 262
Cdd:PRK11831  161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADK--KIVAHGSAQ-ALQANPDP 237

                  ....
gi 1737829014 263 RRKQ 266
Cdd:PRK11831  238 RVRQ 241
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
50-247 3.19e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 98.94  E-value: 3.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  50 EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTL------AG------KPVRgpsQQVAFMLQkdl 117
Cdd:PRK13634   19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGkknkklKPLR---KKVGIVFQ--- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 118 lMP-----WRSIQKNVELGMQIRGRSKAERAEVAKALLArchLKGFE----NHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:PRK13634   93 -FPehqlfEETVEKDICFGPMNFGVSEEDAKQKAREMIE---LVGLPeellARSPFELSGGQMRRVAIAGVLAMEPEVLV 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII 247
Cdd:PRK13634  169 LDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHK--GTVF 225
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
55-231 3.47e-24

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 96.80  E-value: 3.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  55 SDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRgpSQQVAFMLQ----------KDLLMPWrsi 124
Cdd:PRK13538   18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR--RQRDEYHQDllylghqpgiKTELTAL--- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 125 qKNVELGMQIRGRSKAERAEVAkalLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVL 204
Cdd:PRK13538   93 -ENLRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL 168
                         170       180
                  ....*....|....*....|....*..
gi 1737829014 205 QQDLAQMLAsEGKTALMITHDLAEAIA 231
Cdd:PRK13538  169 EALLAQHAE-QGGMVILTTHQDLPVAS 194
cbiO PRK13643
energy-coupling factor transporter ATPase;
53-250 4.03e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 98.65  E-value: 4.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ-----------VAFMLQKDLLMPw 121
Cdd:PRK13643   21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpvrkkvgVVFQFPESQLFE- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 RSIQKNVELGMQIRGRSKAERAEVAKALLARCHL-KGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT 200
Cdd:PRK13643  100 ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 201 KMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE-------RPGTIIEEI 250
Cdd:PRK13643  180 RIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKghiiscgTPSDVFQEV 235
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
23-249 1.41e-23

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: 100.28  E-value: 1.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  23 QPAAAPLPfaieYRGVTRRFKN--------RQGkgemtaVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQ 94
Cdd:COG5265   345 APDAPPLV----VGGGEVRFENvsfgydpeRPI------LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGR 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  95 VTLAGKPVRGPSQQ-------------VAFmlqkdllmpwrsiqkNVELGMQIR-GRSKAERAEVAKAllAR-CHLKGFE 159
Cdd:COG5265   415 ILIDGQDIRDVTQAslraaigivpqdtVLF---------------NDTIAYNIAyGRPDASEEEVEAA--ARaAQIHDFI 477
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 160 NHYPHQ-----------LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQmlASEGKTALMITHDLAe 228
Cdd:COG5265   478 ESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALRE--VARGRTTLVIAHRLS- 554
                         250       260
                  ....*....|....*....|.
gi 1737829014 229 AIALSDRVFVMSErpGTIIEE 249
Cdd:COG5265   555 TIVDADEILVLEA--GRIVER 573
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
33-255 1.72e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 96.74  E-value: 1.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrQGKGEMTaVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVrgpSQQVAFM 112
Cdd:PRK13648    8 IVFKNVSFQY---QSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLMPWRS---------IQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVE 183
Cdd:PRK13648   81 LRKHIGIVFQNpdnqfvgsiVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLqQDLAQMLASEGK-TALMITHDLAEAIAlSDRVFVMSE-------RPGTIIE------E 249
Cdd:PRK13648  161 PSVIILDEATSMLDPDARQNL-LDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKgtvykegTPTEIFDhaeeltR 238

                  ....*.
gi 1737829014 250 ITVDLP 255
Cdd:PRK13648  239 IGLDLP 244
cbiO PRK13642
energy-coupling factor transporter ATPase;
46-249 2.62e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 96.32  E-value: 2.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  46 QGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----QQVAFMLQK-DLLM 119
Cdd:PRK13642   15 EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrRKIGMVFQNpDNQF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 120 PWRSIQKNVELGMQIRGRSKAERAE-VAKALLArCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:PRK13642   95 VGATVEDDVAFGMENQGIPREEMIKrVDEALLA-VNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 199 QTKMVLQQDLAQMLASEGKTALMITHDLAEAiALSDRVFVMseRPGTIIEE 249
Cdd:PRK13642  174 TGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVM--KAGEIIKE 221
cbiO PRK13644
energy-coupling factor transporter ATPase;
53-248 3.08e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 96.21  E-value: 3.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ------VAFMLQK-DLLMPWRSIQ 125
Cdd:PRK13644   17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLqgirklVGIVFQNpETQFVGRTVE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 126 KNVELGMQ------IRGRSKAERAevakalLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQ 199
Cdd:PRK13644   97 EDLAFGPEnlclppIEIRKRVDRA------LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1737829014 200 T-KMVLQQdlAQMLASEGKTALMITHDLaEAIALSDRVFVMsERPGTIIE 248
Cdd:PRK13644  171 SgIAVLER--IKKLHEKGKTIVYITHNL-EELHDADRIIVM-DRGKIVLE 216
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
33-251 3.73e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 95.92  E-value: 3.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTL--------------- 97
Cdd:PRK13633    5 IKCKNVSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgldtsdeenlwdir 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  98 --AGKPVRGPSQQ-VAFMLQKDllmpwrsiqknVELGMQIRGRSKAE-RAEVAKALlARCHLKGFENHYPHQLSGGMRQR 173
Cdd:PRK13633   85 nkAGMVFQNPDNQiVATIVEED-----------VAFGPENLGIPPEEiRERVDESL-KKVGMYEYRRHAPHLLSGGQKQR 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 174 AALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIAlSDRVFVMSErpGTIIEEIT 251
Cdd:PRK13633  153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDS--GKVVMEGT 227
cbiO PRK13649
energy-coupling factor transporter ATPase;
50-250 4.18e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 95.58  E-value: 4.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  50 EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS---------QQVAFMLQ-KDLLM 119
Cdd:PRK13649   19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikqirKKVGLVFQfPESQL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 120 PWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHL-KGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:PRK13649   99 FEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 199 QTKMVLqQDLAQMLASEGKTALMITHDLAEAIALSDRVFVM-------SERPGTIIEEI 250
Cdd:PRK13649  179 KGRKEL-MTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLekgklvlSGKPKDIFQDV 236
cbiO PRK13637
energy-coupling factor transporter ATPase;
50-247 4.46e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 95.88  E-value: 4.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  50 EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFMLQK-DLLMPW------- 121
Cdd:PRK13637   19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKvGLVFQYpeyqlfe 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 RSIQKNVELGMQIRGRSKAERAEVAKALLARCHLK--GFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQ 199
Cdd:PRK13637   99 ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1737829014 200 TKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTII 247
Cdd:PRK13637  179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNK--GKCE 224
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
36-248 5.18e-23

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 94.99  E-value: 5.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  36 RGVTRRFKNRQGkgemtaVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKpvRGPSQQVAFMLQK 115
Cdd:PRK11701   10 RGLTKLYGPRKG------CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR--DGQLRDLYALSEA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 116 DLLMPWRS----IQKNVELGMqiRGRSKAErAEVAKALLArchlKGfENHY------------------------PHQLS 167
Cdd:PRK11701   82 ERRRLLRTewgfVHQHPRDGL--RMQVSAG-GNIGERLMA----VG-ARHYgdiratagdwlerveidaariddlPTTFS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 168 GGMRQRAALARTLAVEPDVLLMDEPFSALD--AQTKMVlqqDLAQMLASE-GKTALMITHDLAEAIALSDRVFVMseRPG 244
Cdd:PRK11701  154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsVQARLL---DLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVM--KQG 228

                  ....
gi 1737829014 245 TIIE 248
Cdd:PRK11701  229 RVVE 232
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
54-248 5.64e-23

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: 98.48  E-value: 5.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAF----MLQKDLLMPWRSIQKNVE 129
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLAnsvaMVDQDIFLFEGTVRDNLT 574
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 130 L---GMQIRGRSKAER-AEVAKALLARChlKGFENHYPH---QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKM 202
Cdd:TIGR03796 575 LwdpTIPDADLVRACKdAAIHDVITSRP--GGYDAELAEggaNLSGGQRQRLEIARALVRNPSILILDEATSALDPETEK 652
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1737829014 203 VLQQDLAQmlasEGKTALMITHDLAeAIALSDRVFVMsERpGTIIE 248
Cdd:TIGR03796 653 IIDDNLRR----RGCTCIIVAHRLS-TIRDCDEIIVL-ER-GKVVQ 691
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
49-239 1.13e-22

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 95.56  E-value: 1.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPS---EGQVTLAGKPV---------RGPSQQVAFMLQKD 116
Cdd:PRK09473   27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlnlpekelnKLRAEQISMIFQDP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 117 L--LMPWRSIQKNV-ELGMQIRGRSKAERAEVAKALL-------ARCHLKgfenHYPHQLSGGMRQRAALARTLAVEPDV 186
Cdd:PRK09473  107 MtsLNPYMRVGEQLmEVLMLHKGMSKAEAFEESVRMLdavkmpeARKRMK----MYPHEFSGGMRQRVMIAMALLCRPKL 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 187 LLMDEPFSALD----AQTkMVLQQDLAQmlasEGKTA-LMITHDLAEAIALSDRVFVM 239
Cdd:PRK09473  183 LIADEPTTALDvtvqAQI-MTLLNELKR----EFNTAiIMITHDLGVVAGICDKVLVM 235
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
47-257 1.59e-22

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 93.90  E-value: 1.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  47 GKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-RGPSQQVAF---MLQKDLLMPWR 122
Cdd:PRK10253   16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVARrigLLAQNATTPGD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 -SIQKNVELG------MQIRGRSKAERAeVAKALLArCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSA 195
Cdd:PRK10253   96 iTVQELVARGryphqpLFTRWRKEDEEA-VTKAMQA-TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 196 LDAQTKMVLQQDLAQMLASEGKTALMITHDLAEA-------IALSDRVFVMSERPGTIieeITVDLPHR 257
Cdd:PRK10253  174 LDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcryashlIALREGKIVAQGAPKEI---VTAELIER 239
cbiO PRK13646
energy-coupling factor transporter ATPase;
50-251 1.84e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 94.08  E-value: 1.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  50 EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG---------KPVRGPSQQVAFMLQ------ 114
Cdd:PRK13646   19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdKYIRPVRKRIGMVFQfpesql 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 115 -KDllmpwrSIQKNVELGMQIRGRSKAERAEVAKALLARChlkGFENHY----PHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:PRK13646   99 fED------TVEREIIFGPKNFKMNLDEVKNYAHRLLMDL---GFSRDVmsqsPFQMSGGQMRKIAIVSILAMNPDIIVL 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEIT 251
Cdd:PRK13646  170 DEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKE--GSIVSQTS 229
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
48-224 2.46e-22

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: 91.79  E-value: 2.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  48 KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV---RGPSQQ-VAFMLQKDLLMPWRS 123
Cdd:cd03231    10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdfqRDSIARgLLYLGHAPGIKTTLS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGRSKAERAevakalLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:cd03231    90 VLENLRFWHADHSDEQVEEA------LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
                         170       180
                  ....*....|....*....|.
gi 1737829014 204 LQQDLAQMLAsEGKTALMITH 224
Cdd:cd03231   164 FAEAMAGHCA-RGGMVVLTTH 183
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
44-256 2.71e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 94.15  E-value: 2.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  44 NRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG---KPVRGPSQQVAFMLQKDLLMP 120
Cdd:PRK13631   32 DEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyiGDKKNNHELITNPYSKKIKNF 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 121 WR-------------------SIQKNVELGMQIRGRSKAERAEVAKALLARCHLK-GFENHYPHQLSGGMRQRAALARTL 180
Cdd:PRK13631  112 KElrrrvsmvfqfpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGIL 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 181 AVEPDVLLMDEPFSALD--AQTKMVlqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE----RPGT--------- 245
Cdd:PRK13631  192 AIQPEILIFDEPTAGLDpkGEHEMM---QLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKgkilKTGTpyeiftdqh 268
                         250
                  ....*....|.
gi 1737829014 246 IIEEITVDLPH 256
Cdd:PRK13631  269 IINSTSIQVPR 279
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
33-254 6.73e-22

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: 94.87  E-value: 6.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQV-----------TLAGKP 101
Cdd:TIGR03269 280 IKVRNVSKRYISVD-RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmTKPGPD 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 102 VRGPSQQ-VAFMLQKDLLMPWRSIQKNVELGMQIR-----GRSKAerAEVAKALlarchlkGFE--------NHYPHQLS 167
Cdd:TIGR03269 359 GRGRAKRyIGILHQEYDLYPHRTVLDNLTEAIGLElpdelARMKA--VITLKMV-------GFDeekaeeilDKYPDELS 429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 168 GGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTII 247
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM--RDGKIV 507
                         250
                  ....*....|..
gi 1737829014 248 -----EEITVDL 254
Cdd:TIGR03269 508 kigdpEEIVEEL 519
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
49-241 6.80e-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: 95.11  E-value: 6.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR-------GPSqqVAFMLQKDLLMPw 121
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwdretfGKH--IGYLPQDVELFP- 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 RSIQKNVElgmqiRGRSKAE-RAEVAKALLARCH--LKGFENHYPHQ-------LSGGMRQRAALARTLAVEPDVLLMDE 191
Cdd:TIGR01842 406 GTVAENIA-----RFGENADpEKIIEAAKLAGVHelILRLPDGYDTVigpggatLSGGQRQRIALARALYGDPKLVVLDE 480
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1737829014 192 PFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAeAIALSDRVFVMSE 241
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKA-LKARGITVVVITHRPS-LLGCVDKILVLQD 528
cbiO PRK13641
energy-coupling factor transporter ATPase;
50-239 7.14e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 92.58  E-value: 7.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  50 EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG---------KPVRGPSQQVAFMLQ-KDLLM 119
Cdd:PRK13641   19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnKNLKKLRKKVSLVFQfPEAQL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 120 PWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLK-GFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:PRK13641   99 FENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1737829014 199 QTKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:PRK13641  179 EGRKEMMQ-LFKDYQKAGHTVILVTHNMDDVAEYADDVLVL 218
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
45-249 9.64e-22

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 94.77  E-value: 9.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  45 RQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKS-TLLNMGAGLYAPS----EGQVTLAGKP-----------VRGpsQQ 108
Cdd:PRK15134   16 RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESllhaseqtlrgVRG--NK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 VAFMLQKDL--LMPWRSIQKNV-ELGMQIRG-RSKAERAEVAKAL--LARCHLKGFENHYPHQLSGGMRQRAALARTLAV 182
Cdd:PRK15134   94 IAMIFQEPMvsLNPLHTLEKQLyEVLSLHRGmRREAARGEILNCLdrVGIRQAAKRLTDYPHQLSGGERQRVMIAMALLT 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 183 EPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEE 249
Cdd:PRK15134  174 RPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM--QNGRCVEQ 238
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
52-241 9.78e-22

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 91.11  E-value: 9.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVT----------LAGKPVRGpsqqVAFMLQKDLLMPW 121
Cdd:PRK10895   17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllpLHARARRG----IGYLPQEASIFRR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 RSIQKNVELGMQIRGR-SKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT 200
Cdd:PRK10895   93 LSVYDNLMAVLQIRDDlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1737829014 201 KMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK10895  173 VIDIKR-IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQ 212
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
32-247 1.09e-21

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 92.46  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFKNRQG--------KG-------EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVT 96
Cdd:COG4586     1 IIEVENLSKTYRVYEKepglkgalKGlfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  97 LAGK-PVRgpsQQVAF-------MLQK-----DLlmpwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYP 163
Cdd:COG4586    81 VLGYvPFK---RRKEFarrigvvFGQRsqlwwDL-----PAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 164 HQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErp 243
Cdd:COG4586   153 RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH-- 230

                  ....
gi 1737829014 244 GTII 247
Cdd:COG4586   231 GRII 234
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
61-276 1.51e-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: 90.93  E-value: 1.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAF---MLQKDLLMpwrSIQKNVelgmqirGR 137
Cdd:cd03237    22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAdyeGTVRDLLS---SITKDF-------YT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 138 SKAERAEVAKALlarchlkGFENHYPHQ---LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAS 214
Cdd:cd03237    92 HPYFKTEIAKPL-------QIEQILDREvpeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAEN 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 215 EGKTALMITHDLAEAIALSDRVFVMSERPGtiieEITVDLPhrdnPIERRkqAGMNEYVAHL 276
Cdd:cd03237   165 NEKTAFVVEHDIIMIDYLADRLIVFEGEPS----VNGVANP----PQSLR--SGMNRFLKNL 216
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
54-273 1.61e-21

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 91.25  E-value: 1.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  54 VSDVSIGIKAGEFVSLIGPSGCGKSTL---LNMGAGLyapsEGQVTLAGK-------------PVRGPSQQVAFMLQKDL 117
Cdd:PRK14258   23 LEGVSMEIYQSKVTAIIGPSGCGKSTFlkcLNRMNEL----ESEVRVEGRveffnqniyerrvNLNRLRRQVSMVHPKPN 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 118 LMPwRSIQKNVELGMQIRG-RSKAERAEVAKALLARCHLKGFENHYPHQ----LSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:PRK14258   99 LFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMDEP 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 193 FSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPGTIIEEITVDLPHR--DNPIERRKQagmn 270
Cdd:PRK14258  178 CFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEFGLTKKifNSPHDSRTR---- 253

                  ...
gi 1737829014 271 EYV 273
Cdd:PRK14258  254 EYV 256
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
42-239 2.07e-21

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 92.24  E-value: 2.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  42 FKNRQGKGEMTAVSDV-SIGIKAgefvsLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG-------KPVRGPSQQ--VAF 111
Cdd:PRK11144    6 FKQQLGDLCLTVNLTLpAQGITA-----IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLPPEKrrIGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 MLQKDLLMPWRSIQKNVELGMqirgrSKAERAEVAK--ALLARCHLKgfeNHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:PRK11144   81 VFQDARLFPHYKVRGNLRYGM-----AKSMVAQFDKivALLGIEPLL---DRYPGSLSGGEKQRVAIGRALLTAPELLLM 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 190 DEPFSALDAQTKMVLQQDLaQMLASEGKTA-LMITHDLAEAIALSDRVFVM 239
Cdd:PRK11144  153 DEPLASLDLPRKRELLPYL-ERLAREINIPiLYVSHSLDEILRLADRVVVL 202
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
48-224 2.12e-21

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


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 89.34  E-value: 2.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  48 KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV----RGPSQQVAFMLQKDLLMPWRS 123
Cdd:TIGR01189  10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqrDEPHENILYLGHLPGLKPELS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGrskAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:TIGR01189  90 ALENLHFWAAIHG---GAQRTIEDAL-AAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
                         170       180
                  ....*....|....*....|.
gi 1737829014 204 LQQDLAQMLASEGkTALMITH 224
Cdd:TIGR01189 166 LAGLLRAHLARGG-IVLLTTH 185
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
54-246 3.30e-21

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


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 93.27  E-value: 3.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR-------GPS-----QQVAfmlqkdlLMPw 121
Cdd:COG4618   348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwdreelGRHigylpQDVE-------LFD- 419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 RSIQKNVelgmqirGRSKAERAE--VAKALLARCH---LKgFENHY-------PHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:COG4618   420 GTIAENI-------ARFGDADPEkvVAAAKLAGVHemiLR-LPDGYdtrigegGARLSGGQRQRIGLARALYGDPRLVVL 491
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAeAIALSDRVFVMseRPGTI 246
Cdd:COG4618   492 DEPNSNLDDEGEAALAAAIRA-LKARGATVVVITHRPS-LLAAVDKLLVL--RDGRV 544
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
22-249 3.98e-21

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 92.85  E-value: 3.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  22 AQPAAAPLPFA------IEYRGVTRRFKNRQG-----KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTllnmgAGL--- 87
Cdd:PRK15134  259 SEPSGDPVPLPepasplLDVEQLQVAFPIRKGilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKST-----TGLall 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  88 -YAPSEGQVTLAGKPVRGPSQ----------QVAFMLQKDLLMPWRSIQKNVELGMQIRGR--SKAERAEVAKALLARCH 154
Cdd:PRK15134  334 rLINSQGEIWFDGQPLHNLNRrqllpvrhriQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPtlSAAQREQQVIAVMEEVG 413
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 155 LKGFENH-YPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDaqtKMVLQQDLA--QMLASEGKTA-LMITHDLAEAI 230
Cdd:PRK15134  414 LDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD---KTVQAQILAllKSLQQKHQLAyLFISHDLHVVR 490
                         250
                  ....*....|....*....
gi 1737829014 231 ALSDRVFVMseRPGTIIEE 249
Cdd:PRK15134  491 ALCHQVIVL--RQGEVVEQ 507
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
17-249 4.72e-21

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 90.16  E-value: 4.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  17 ADARHAQPAAAPLPFAIEYRGvtrrfknrqgkgeMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLL------NMGAGLYAP 90
Cdd:PRK14271   13 ADVDAAAPAMAAVNLTLGFAG-------------KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmNDKVSGYRY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  91 SeGQVTLAGKPVRGPS------QQVAFMLQKDLLMPwRSIQKNVELGmqIRGRSKAERAE---VAKALLARCHL----KG 157
Cdd:PRK14271   80 S-GDVLLGGRSIFNYRdvlefrRRVGMLFQRPNPFP-MSIMDNVLAG--VRAHKLVPRKEfrgVAQARLTEVGLwdavKD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 158 FENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAEAIALSDRVF 237
Cdd:PRK14271  156 RLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAA 233
                         250
                  ....*....|..
gi 1737829014 238 VMSErpGTIIEE 249
Cdd:PRK14271  234 LFFD--GRLVEE 243
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
49-248 4.98e-21

phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]


Pssm-ID: 188208 [Multi-domain]  Cd Length: 253  Bit Score: 89.50  E-value: 4.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAgkpVRGPSQQVAFML---QKDLLM--PWRS 123
Cdd:TIGR02323  14 GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYI---MRSGAELELYQLseaERRRLMrtEWGF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGMQIRGRSKAERAEVAKALLARCH----------LKGFE------NHYPHQLSGGMRQRAALARTLAVEPDVL 187
Cdd:TIGR02323  91 VHQNPRDGLRMRVSAGANIGERLMAIGARHYgnirataqdwLEEVEidptriDDLPRAFSGGMQQRLQIARNLVTRPRLV 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 188 LMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:TIGR02323 171 FMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQ--GRVVE 229
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
54-241 5.22e-21

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 89.51  E-value: 5.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLyAPSEGQVTLAGKPVRGPS-----QQVAFMLQKDL---LMP-WRSI 124
Cdd:COG4138    12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSaaelaRHRAYLSQQQSppfAMPvFQYL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 125 QknveLGMQirgrSKAERAEVAKALLARCHLKGFENHYP---HQLSGGMRQRAALARTL-----AVEPD--VLLMDEPFS 194
Cdd:COG4138    91 A----LHQP----AGASSEAVEQLLAQLAEALGLEDKLSrplTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMN 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1737829014 195 ALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:COG4138   163 SLDVAQQAALDRLLRE-LCQQGITVVMSSHDLNHTLRHADRVWLLKQ 208
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
22-248 7.17e-21

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 92.20  E-value: 7.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  22 AQPAAAPLPFAIEYRGVTRRFKNRqgkgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKP 101
Cdd:PRK11160  328 TTSTAAADQVSLTLNNVSFTYPDQ----PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP 403
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 102 VRGPS-----QQVAFMLQK-DLLMpwRSIQKNVELGmqirgrskAERA--EVAKALLARCHL-KGFENHYP--------- 163
Cdd:PRK11160  404 IADYSeaalrQAISVVSQRvHLFS--ATLRDNLLLA--------APNAsdEALIEVLQQVGLeKLLEDDKGlnawlgegg 473
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 164 HQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKmvlQQDLAQMLA-SEGKTALMITHDLAeAIALSDRVFVMSEr 242
Cdd:PRK11160  474 RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETE---RQILELLAEhAQNKTVLMITHRLT-GLEQFDRICVMDN- 548

                  ....*.
gi 1737829014 243 pGTIIE 248
Cdd:PRK11160  549 -GQIIE 553
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
49-241 7.74e-21

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 88.39  E-value: 7.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-RGPSQQVAF------MLQKD--LLM 119
Cdd:PRK10908   13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItRLKNREVPFlrrqigMIFQDhhLLM 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 120 PwRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD-A 198
Cdd:PRK10908   93 D-RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdA 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1737829014 199 QTKMVLQqdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK10908  172 LSEGILR--LFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSD 212
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
55-258 9.29e-21

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 91.51  E-value: 9.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  55 SDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--RGPSQQVA--FML-----QKDLLMPWRSIQ 125
Cdd:PRK11288  270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdiRSPRDAIRagIMLcpedrKAEGIIPVHSVA 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 126 KNVEL---------GMQIRGRSKAERAEVAKALLArchlkgFENHYPHQ----LSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:PRK11288  350 DNINIsarrhhlraGCLINNRWEAENADRFIRSLN------IKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEP 423
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 193 FSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFVMSErpgtiiEEITVDLPHRD 258
Cdd:PRK11288  424 TRGIDVGAKHEIYNVIYE-LAAQGVAVLFVSSDLPEVLGVADRIVVMRE------GRIAGELAREQ 482
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
49-248 1.78e-20

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 87.91  E-value: 1.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLN----MGAglYAPS---EGQVTLAGKPVRGPSQQVAfMLQKDLLMPW 121
Cdd:PRK14239   16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRsinrMND--LNPEvtiTGSIVYNGHNIYSPRTDTV-DLRKEIGMVF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 R-------SIQKNVELGMQIRGRSKAER--AEVAKALLA---------RCHLKGFenhyphQLSGGMRQRAALARTLAVE 183
Cdd:PRK14239   93 QqpnpfpmSIYENVVYGLRLKGIKDKQVldEAVEKSLKGasiwdevkdRLHDSAL------GLSGGQQQRVCIARVLATS 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAEAIALSDRV-FVMSerpGTIIE 248
Cdd:PRK14239  167 PKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTgFFLD---GDLIE 227
PLN03211 PLN03211
ABC transporter G-25; Provisional
50-241 4.40e-20

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 89.94  E-value: 4.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  50 EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAG-LYAPSEGQVTLA--GKPVRGPSQQVAFMLQKDLLMPWRSIQK 126
Cdd:PLN03211   80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNFTGTILAnnRKPTKQILKRTGFVTQDDILYPHLTVRE 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 N---VELGMQIRGRSKAERAEVAKAL-----LARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:PLN03211  160 TlvfCSLLRLPKSLTKQEKILVAESViselgLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1737829014 199 QTKMVLQQDLAQmLASEGKTALMITHDLAEAI-ALSDRVFVMSE 241
Cdd:PLN03211  240 TAAYRLVLTLGS-LAQKGKTIVTSMHQPSSRVyQMFDSVLVLSE 282
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
33-248 6.26e-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: 85.62  E-value: 6.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GPS---Q 107
Cdd:cd03244     3 IEFKNVSLRYRP----NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkiGLHdlrS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPwRSIQKNVELgmqirgRSKAERAEVAKALlARCHLKGFENHYPHQL-----------SGGMRQRAAL 176
Cdd:cd03244    79 RISIIPQDPVLFS-GTIRSNLDP------FGEYSDEELWQAL-ERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCL 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 177 ARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLAseGKTALMITHDLaEAIALSDRVFVMSErpGTIIE 248
Cdd:cd03244   151 ARALLRKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRL-DTIIDSDRILVLDK--GRVVE 217
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
32-234 6.55e-20

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 86.86  E-value: 6.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFKNRQgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ--V 109
Cdd:PRK15056    6 GIVVNDVTVTWRNGH-----TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKnlV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 AFMLQKDLLmPWRS---IQKNVELG----MQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAV 182
Cdd:PRK15056   81 AYVPQSEEV-DWSFpvlVEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 183 EPDVLLMDEPFSALDAQTKMVLqQDLAQMLASEGKTALMITHDLAEAIALSD 234
Cdd:PRK15056  160 QGQVILLDEPFTGVDVKTEARI-ISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
54-244 8.80e-20

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 89.10  E-value: 8.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLagkPvrgPSQQVAFMLQKdLLMPWRSiqknveLGMQ 133
Cdd:COG4178   379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---P---AGARVLFLPQR-PYLPLGT------LREA 445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 134 I---RGRSKAERAEVAKALlARCHLKGF------ENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTkmvl 204
Cdd:COG4178   446 LlypATAEAFSDAELREAL-EAVGLGHLaerldeEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN---- 520
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1737829014 205 QQDLAQMLASE--GKTALMITHDlAEAIALSDRVFVMSERPG 244
Cdd:COG4178   521 EAALYQLLREElpGTTVISVGHR-STLAAFHDRVLELTGDGS 561
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
49-224 1.18e-19

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 84.54  E-value: 1.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS--QQVAFMLQKDLLMPWRSIQK 126
Cdd:PRK13539   13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaEACHYLGHRNAMKPALTVAE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 NVELGMQIRGRSKAERAEVAKAL-LARC-HLKGfenhypHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVL 204
Cdd:PRK13539   93 NLEFWAAFLGGEELDIAAALEAVgLAPLaHLPF------GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
                         170       180
                  ....*....|....*....|
gi 1737829014 205 QQDLAQMLASEGkTALMITH 224
Cdd:PRK13539  167 AELIRAHLAQGG-IVIAATH 185
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
32-263 1.19e-19

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 88.62  E-value: 1.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTrrFKNRQGKgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQV-- 109
Cdd:PRK10790  340 RIDIDNVS--FAYRDDN---LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlr 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 110 --AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAE-VAKALLARCHLKGFENHYPHQ---LSGGMRQRAALARTLAVE 183
Cdd:PRK10790  415 qgVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALEtVQLAELARSLPDGLYTPLGEQgnnLSVGQKQLLALARVLVQT 494
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 184 PDVLLMDEPFSALDAQTKMVLQQDLAqmLASEGKTALMITHDLAeaialsdrvfvmserpgTIIEEITVDLPHRDNPIER 263
Cdd:PRK10790  495 PQILILDEATANIDSGTEQAIQQALA--AVREHTTLVVIAHRLS-----------------TIVEADTILVLHRGQAVEQ 555
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
54-241 1.37e-19

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: 88.34  E-value: 1.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLY-APSEGQVTLAGKPV--RGPSQQVAFML-------QKDLLMPWRS 123
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPVdiRNPAQAIRAGIamvpedrKRHGIVPILG 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGM--QIRGRSKAERAEVAKALLA---RCHLKGFENHYP-HQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD 197
Cdd:TIGR02633 356 VGKNITLSVlkSFCFKMRIDAAAELQIIGSaiqRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1737829014 198 AQTKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:TIGR02633 436 VGAKYEIYK-LINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGE 478
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
55-242 2.60e-19

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: 82.11  E-value: 2.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  55 SDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAgkpvrgpsqqvafmlqkdllmpwrsiqKNVELGmqi 134
Cdd:cd03221    17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------------------STVKIG--- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 135 rgrskaeraevakallarchlkgfenhYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVlqqdLAQMLAS 214
Cdd:cd03221    67 ---------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA----LEEALKE 115
                         170       180       190
                  ....*....|....*....|....*....|
gi 1737829014 215 EGKTALMITHD--LAEAIAlsDRVFVMSER 242
Cdd:cd03221   116 YPGTVILVSHDryFLDQVA--TKIIELEDG 143
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
33-248 2.82e-19

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 87.60  E-value: 2.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQG-----KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQ 107
Cdd:PRK10261  314 LQVRNLVTRFPLRSGllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP 393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLM----PWRSIQKNVELGMQIR--------GRSKAERAEVAKaLLARCHLKgfENH---YPHQLSGGMRQ 172
Cdd:PRK10261  394 GKLQALRRDIQFifqdPYASLDPRQTVGDSIMeplrvhglLPGKAAAARVAW-LLERVGLL--PEHawrYPHEFSGGQRQ 470
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 173 RAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:PRK10261  471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYL--GQIVE 544
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
33-248 2.90e-19

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 84.84  E-value: 2.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQG---KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-----RG 104
Cdd:PRK15112    5 LEVRNLSKTFRYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdySY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 105 PSQQVAFMLQ--KDLLMPWRSIQKNVELGMQIR-GRSKAERAEVAKALLARCHLK-GFENHYPHQLSGGMRQRAALARTL 180
Cdd:PRK15112   85 RSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARAL 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 181 AVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:PRK15112  165 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ--GEVVE 230
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
33-248 3.99e-19

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 87.00  E-value: 3.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrQGKgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS-----Q 107
Cdd:PRK11176  342 IEFRNVTFTY---PGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTlaslrN 417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPwRSIQKNVELGMQirgrSKAERAEVAKAllAR-CHLKGFENHYPH-----------QLSGGMRQRAA 175
Cdd:PRK11176  418 QVALVSQNVHLFN-DTIANNIAYART----EQYSREQIEEA--ARmAYAMDFINKMDNgldtvigengvLLSGGQRQRIA 490
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 176 LARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAeAIALSDRVFVMSErpGTIIE 248
Cdd:PRK11176  491 IARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEKADEILVVED--GEIVE 558
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
49-249 5.32e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 83.81  E-value: 5.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLL---NMGAGLY--APSEGQVTLAGK-----PVRGPSQQVAFMLQKDLL 118
Cdd:PRK14247   14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYpeARVSGEVYLDGQdifkmDVIELRRRVQMVFQIPNP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 119 MPWRSIQKNVELGMQIR--GRSKAERAEVAKALLARCHL----KGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:PRK14247   94 IPNLSIFENVALGLKLNrlVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 193 FSALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:PRK14247  174 TANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYK--GQIVEW 226
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
57-240 7.04e-19

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 83.44  E-value: 7.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  57 VSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYaPSEGQVTLAGKPVRGPS-----QQVAFMLQKD---LLMPwrsiqknV 128
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSaaelaRHRAYLSQQQtppFAMP-------V 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 129 ELGMQIRGRSKAERAEVAKALLARCHLKGFENHYP---HQLSGGMRQRAALART-LAVEPDV------LLMDEPFSALDA 198
Cdd:PRK03695   87 FQYLTLHQPDKTRTEAVASALNEVAEALGLDDKLGrsvNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPMNSLDV 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1737829014 199 QTKMVLQQDLAQMlASEGKTALMITHDLAEAIALSDRVFVMS 240
Cdd:PRK03695  167 AQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLK 207
cbiO PRK13645
energy-coupling factor transporter ATPase;
50-248 9.20e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 83.90  E-value: 9.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  50 EMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQvTLAG-----------KPVRGPSQQVAFMLQ-KDL 117
Cdd:PRK13645   23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGdyaipanlkkiKEVKRLRKEIGLVFQfPEY 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 118 LMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHL-KGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSAL 196
Cdd:PRK13645  102 QLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 197 DAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:PRK13645  182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHE--GKVIS 231
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1-248 9.91e-19

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 85.89  E-value: 9.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   1 MLRSIQLKDANVAEAYADARHAQPAAAPLPfAIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTL 80
Cdd:COG0488   285 ALEKLEREEPPRRDKTVEIRFPPPERLGKK-VLELEGLSKSY------GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTL 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  81 LNMGAGLYAPSEGQVTlagkpvRGPSQQVAFMLQK-DLLMPWRSIQKNVElgmqiRGRSKAERAEVAkALLARCHLKGFE 159
Cdd:COG0488   358 LKLLAGELEPDSGTVK------LGETVKIGYFDQHqEELDPDKTVLDELR-----DGAPGGTEQEVR-GYLGRFLFSGDD 425
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 160 NHYP-HQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQqdlaQMLAS-EGkTALMITHD--LAEAIAlsDR 235
Cdd:COG0488   426 AFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE----EALDDfPG-TVLLVSHDryFLDRVA--TR 498
                         250
                  ....*....|...
gi 1737829014 236 VFVMseRPGTIIE 248
Cdd:COG0488   499 ILEF--EDGGVRE 509
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
48-241 1.26e-18

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 85.48  E-value: 1.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  48 KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPS---EGQVTLAGKPVRGPSQQV--AFMLQKDLLMPWR 122
Cdd:TIGR00955  35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAisAYVQQDDLFIPTL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 SIQKNV----ELGMQiRGRSKAERAEVAKALLARCHLK-------GFENHYpHQLSGGMRQRAALARTLAVEPDVLLMDE 191
Cdd:TIGR00955 115 TVREHLmfqaHLRMP-RRVTKKEKRERVDEVLQALGLRkcantriGVPGRV-KGLSGGERKRLAFASELLTDPPLLFCDE 192
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 192 PFSALDA-QTKMVLQqdLAQMLASEGKTALMITHD-LAEAIALSDRVFVMSE 241
Cdd:TIGR00955 193 PTSGLDSfMAYSVVQ--VLKGLAQKGKTIICTIHQpSSELFELFDKIILMAE 242
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
33-253 1.28e-18

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 85.61  E-value: 1.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFM 112
Cdd:PRK09700    6 ISMAGIGKSF------GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 L------QKDLLMPWRSIQKNVELG-------MQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALART 179
Cdd:PRK09700   80 LgigiiyQELSVIDELTVLENLYIGrhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 180 LAVEPDVLLMDEPFSAL-DAQTK---MVLQQdlaqmLASEGKTALMITHDLAEAIALSDRVFVMSErpGT-----IIEEI 250
Cdd:PRK09700  160 LMLDAKVIIMDEPTSSLtNKEVDylfLIMNQ-----LRKEGTAIVYISHKLAEIRRICDRYTVMKD--GSsvcsgMVSDV 232

                  ...
gi 1737829014 251 TVD 253
Cdd:PRK09700  233 SND 235
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
53-241 2.06e-18

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 82.75  E-value: 2.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYA---PSEGQVTLAGKPV----------RGPSQQVAFMLQKDLLM 119
Cdd:PRK09984   19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSAGSHIELLGRTVqregrlardiRKSRANTGYIFQQFNLV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 120 PWRSIQKNVELGMQ---------IRGRSKAERAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMD 190
Cdd:PRK09984   99 NRLSVLENVLIGALgstpfwrtcFSWFTREQKQRALQAL-TRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 191 EPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK09984  178 EPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQ 228
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
49-236 2.15e-18

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 82.47  E-value: 2.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVtlagkpVRGPSQQVAFMLQKDLLMPwrSIQKNV 128
Cdd:PRK09544   15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLRIGYVPQKLYLDT--TLPLTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 129 ELGMQIRGRSKaeRAEVAKALlARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDL 208
Cdd:PRK09544   87 NRFLRLRPGTK--KEDILPAL-KRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLI 163
                         170       180
                  ....*....|....*....|....*...
gi 1737829014 209 AQMLASEGKTALMITHDLAEAIALSDRV 236
Cdd:PRK09544  164 DQLRRELDCAVLMVSHDLHLVMAKTDEV 191
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
56-249 2.56e-18

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: 81.03  E-value: 2.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  56 DVSIGIKAGEFVSLIGPSGCGKSTLLN--MGAGLYAPSEGQVTLAGKPVrgpsqqvafmlqKDLLMPWRSiQKNVELGMQ 133
Cdd:cd03217    18 GVNLTIKKGEVHALMGPNGSGKSTLAKtiMGHPKYEVTEGEILFKGEDI------------TDLPPEERA-RLGIFLAFQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 134 irgrSKAERAEVAKALLARCHLKGFenhyphqlSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQ-TKMVlqQDLAQML 212
Cdd:cd03217    85 ----YPPEIPGVKNADFLRYVNEGF--------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDaLRLV--AEVINKL 150
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1737829014 213 ASEGKTALMITH--DLAEAIAlSDRVFVMSErpGTIIEE 249
Cdd:cd03217   151 REEGKSVLIITHyqRLLDYIK-PDRVHVLYD--GRIVKS 186
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
45-239 4.00e-18

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 84.14  E-value: 4.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  45 RQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAFMLQK--------- 115
Cdd:PRK10261   23 MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQsaaqmrhvr 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 116 --DLLM----PWRSIQKNVELGMQI-------RGRSKAERAEVAKALLARCHL---KGFENHYPHQLSGGMRQRAALART 179
Cdd:PRK10261  103 gaDMAMifqePMTSLNPVFTVGEQIaesirlhQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMA 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 180 LAVEPDVLLMDEPFSALDA-------QTKMVLQQDLAQmlasegkTALMITHDLAEAIALSDRVFVM 239
Cdd:PRK10261  183 LSCRPAVLIADEPTTALDVtiqaqilQLIKVLQKEMSM-------GVIFITHDMGVVAEIADRVLVM 242
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
48-253 1.00e-17

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 81.00  E-value: 1.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  48 KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKP-----VRGPSQQVAFMLQK-DLLMPW 121
Cdd:PRK13652   14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPitkenIREVRKFVGLVFQNpDDQIFS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 RSIQKNVELG---MQIRGRSKAERAEVAKALLARCHLKgfeNHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:PRK13652   94 PTVEQDIAFGpinLGLDEETVAHRVSSALHMLGLEELR---DRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 199 QTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:PRK13652  171 QGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDK--GRIVAYGTVE 223
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
33-262 1.01e-17

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: 82.93  E-value: 1.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGL--YAPSEGQV--------------- 95
Cdd:TIGR03269   1 IEVKNLTKKFDGKE------VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyver 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  96 -TLAGKPV----------------------RGPSQQVAFMLQKDL-LMPWRSIQKNVELGMQIRGRSKAERAEVAKALLA 151
Cdd:TIGR03269  75 pSKVGEPCpvcggtlepeevdfwnlsdklrRRIRKRIAIMLQRTFaLYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 152 RCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITH------D 225
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpevieD 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1737829014 226 LAE-AIALSDRVFVMSERPGTIIEEI--TVDLPHRDNPIE 262
Cdd:TIGR03269 235 LSDkAIWLENGEIKEEGTPDEVVAVFmeGVSEVEKECEVE 274
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
54-241 1.85e-17

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 81.90  E-value: 1.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLY-APSEGQVTLAGKPV--RGPSQQVAF---ML----QKDLLMPWRS 123
Cdd:PRK13549  278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYpGRWEGEIFIDGKPVkiRNPQQAIAQgiaMVpedrKRDGIVPVMG 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGM--QIRGRS---KAERAEVAKALLARCHLKGFENHYP-HQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD 197
Cdd:PRK13549  358 VGKNITLAAldRFTGGSridDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1737829014 198 AQTKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK13549  438 VGAKYEIYK-LINQLVQQGVAIIVISSELPEVLGLSDRVLVMHE 480
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
54-248 2.07e-17

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 79.74  E-value: 2.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAP----SEGQVTLAGKPVRG---PSQQVAFMLQ--KDLLMPWRSI 124
Cdd:PRK10418   19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPcalRGRKIATIMQnpRSAFNPLHTM 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 125 QKNVELGMQIRGRSKAERAevakaLLARCHLKGFENH------YPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDA 198
Cdd:PRK10418   99 HTHARETCLALGKPADDAT-----LTAALEAVGLENAarvlklYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1737829014 199 QTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIE 248
Cdd:PRK10418  174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSH--GRIVE 221
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
33-239 2.72e-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: 81.41  E-value: 2.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLY--APSEGQVTLAGKPVRGPS---- 106
Cdd:TIGR02633   2 LEMKGIVKTF------GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNirdt 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 --QQVAFMLQKDLLMPWRSIQKNVELGMQI--RGRSKAERAEV--AKALLARCHLKGFENHYP-HQLSGGMRQRAALART 179
Cdd:TIGR02633  76 erAGIVIIHQELTLVPELSVAENIFLGNEItlPGGRMAYNAMYlrAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKA 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 180 LAVEPDVLLMDEPFSALDAQTKMVLqQDLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEIL-LDIIRDLKAHGVACVYISHKLNEVKAVCDTICVI 214
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
34-251 3.21e-17

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 81.37  E-value: 3.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  34 EYRGVTRRFKNRqgkgemtaVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAfmL 113
Cdd:PRK09700  267 EVRNVTSRDRKK--------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDA--V 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 114 QKDL-----------LMPWRSIQKNVELGMQIR------------GRSKAERAEVAKALLA-RCHLKgfeNHYPHQLSGG 169
Cdd:PRK09700  337 KKGMayitesrrdngFFPNFSIAQNMAISRSLKdggykgamglfhEVDEQRTAENQRELLAlKCHSV---NQNITELSGG 413
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 170 MRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEE 249
Cdd:PRK09700  414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYK-VMRQLADDGKVILMVSSELPEIITVCDRIAVFCE--GRLTQI 490

                  ..
gi 1737829014 250 IT 251
Cdd:PRK09700  491 LT 492
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
52-249 3.39e-17

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 79.45  E-value: 3.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV-----RGPSQQVAFMLQkdllmpwrsiQK 126
Cdd:PRK10575   25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswssKAFARKVAYLPQ----------QL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 NVELGMQIR-----------------GRSKAERAEVAKALLArchLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:PRK10575   95 PAAEGMTVRelvaigrypwhgalgrfGAADREKVEEAISLVG---LKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 190 DEPFSALD-AQTKMVLQqdLAQMLASE-GKTALMITHDLAEAIALSDRVFVMseRPGTIIEE 249
Cdd:PRK10575  172 DEPTSALDiAHQVDVLA--LVHRLSQErGLTVIAVLHDINMAARYCDYLVAL--RGGEMIAQ 229
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
53-241 4.54e-17

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: 81.60  E-value: 4.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR----GPSQQVAFMLQKDLLMPWRSIQKNV 128
Cdd:TIGR01257  945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtnldAVRQSLGMCPQHNILFHHLTVAEHI 1024
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  129 ELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDL 208
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1737829014  209 AQMlaSEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:TIGR01257 1105 LKY--RSGRTIIMSTHHMDEADLLGDRIAIISQ 1135
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
32-192 5.18e-17

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 80.94  E-value: 5.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGP------ 105
Cdd:NF033858    1 VARLEGVSHRY------GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADArhrrav 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 106 SQQVAFMLQ---KDlLMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAV 182
Cdd:NF033858   75 CPRIAYMPQglgKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIH 153
                         170
                  ....*....|
gi 1737829014 183 EPDVLLMDEP 192
Cdd:NF033858  154 DPDLLILDEP 163
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
2-248 6.02e-17

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: 80.61  E-value: 6.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   2 LRSIQLKDANVAEAYADArhAQPAAAPLPFAIEYRGVTRRFKNRQGkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLL 81
Cdd:COG4615   299 IEELELALAAAEPAAADA--AAPPAPADFQTLELRGVTYRYPGEDG-DEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLA 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  82 NMGAGLYAPSEGQVTLAGKPVRGPS-----QQVA-----FMLQKDLLmpwrsiqknvelgmqirGRSKAERAEVAKALLA 151
Cdd:COG4615   376 KLLTGLYRPESGEILLDGQPVTADNreayrQLFSavfsdFHLFDRLL-----------------GLDGEADPARARELLE 438
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 152 RCHLKG---FENHY--PHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHD- 225
Cdd:COG4615   439 RLELDHkvsVEDGRfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYTELLPELKARGKTVIAISHDd 518
                         250       260
                  ....*....|....*....|....*..
gi 1737829014 226 ----LAeaialsDRVFVMSErpGTIIE 248
Cdd:COG4615   519 ryfdLA------DRVLKMDY--GKLVE 537
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
69-239 6.03e-17

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 78.51  E-value: 6.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  69 LIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV----RG---PSQQVAFMLQK-DLLMPWRSIQKNVELGMQIRGRSKA 140
Cdd:PRK13638   32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskRGllaLRQQVATVFQDpEQQIFYTDIDSDIAFSLRNLGVPEA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 141 ERAEVAKALLARCHLKGFEnHYPHQ-LSGGMRQRAALARTLAVEPDVLLMDEPFSALD--AQTKMVLqqdLAQMLASEGK 217
Cdd:PRK13638  112 EITRRVDEALTLVDAQHFR-HQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpaGRTQMIA---IIRRIVAQGN 187
                         170       180
                  ....*....|....*....|..
gi 1737829014 218 TALMITHDLAEAIALSDRVFVM 239
Cdd:PRK13638  188 HVIISSHDIDLIYEISDAVYVL 209
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
51-226 6.56e-17

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: 77.76  E-value: 6.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  51 MTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQ---------VAFMLQKdllmPW 121
Cdd:cd03290    14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEatrsrnrysVAYAAQK----PW 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 122 ---RSIQKNVELGMQIRGRSkaeraevAKALLARCHLKGFENHYPH-----------QLSGGMRQRAALARTLAVEPDVL 187
Cdd:cd03290    90 llnATVEENITFGSPFNKQR-------YKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIV 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1737829014 188 LMDEPFSALDAQ-TKMVLQQDLAQMLASEGKTALMITHDL 226
Cdd:cd03290   163 FLDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKL 202
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
33-225 6.63e-17

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: 80.36  E-value: 6.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLagkpvrGPSQQVAFM 112
Cdd:TIGR03719 323 IEAENLTKAF------GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------GETVKLAYV 390
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQ-KDLLMPWRSIQKNVELG---MQIRGRSKAERAEVAkallaRCHLKGFENHYP-HQLSGGMRQRAALARTLAVEPDVL 187
Cdd:TIGR03719 391 DQsRDALDPNKTVWEEISGGldiIKLGKREIPSRAYVG-----RFNFKGSDQQKKvGQLSGGERNRVHLAKTLKSGGNVL 465
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1737829014 188 LMDEPFSALDAQTKMVLQQDLaqmLASEGkTALMITHD 225
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEAL---LNFAG-CAVVISHD 499
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
48-240 7.70e-17

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: 80.76  E-value: 7.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   48 KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQvafMLQKDllmpwrSIQKN 127
Cdd:TIGR00957  648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQA---WIQND------SLREN 718
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  128 VELGMQIRGRSKAERAEvAKALLARCHL-----------KGFenhyphQLSGGMRQRAALARTLAVEPDVLLMDEPFSAL 196
Cdd:TIGR00957  719 ILFGKALNEKYYQQVLE-ACALLPDLEIlpsgdrteigeKGV------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1737829014  197 DAQT-KMVLQQDLAQMLASEGKTALMITHDLAeAIALSDRVFVMS 240
Cdd:TIGR00957  792 DAHVgKHIFEHVIGPEGVLKNKTRILVTHGIS-YLPQVDVIIVMS 835
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
49-239 1.00e-16

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 77.61  E-value: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  49 GEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV------RGPSQQVAFMLQKDLLMPWR 122
Cdd:PRK11614   16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwqtaKIMREAVAIVPEGRRVFSRM 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 SIQKNVELGMQIRGRSK-AERAEVAKALLARCHLKGFENhyPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALdaqTK 201
Cdd:PRK11614   96 TVEENLAMGGFFAERDQfQERIKWVYELFPRLHERRIQR--AGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL---AP 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1737829014 202 MVLQQ--DLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:PRK11614  171 IIIQQifDTIEQLREQGMTIFLVEQNANQALKLADRGYVL 210
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
63-258 1.18e-16

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 79.71  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  63 AGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----QQVAFML--QKDLLMPWRSIQKNVELGMQIRG 136
Cdd:PRK15439   36 AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakaHQLGIYLvpQEPLLFPNLSVKENILFGLPKRQ 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 137 RSKAERAEVAKALlaRCHLKgfenhyPHQLSGGM----RQRAALARTLAVEPDVLLMDEPFSALD-AQTKMVLQQdlAQM 211
Cdd:PRK15439  116 ASMQKMKQLLAAL--GCQLD------LDSSAGSLevadRQIVEILRGLMRDSRILILDEPTASLTpAETERLFSR--IRE 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1737829014 212 LASEGKTALMITHDLAEAIALSDRVFVMseRPGTI-IEEITVDLPHRD 258
Cdd:PRK15439  186 LLAQGVGIVFISHKLPEIRQLADRISVM--RDGTIaLSGKTADLSTDD 231
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
34-238 1.34e-16

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 79.57  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  34 EYRGVTRRFKNRQgkgemtAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS------Q 107
Cdd:PRK11288    6 SFDGIGKTFPGVK------ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASttaalaA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QVAFMLQKDLLMPWRSIQKNVELGmQIRGRS----KAERAEVAKALLARCHLKgFENHYP-HQLSGGMRQRAALARTLAV 182
Cdd:PRK11288   80 GVAIIYQELHLVPEMTVAENLYLG-QLPHKGgivnRRLLNYEAREQLEHLGVD-IDPDTPlKYLSIGQRQMVEIAKALAR 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 183 EPDVLLMDEPFSALDAQTKMVLQQDLAQmLASEGKTALMITHDLAEAIALSDRVFV 238
Cdd:PRK11288  158 NARVIAFDEPTSSLSAREIEQLFRVIRE-LRAEGRVILYVSHRMEEIFALCDAITV 212
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
53-263 1.34e-16

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 79.28  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR--GP--SQQ--VAFMLQKDLLMPWRSIQK 126
Cdd:PRK10762   19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPksSQEagIGIIHQELNLIPQLTIAE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 NVELGMQIRGRS-----KAERAEvAKALLARCHLKgfenHYPHQLSG----GMRQRAALARTLAVEPDVLLMDEPFSAL- 196
Cdd:PRK10762   99 NIFLGREFVNRFgridwKKMYAE-ADKLLARLNLR----FSSDKLVGelsiGEQQMVEIAKVLSFESKVIIMDEPTDALt 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 197 DAQTKMVLQqdLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEEITVDLPHRDNPIER 263
Cdd:PRK10762  174 DTETESLFR--VIRELKSQGRGIVYISHRLKEIFEICDDVTVF--RDGQFIAEREVADLTEDSLIEM 236
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
6-248 1.75e-16

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 79.25  E-value: 1.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   6 QLKDANVAEAYADarHAQPAAAPLPFAIEYRGVTRRFKNRQgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGA 85
Cdd:PRK10522  298 KLNKLALAPYKAE--FPRPQAFPDWQTLELRNVTFAYQDNG-----FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLT 370
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  86 GLYAPSEGQVTLAGKPVrGPSQQVAFMLQkdllmpWRSIQKNVELGMQIRG-RSKAERAEVAKALLARCHLKG---FENH 161
Cdd:PRK10522  371 GLYQPQSGEILLDGKPV-TAEQPEDYRKL------FSAVFTDFHLFDQLLGpEGKPANPALVEKWLERLKMAHkleLEDG 443
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 162 Y--PHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIaLSDRVFVM 239
Cdd:PRK10522  444 RisNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFI-HADRLLEM 522

                  ....*....
gi 1737829014 240 seRPGTIIE 248
Cdd:PRK10522  523 --RNGQLSE 529
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
33-224 2.93e-16

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: 74.50  E-value: 2.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTrrFKNRQGKgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVtlaGKPVRGpsqQVAFM 112
Cdd:cd03223     1 IELENLS--LATPDGR---VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGE---DLLFL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQKDLLmpwrsiqknvelgmqIRGRSKAeraevakALLarchlkgfenhYP--HQLSGGMRQRAALARTLAVEPDVLLMD 190
Cdd:cd03223    70 PQRPYL---------------PLGTLRE-------QLI-----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLD 116
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1737829014 191 EPFSALDAQTkmvlQQDLAQMLASEGKTALMITH 224
Cdd:cd03223   117 EATSALDEES----EDRLYQLLKELGITVISVGH 146
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
31-230 3.00e-16

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 75.77  E-value: 3.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  31 FAIEYRGVTRRFknrqgkgemtaVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLY--APSEGQVTLagkpvrgpsqq 108
Cdd:COG2401    34 FGVELRVVERYV-----------LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV----------- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 109 vafmlqkdllmPWRSIQKNVELGMQI-RGRSKAEraevAKALLARChlkGFENHY-----PHQLSGGMRQRAALARTLAV 182
Cdd:COG2401    92 -----------PDNQFGREASLIDAIgRKGDFKD----AVELLNAV---GLSDAVlwlrrFKELSTGQKFRFRLALLLAE 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1737829014 183 EPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITH--DLAEAI 230
Cdd:COG2401   154 RPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHhyDVIDDL 203
cyc_pep_trnsptr TIGR01194
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ...
32-242 3.70e-16

cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]


Pssm-ID: 130262 [Multi-domain]  Cd Length: 555  Bit Score: 78.08  E-value: 3.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFKNRQGKgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV----RGPSQ 107
Cdd:TIGR01194 337 SIELKDVHMNPKAPEGS-EGFALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVsadsRDDYR 415
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 108 QV------AFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERaevakallaRCHLKGFENHYPHQLSGGMRQRAALARTLA 181
Cdd:TIGR01194 416 DLfsaifaDFHLFDDLIGPDEGEHASLDNAQQYLQRLEIAD---------KVKIEDGGFSTTTALSTGQQKRLALICAWL 486
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 182 VEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDlaeaialsDRVFVMSER 242
Cdd:TIGR01194 487 EDRPILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHD--------DQYFELADQ 539
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
56-241 4.18e-16

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: 76.43  E-value: 4.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKpvrgpsqqVAFMLQKDLLMPwRSIQKNVELGM--- 132
Cdd:cd03291    55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------ISFSSQFSWIMP-GTIKENIIFGVsyd 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 133 QIRGRSkaeraeVAKAllarCHLKGFENHYPHQ-----------LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT- 200
Cdd:cd03291   126 EYRYKS------VVKA----CQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTe 195
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1737829014 201 KMVLQQDLAQMLASegKTALMITHDLaEAIALSDRVFVMSE 241
Cdd:cd03291   196 KEIFESCVCKLMAN--KTRILVTSKM-EHLKKADKILILHE 233
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
56-241 1.98e-15

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: 76.49  E-value: 1.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKpvrgpsqqVAFMLQKDLLMPwRSIQKNVELGM--- 132
Cdd:TIGR01271  444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------ISFSPQTSWIMP-GTIKDNIIFGLsyd 514
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  133 QIRGRSkaeraeVAKAllarCHLKGFENHYPHQ-----------LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT- 200
Cdd:TIGR01271  515 EYRYTS------VIKA----CQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTe 584
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1737829014  201 KMVLQQDLAQMLASegKTALMITHDLaEAIALSDRVFVMSE 241
Cdd:TIGR01271  585 KEIFESCLCKLMSN--KTRILVTSKL-EHLKKADKILLLHE 622
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
52-253 2.12e-15

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 75.83  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSqqVAFMLQKDL-----------LMP 120
Cdd:COG3845   272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS--PRERRRLGVayipedrlgrgLVP 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 121 WRSIQKNVELGMQIRGR-------SKAERAEVAKALLARCHLKGFENHYP-HQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:COG3845   350 DMSVAENLILGRYRRPPfsrggflDRKAIRAFAEELIEEFDVRTPGPDTPaRSLSGGNQQKVILARELSRDPKLLIAAQP 429
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 193 FSALDAQ-TKMVLQQDLAqmLASEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:COG3845   430 TRGLDVGaIEFIHQRLLE--LRDAGAAVLLISEDLDEILALSDRIAVMYE--GRIVGEVPAA 487
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
30-238 2.24e-15

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 75.74  E-value: 2.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  30 PFAIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYaPS---EGQVTLAGKPVRGPS 106
Cdd:PRK13549    3 EYLLEMKNITKTF------GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 ------QQVAFMLQKDLLMPWRSIQKNVELGMQIRGRSKAERAEV---AKALLARCHLKGFENHYPHQLSGGMRQRAALA 177
Cdd:PRK13549   76 irdterAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMylrAQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737829014 178 RTLAVEPDVLLMDEPFSALDAQTKMVLqQDLAQMLASEGKTALMITHDLAEAIALSDRVFV 238
Cdd:PRK13549  156 KALNKQARLLILDEPTASLTESETAVL-LDIIRDLKAHGIACIYISHKLNEVKAISDTICV 215
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
53-249 2.43e-15

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 74.78  E-value: 2.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKS--TLLNMGAGLYAP--SEGQVTLAGKPVRGPSQQ---------VAFMLQKdllm 119
Cdd:PRK11022   22 AVDRISYSVKQGEVVGIVGESGSGKSvsSLAIMGLIDYPGrvMAEKLEFNGQDLQRISEKerrnlvgaeVAMIFQD---- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 120 PWRSIQKNVELGMQI-------RGRSKAERAEVAKALLARCHLKGFENH---YPHQLSGGMRQRAALARTLAVEPDVLLM 189
Cdd:PRK11022   98 PMTSLNPCYTVGFQImeaikvhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEE 249
Cdd:PRK11022  178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVM--YAGQVVET 235
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
61-276 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: 75.59  E-value: 2.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEG----QVTLAGKPvrgpsQQV---AFMLQKDLLMpwRSIQKNVElgmq 133
Cdd:COG1245   363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGevdeDLKISYKP-----QYIspdYDGTVEEFLR--SANTDDFG---- 431
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 134 irgrSKAERAEVAKAL-LARCHLKGFENhyphqLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQML 212
Cdd:COG1245   432 ----SSYYKTEIIKPLgLEKLLDKNVKD-----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFA 502
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 213 ASEGKTALMITHDLAEAIALSDRVFVMSERPGTiieeitvdLPHRDNPIERRKqaGMNEYVAHL 276
Cdd:COG1245   503 ENRGKTAMVVDHDIYLIDYISDRLMVFEGEPGV--------HGHASGPMDMRE--GMNRFLKEL 556
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
61-276 9.53e-15

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 74.07  E-value: 9.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQV----TLAGKPVR-GPSQQvafMLQKDLLmpwRSIQKNVelgmqir 135
Cdd:PRK13409  362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelKISYKPQYiKPDYD---GTVEDLL---RSITDDL------- 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 136 gRSKAERAEVAKALlarchlkGFENHYPHQ---LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQML 212
Cdd:PRK13409  429 -GSSYYKSEIIKPL-------QLERLLDKNvkdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIA 500
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 213 ASEGKTALMITHDLAEAIALSDRVFVMSERPGTiieeitvdLPHRDNPIERRKqaGMNEYVAHL 276
Cdd:PRK13409  501 EEREATALVVDHDIYMIDYISDRLMVFEGEPGK--------HGHASGPMDMRE--GMNRFLKEL 554
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
31-228 1.17e-14

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 73.77  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  31 FAIEYRGVTRRFK-------------NRQGKGEM-TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVT 96
Cdd:PRK13545    3 YKVKFEHVTKKYKmynkpfdklkdlfFRSKDGEYhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  97 lagkpVRGPSQQVAFM--LQKDLlmpwrSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRA 174
Cdd:PRK13545   83 -----IKGSAALIAISsgLNGQL-----TGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRL 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 175 ALARTLAVEPDVLLMDEPFSALDAQ-TKMVLqqDLAQMLASEGKTALMITHDLAE 228
Cdd:PRK13545  153 GFAISVHINPDILVIDEALSVGDQTfTKKCL--DKMNEFKEQGKTIFFISHSLSQ 205
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
53-239 2.20e-14

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 73.51  E-value: 2.20e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKP----VRGPSQQVAFMLQKDLLMPWRSIQKNV 128
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltnISDVHQNMGYCPQFDAIDDLLTGREHL 2033
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  129 ELGMQIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDL 208
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1737829014  209 AQMLaSEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:TIGR01257 2114 VSII-REGRAVVLTSHSMEECEALCTRLAIM 2143
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
33-265 2.35e-14

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 73.14  E-value: 2.35e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   33 IEYRGVTRRFKNRQgkgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQV------TLAGKPVRGPS 106
Cdd:PTZ00265   383 IQFKNVRFHYDTRK---DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshNLKDINLKWWR 459
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  107 QQVAFMLQKDLLMPwRSIQKNVEL------------------------GMQIRGRSKAERA------------------- 143
Cdd:PTZ00265   460 SKIGVVSQDPLLFS-NSIKNNIKYslyslkdlealsnyynedgndsqeNKNKRNSCRAKCAgdlndmsnttdsneliemr 538
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  144 ------------EVAKALLARCHLKGFENHY-------PHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVL 204
Cdd:PTZ00265   539 knyqtikdsevvDVSKKVLIHDFVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737829014  205 QQDLAQMLASEGKTALMITHDLAeAIALSDRVFVMS--ERPGTIIEEITVDLPHRDNPIERRK 265
Cdd:PTZ00265   619 QKTINNLKGNENRITIIIAHRLS-TIRYANTIFVLSnrERGSTVDVDIIGEDPTKDNKENNNK 680
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
42-241 2.53e-14

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


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 69.98  E-value: 2.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  42 FKNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGL---YAPSEGQVTLAGKPVRG----PSQQVAFMLQ 114
Cdd:cd03233    11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKEfaekYPGEIIYVSE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 115 KDLLMPwrsiqknvELgmqirgrskaeraEVAKALLARCHLKGfeNHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFS 194
Cdd:cd03233    91 EDVHFP--------TL-------------TVRETLDFALRCKG--NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1737829014 195 ALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAI-ALSDRVFVMSE 241
Cdd:cd03233   148 GLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIyDLFDKVLVLYE 195
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
54-241 3.31e-14

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 72.34  E-value: 3.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--RGPSQQVAFML-------QKDLLMPWRSI 124
Cdd:PRK10762  268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtRSPQDGLANGIvyisedrKRDGLVLGMSV 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 125 QKNVEL---------GMQIRGrsKAERAEVAKallarcHLKGFENHYPHQ------LSGGMRQRAALARTLAVEPDVLLM 189
Cdd:PRK10762  348 KENMSLtalryfsraGGSLKH--ADEQQAVSD------FIRLFNIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLIL 419
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1737829014 190 DEPFSALDAQTKMVLQQDLAQMLAsEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:PRK10762  420 DEPTRGVDVGAKKEIYQLINQFKA-EGLSIILVSSEMPEVLGMSDRILVMHE 470
GguA NF040905
sugar ABC transporter ATP-binding protein;
34-285 3.84e-14

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 72.13  E-value: 3.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  34 EYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYaPS---EGQVTLAGKPVR----GPS 106
Cdd:NF040905    3 EMRGITKTF------PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRfkdiRDS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 107 QQVAFML--QKDLLMPWRSIQKNVELGMQIRGRSKAERAEV---AKALLARCHLKgfENhyPHQLSG----GMRQRAALA 177
Cdd:NF040905   76 EALGIVIihQELALIPYLSIAENIFLGNERAKRGVIDWNETnrrARELLAKVGLD--ES--PDTLVTdigvGKQQLVEIA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 178 RTLAVEPDVLLMDEPFSAL-DAQTKMVLqqDLAQMLASEGKTALMITHDLAEAIALSDRVFVMseRPGTIIEeiTVDLpH 256
Cdd:NF040905  152 KALSKDVKLLILDEPTAALnEEDSAALL--DLLLELKAQGITSIIISHKLNEIRRVADSITVL--RDGRTIE--TLDC-R 224
                         250       260
                  ....*....|....*....|....*....
gi 1737829014 257 RDNPIERRKQAGMneyvahlmellkVGRD 285
Cdd:NF040905  225 ADEVTEDRIIRGM------------VGRD 241
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
56-225 7.18e-14

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 71.50  E-value: 7.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAgkpvrgPSQQVAFMLQKDLLMPWRSIQKNVELGMQ-I 134
Cdd:TIGR03719  23 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ------PGIKVGYLPQEPQLDPTKTVRENVEEGVAeI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 135 RGRSK--------------------AERAEV-------------------AKALlaRChlkgfenhyP------HQLSGG 169
Cdd:TIGR03719  97 KDALDrfneisakyaepdadfdklaAEQAELqeiidaadawdldsqleiaMDAL--RC---------PpwdadvTKLSGG 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 170 MRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMlasEGkTALMITHD 225
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY---PG-TVVAVTHD 217
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
62-244 1.12e-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: 69.32  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  62 KAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTlaGKP--------VRGPSQQVAF--MLQKDLlmpwRSIQK--NVE 129
Cdd:cd03236    24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD--DPPdwdeildeFRGSELQNYFtkLLEGDV----KVIVKpqYVD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 130 L-GMQIRGR-----SKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:cd03236    98 LiPKAVKGKvgellKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1737829014 204 LQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPG 244
Cdd:cd03236   178 AAR-LIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYGEPG 217
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
48-239 1.28e-13

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 69.93  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  48 KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLN--MGAglyAPSEGQVT-----LAGKPVRG--PSQQVAFMlQKDLL 118
Cdd:COG4170    17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaiCGI---TKDNWHVTadrfrWNGIDLLKlsPRERRKII-GREIA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 119 M----PWRSIQKNVELGMQI---------RG---RSKAERAEVAKALLarcHLKGFENH------YPHQLSGGMRQRAAL 176
Cdd:COG4170    93 MifqePSSCLDPSAKIGDQLieaipswtfKGkwwQRFKWRKKRAIELL---HRVGIKDHkdimnsYPHELTEGECQKVMI 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737829014 177 ARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:COG4170   170 AMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
54-236 1.62e-13

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 68.92  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVR-----------GPSQQVAFMLQKDLLMPWR 122
Cdd:PRK14246   26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqidaiKLRKEVGMVFQQPNPFPHL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 SIQKNVELGMQIRG-RSKAERAEVAKALLARCHL----KGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALD 197
Cdd:PRK14246  106 SIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1737829014 198 aqtkMVLQQDLAQMLASEGK--TALMITHDLAEAIALSDRV 236
Cdd:PRK14246  186 ----IVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYV 222
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
52-248 5.41e-13

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 68.97  E-value: 5.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV--------RGpsqQVAFMLQKDLLMPwRS 123
Cdd:PRK10789  329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtklqldswRS---RLAVVSQTPFLFS-DT 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 124 IQKNVELGmqirgRSKAERAEVAK-ALLARCH------LKGFENHYPHQ---LSGGMRQRAALARTLAVEPDVLLMDEPF 193
Cdd:PRK10789  405 VANNIALG-----RPDATQQEIEHvARLASVHddilrlPQGYDTEVGERgvmLSGGQKQRISIARALLLNAEILILDDAL 479
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 194 SALDAQTKMVLQQDLAQMlaSEGKTALMITHDLAeAIALSDRVFVMSErpGTIIE 248
Cdd:PRK10789  480 SAVDGRTEHQILHNLRQW--GEGRTVIISAHRLS-ALTEASEILVMQH--GHIAQ 529
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
61-244 6.01e-13

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: 65.67  E-value: 6.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVafmlqkdllmpwrsiqknvelgmqirgrska 140
Cdd:cd03222    22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 141 eraevakallarchlkgfenhyphQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTAL 220
Cdd:cd03222    71 ------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTAL 126
                         170       180
                  ....*....|....*....|....
gi 1737829014 221 MITHDLAEAIALSDRVFVMSERPG 244
Cdd:cd03222   127 VVEHDLAVLDYLSDRIHVFEGEPG 150
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
56-239 6.09e-13

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: 66.11  E-value: 6.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPS--EGQVTLAGKPVRGPSQ-QVAFMLQKDLLMPwrsiqknvelgm 132
Cdd:cd03232    25 NISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNFQrSTGYVEQQDVHSP------------ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 133 qirgrskaeRAEVAKALLARCHLKGfenhyphqLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLaQML 212
Cdd:cd03232    93 ---------NLTVREALRFSALLRG--------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL-KKL 154
                         170       180
                  ....*....|....*....|....*...
gi 1737829014 213 ASEGKTALMITHDLAEAI-ALSDRVFVM 239
Cdd:cd03232   155 ADSGQAILCTIHQPSASIfEKFDRLLLL 182
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
61-243 9.15e-13

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 66.03  E-value: 9.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGP--SQQVAFMLQKDLLMPWRSIQKNVELGMQIRGRS 138
Cdd:PRK13543   34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGdrSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRR 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 139 KAERAEVAKALLArchLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGkT 218
Cdd:PRK13543  114 AKQMPGSALAIVG---LAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGG-A 189
                         170       180
                  ....*....|....*....|....*
gi 1737829014 219 ALMITHDLAEAIALSDRVFVMSERP 243
Cdd:PRK13543  190 ALVTTHGAYAAPPVRTRMLTLEAAA 214
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
69-225 1.08e-12

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 67.84  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  69 LIGPSGCGKSTLLNMGAGLYAPSEGQVTLAgkpvrgPSQQVAFMLQKDLLMPWRSIQKNVELGMQ----IRGR------- 137
Cdd:PRK11819   38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPA------PGIKVGYLPQEPQLDPEKTVRENVEEGVAevkaALDRfneiyaa 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 138 -------------------------------SKAERAevAKALlaRChlkgfenhyPH------QLSGGMRQRAALARTL 180
Cdd:PRK11819  112 yaepdadfdalaaeqgelqeiidaadawdldSQLEIA--MDAL--RC---------PPwdakvtKLSGGERRRVALCRLL 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1737829014 181 AVEPDVLLMDEPFSALDAQTKMVLQQDLAQMlasEGkTALMITHD 225
Cdd:PRK11819  179 LEKPDMLLLDEPTNHLDAESVAWLEQFLHDY---PG-TVVAVTHD 219
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
33-225 1.88e-12

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 67.07  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLagkpvrGPSQQVAFM 112
Cdd:PRK11819  325 IEAENLSKSF------GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------GETVKLAYV 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 LQ-KDLLMPWRSIQKNVELG---MQIRGRSKAERAEVAkallaRCHLKGfenhyPHQ------LSGGMRQRAALARTLAV 182
Cdd:PRK11819  393 DQsRDALDPNKTVWEEISGGldiIKVGNREIPSRAYVG-----RFNFKG-----GDQqkkvgvLSGGERNRLHLAKTLKQ 462
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1737829014 183 EPDVLLMDEPFSALDAQTKMVLQQDLaqmLASEGkTALMITHD 225
Cdd:PRK11819  463 GGNVLLLDEPTNDLDVETLRALEEAL---LEFPG-CAVVISHD 501
PLN03130 PLN03130
ABC transporter C family member; Provisional
48-273 2.57e-12

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 67.07  E-value: 2.57e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   48 KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAP-SEGQVTLAGKpvrgpsqqVAFMLQkdllMPW---RS 123
Cdd:PLN03130   627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGT--------VAYVPQ----VSWifnAT 694
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  124 IQKNVELGMQIRgRSKAERAEVAKAL-----------LARCHLKGFenhyphQLSGGMRQRAALARTLAVEPDVLLMDEP 192
Cdd:PLN03130   695 VRDNILFGSPFD-PERYERAIDVTALqhdldllpggdLTEIGERGV------NISGGQKQRVSMARAVYSNSDVYIFDDP 767
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  193 FSALDAQtkmVLQQDLAQMLASE--GKTALMITHDLaEAIALSDRVFVMSErpGTIIEEITVDLPHRDNPIERR--KQAG 268
Cdd:PLN03130   768 LSALDAH---VGRQVFDKCIKDElrGKTRVLVTNQL-HFLSQVDRIILVHE--GMIKEEGTYEELSNNGPLFQKlmENAG 841

                   ....*.
gi 1737829014  269 -MNEYV 273
Cdd:PLN03130   842 kMEEYV 847
PLN03232 PLN03232
ABC transporter C family member; Provisional
48-251 4.06e-12

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 66.54  E-value: 4.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   48 KGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLagkpVRGpsqQVAFMLQkdllMPW---RSI 124
Cdd:PLN03232   627 KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV----IRG---SVAYVPQ----VSWifnATV 695
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  125 QKNVELGmqirgrSKAERAEVAKAL--LARCH-LKGFENHYPHQL-------SGGMRQRAALARTLAVEPDVLLMDEPFS 194
Cdd:PLN03232   696 RENILFG------SDFESERYWRAIdvTALQHdLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLS 769
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014  195 ALDAQtkmVLQQDLAQMLASE--GKTALMITHDLaEAIALSDRVFVMSErpGTIIEEIT 251
Cdd:PLN03232   770 ALDAH---VAHQVFDSCMKDElkGKTRVLVTNQL-HFLPLMDRIILVSE--GMIKEEGT 822
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
56-249 7.33e-12

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 63.93  E-value: 7.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  56 DVSIGIKAGEFVSLIGPSGCGKSTLLN--MGAGLYAPSEGQVTLAGK---------------------PVRGPSQQVAFM 112
Cdd:COG0396    18 GVNLTIKPGEVHAIMGPNGSGKSTLAKvlMGHPKYEVTSGSILLDGEdilelspderaragiflafqyPVEIPGVSVSNF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 113 L------QKDLLMPWRSIQKNVelgmqirgRSKAERAEVAKALLARCHLKGFenhyphqlSGGMRQRAALARTLAVEPDV 186
Cdd:COG0396    98 LrtalnaRRGEELSAREFLKLL--------KEKMKELGLDEDFLDRYVNEGF--------SGGEKKRNEILQMLLLEPKL 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 187 LLMDEPFSALDAQT-KMVlqQDLAQMLASEGKTALMITH-----DLAEAialsDRVFVMSErpGTIIEE 249
Cdd:COG0396   162 AILDETDSGLDIDAlRIV--AEGVNKLRSPDRGILIITHyqrilDYIKP----DFVHVLVD--GRIVKS 222
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
62-244 1.12e-11

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: 64.81  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  62 KAGEFVSLIGPSGCGKSTLLNMGAGLYAP------------------------------SEGQVTLAGKPvrgpsQQVaf 111
Cdd:COG1245    97 KKGKVTGILGPNGIGKSTALKILSGELKPnlgdydeepswdevlkrfrgtelqdyfkklANGEIKVAHKP-----QYV-- 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 112 mlqkDLLmPwRSIQKNV-ELGMQIRGRSKAEraEVAKALlarcHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMD 190
Cdd:COG1245   170 ----DLI-P-KVFKGTVrELLEKVDERGKLD--ELAEKL----GLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1737829014 191 EPFSALDAQTKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMSERPG 244
Cdd:COG1245   238 EPSSYLDIYQRLNVAR-LIRELAEEGKYVLVVEHDLAILDYLADYVHILYGEPG 290
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
56-248 1.26e-11

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: 62.43  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGK-----PVRGPSQQVAFMLQKDLLMPwRSIQKNVEL 130
Cdd:cd03369    26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLEDLRSSLTIIPQDPTLFS-GTIRSNLDP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 131 gmqirgRSKAERAEVAKALLARchlKGFENhyphqLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQ 210
Cdd:cd03369   105 ------FDEYSDEEIYGALRVS---EGGLN-----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE 170
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1737829014 211 MLAseGKTALMITHDLaEAIALSDRVFVMSErpGTIIE 248
Cdd:cd03369   171 EFT--NSTILTIAHRL-RTIIDYDKILVMDA--GEVKE 203
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
55-239 1.30e-11

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 64.69  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  55 SDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPS----------------QQVAFMLQKDLL 118
Cdd:PRK15439  280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStaqrlarglvylpedrQSSGLYLDAPLA 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 119 MPWRSIQKNvELGMQIRGrsKAERAEVAK---ALLARChlkgfeNHyPHQ----LSGGMRQRAALARTLAVEPDVLLMDE 191
Cdd:PRK15439  360 WNVCALTHN-RRGFWIKP--ARENAVLERyrrALNIKF------NH-AEQaartLSGGNQQKVLIAKCLEASPQLLIVDE 429
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1737829014 192 PFSALDAQTKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:PRK15439  430 PTRGVDVSARNDIYQ-LIRSIAAQNVAVLFISSDLEEIEQMADRVLVM 476
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
31-248 2.53e-11

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 64.28  E-value: 2.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   31 FAIEYRGVTRRFKNRQGKGEMtavsdvSIGIK-AGEFvSLIGPSGCGK-STLLNmgaglyapSEGQVTLAGKPV-----R 103
Cdd:PTZ00265  1228 FKNEHTNDMTNEQDYQGDEEQ------NVGMKnVNEF-SLTKEGGSGEdSTVFK--------NSGKILLDGVDIcdynlK 1292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  104 GPSQQVAFMLQKDLLMPwRSIQKNVELGMQIRGRSKAERAEVAKALLArcHLKGFENHY-----PH--QLSGGMRQRAAL 176
Cdd:PTZ00265  1293 DLRNLFSIVSQEPMLFN-MSIYENIKFGKEDATREDVKRACKFAAIDE--FIESLPNKYdtnvgPYgkSLSGGQKQRIAI 1369
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737829014  177 ARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAeAIALSDRVFVMS--ERPGTIIE 248
Cdd:PTZ00265  1370 ARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIKRSDKIVVFNnpDRTGSFVQ 1442
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
53-228 4.80e-11

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 61.76  E-value: 4.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGkpvrgpsqQVAFMLQKDLLMPWRSIQKNVELGM 132
Cdd:PRK13546   39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG--------EVSVIAISAGLSGQLTGIENIEFKM 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 133 QIRGRSKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDaQTkmVLQQDLAQM- 211
Cdd:PRK13546  111 LCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD-QT--FAQKCLDKIy 187
                         170
                  ....*....|....*...
gi 1737829014 212 -LASEGKTALMITHDLAE 228
Cdd:PRK13546  188 eFKEQNKTIFFVSHNLGQ 205
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
32-253 5.32e-11

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 62.45  E-value: 5.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFknrqgkGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLnMGAGLYAPSEGQV---------------- 95
Cdd:NF000106   13 AVEVRGLVKHF------GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRpwrf*twcanrralrr 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  96 TLAG-KPVRGPSQQvAFMLQKDLLMpwrsiqknveLGMQIRGRSKAERAEvAKALLARCHLKGFENHYPHQLSGGMRQRA 174
Cdd:NF000106   86 TIG*hRPVR*GRRE-SFSGRENLYM----------IGR*LDLSRKDARAR-ADELLERFSLTEAAGRAAAKYSGGMRRRL 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 175 ALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLaSEGKTALMITHDLAEAIALSDRVFVMSErpGTIIEEITVD 253
Cdd:NF000106  154 DLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDR--GRVIADGKVD 229
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
64-239 8.87e-11

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: 58.92  E-value: 8.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   64 GEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGkpvrgpsqqvafmlqkdllmpwrsiqknvelgmqirgrskaerA 143
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------------------------------------------G 38
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  144 EVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQD-----LAQMLASEGKT 218
Cdd:smart00382  39 EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKNLT 118
                          170       180
                   ....*....|....*....|....*.
gi 1737829014  219 ALMITHDL-----AEAIALSDRVFVM 239
Cdd:smart00382 119 VILTTNDEkdlgpALLRRRFDRRIVL 144
GguA NF040905
sugar ABC transporter ATP-binding protein;
166-251 1.72e-10

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 60.96  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 166 LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKM----VLQQdlaqmLASEGKTALMITHDLAEAIALSDRVFVMSE 241
Cdd:NF040905  405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYeiytIINE-----LAAEGKGVIVISSELPELLGMCDRIYVMNE 479
                          90
                  ....*....|
gi 1737829014 242 rpGTIIEEIT 251
Cdd:NF040905  480 --GRITGELP 487
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
52-225 2.85e-10

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 60.73  E-value: 2.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTlagkpvRGPSQQVAFMLQ-KDLLMPWRSIQKNVEL 130
Cdd:PRK11147  333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH------CGTKLEVAYFDQhRAELDPEKTVMDNLAE 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 131 GMQ---IRGRSKAeraevakallARCHLKGFENHyPHQ-------LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT 200
Cdd:PRK11147  407 GKQevmVNGRPRH----------VLGYLQDFLFH-PKRamtpvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
                         170       180
                  ....*....|....*....|....*
gi 1737829014 201 KMVLQqdlaQMLASEGKTALMITHD 225
Cdd:PRK11147  476 LELLE----ELLDSYQGTVLLVSHD 496
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
54-224 3.18e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 58.42  E-value: 3.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGP----SQQVAFMLQKDLLMPWRSIQKNVE 129
Cdd:PRK13540   17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDlctyQKQLCFVGHRSGINPYLTLRENCL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 130 LGMQIrgrskaerAEVAKALLARCHLKGFENH--YP-HQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQ 206
Cdd:PRK13540   97 YDIHF--------SPGAVGITELCRLFSLEHLidYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
                         170
                  ....*....|....*...
gi 1737829014 207 DLaQMLASEGKTALMITH 224
Cdd:PRK13540  169 KI-QEHRAKGGAVLLTSH 185
PTZ00243 PTZ00243
ABC transporter; Provisional
56-239 4.36e-10

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 60.18  E-value: 4.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVtLAGKPVRGPSQQVAFM---LQKDLLmpWRSIQKNVELGM 132
Cdd:PTZ00243   678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSIAYVPQQAWIMnatVRGNIL--FFDEEDAARLAD 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  133 QIR-GRSKAERAEVAKALLARCHLKGFenhyphQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQT-KMVLQQDLAQ 210
Cdd:PTZ00243   755 AVRvSQLEADLAQLGGGLETEIGEKGV------NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVEECFLG 828
                          170       180
                   ....*....|....*....|....*....
gi 1737829014  211 MLAseGKTALMITHDLaEAIALSDRVFVM 239
Cdd:PTZ00243   829 ALA--GKTRVLATHQV-HVVPRADYVVAL 854
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
61-244 6.50e-10

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 59.44  E-value: 6.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG------KPVRGPSQQVAF--MLQKDLlmpwRSIQKN--VEL 130
Cdd:PRK13409   96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdevlKRFRGTELQNYFkkLYNGEI----KVVHKPqyVDL 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 131 -GMQIRGR-----SKAERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV- 203
Cdd:PRK13409  172 iPKVFKGKvrellKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNv 251
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1737829014 204 --LQQDLAqmlasEGKTALMITHDLAEAIALSDRVFVMSERPG 244
Cdd:PRK13409  252 arLIRELA-----EGKYVLVVEHDLAVLDYLADNVHIAYGEPG 289
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
36-240 1.69e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 58.20  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  36 RGVTRRFKNRQGK-GEMT------------AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPV 102
Cdd:PRK10982  233 RSLTQRFPDKENKpGEVIlevrnltslrqpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 103 RGPSQQVA----FMLQKD----------LLMPWRSIQKNVE-----LGMQIRGRSKAERAEVAKALLARChlkgfENHYP 163
Cdd:PRK10982  313 NNHNANEAinhgFALVTEerrstgiyayLDIGFNSLISNIRnyknkVGLLDNSRMKSDTQWVIDSMRVKT-----PGHRT 387
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737829014 164 H--QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVMS 240
Cdd:PRK10982  388 QigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQ-LIAELAKKDKGIIIISSEMPELLGITDRILVMS 465
hmuV PRK13547
heme ABC transporter ATP-binding protein;
56-263 4.41e-09

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 55.99  E-value: 4.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPS--------EGQVTLAGKPVRG-PSQQVAfMLQKDLLMPWR---- 122
Cdd:PRK13547   19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAiDAPRLA-RLRAVLPQAAQpafa 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 123 -SIQKNVELGMQIRGRSKAERA----EVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLA---------VEPDVLL 188
Cdd:PRK13547   98 fSAREIVLLGRYPHARRAGALThrdgEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRYLL 177
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737829014 189 MDEPFSALD-AQTKMVLqqDLAQMLASEGKT-ALMITHDLAEAIALSDRVFVMSErpGTIIEEITVDLPHRDNPIER 263
Cdd:PRK13547  178 LDEPTAALDlAHQHRLL--DTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLAD--GAIVAHGAPADVLTPAHIAR 250
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
33-239 6.70e-09

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 55.96  E-value: 6.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  33 IEYRGVTRRFKNrqGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLyAPSEGQVT-------------LAG 99
Cdd:PRK15093    4 LDIRNLTIEFKT--SDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTadrmrfddidllrLSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 100 KPVR---GPSQQVAFMLQKDLLMPWRSIQKNVEL---GMQIRGRSKAE---RAEVAKALLarcHLKGFENH------YPH 164
Cdd:PRK15093   81 RERRklvGHNVSMIFQEPQSCLDPSERVGRQLMQnipGWTYKGRWWQRfgwRKRRAIELL---HRVGIKDHkdamrsFPY 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 165 QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:PRK15093  158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
8-241 1.40e-08

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 55.89  E-value: 1.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014    8 KDANVAEAYADARhAQPAAAPLPFAIEYRGVTRRFKNRQGKgEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGA-- 85
Cdd:TIGR00956   33 KNLSAYGVAADSD-YQPTFPNALLKILTRGFRKLKKFRDTK-TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsn 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   86 --GLYAPSEGQVTLAG-------KPVRGpsqQVAFMLQKDLLMPWRSIQKNVELGMQIR-------GRSKAERAE----V 145
Cdd:TIGR00956  111 tdGFHIGVEGVITYDGitpeeikKHYRG---DVVYNAETDVHFPHLTVGETLDFAARCKtpqnrpdGVSREEYAKhiadV 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  146 AKALLARCHLKGFE--NHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASEGKTALMIT 223
Cdd:TIGR00956  188 YMATYGLSHTRNTKvgNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAI 267
                          250
                   ....*....|....*....
gi 1737829014  224 HDLAE-AIALSDRVFVMSE 241
Cdd:TIGR00956  268 YQCSQdAYELFDKVIVLYE 286
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
61-200 1.52e-08

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 55.34  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVrgpsqqVAfMLQKDllmPWRSIQKNV---------ELG 131
Cdd:PRK11147   26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLI------VA-RLQQD---PPRNVEGTVydfvaegieEQA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 132 MQIRG----RSKAERAEVAKAL--LARC-----HLKG--FENHY----------PHQ----LSGGMRQRAALARTLAVEP 184
Cdd:PRK11147   96 EYLKRyhdiSHLVETDPSEKNLneLAKLqeqldHHNLwqLENRInevlaqlgldPDAalssLSGGWLRKAALGRALVSNP 175
                         170
                  ....*....|....*.
gi 1737829014 185 DVLLMDEPFSALDAQT 200
Cdd:PRK11147  176 DVLLLDEPTNHLDIET 191
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
22-239 1.66e-08

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 55.72  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   22 AQPAAAPLPFAIEYRGVTRRFKnrqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTllnMGAGLY---APSEGQVTLA 98
Cdd:TIGR00957 1274 APPSGWPPRGRVEFRNYCLRYR----EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSS---LTLGLFrinESAEGEIIID 1346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   99 GkpvrgpsQQVAFMLQKDL-----LMPWRSIQKNVELGMQIRGRSKAERAEVAKAL-LArcHLKGFENHYP----HQ--- 165
Cdd:TIGR00957 1347 G-------LNIAKIGLHDLrfkitIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALeLA--HLKTFVSALPdkldHEcae 1417
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014  166 ----LSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLasEGKTALMITHDLaEAIALSDRVFVM 239
Cdd:TIGR00957 1418 ggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQF--EDCTVLTIAHRL-NTIMDYTRVIVL 1492
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
58-222 8.93e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 52.71  E-value: 8.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  58 SIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLA-GKPVRGPSQQvafmLQKDLLMPWrsiQKN----VELGM 132
Cdd:PRK10938   23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfSHITRLSFEQ----LQKLVSDEW---QRNntdmLSPGE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 133 QIRGRSKAE--RAEVAKAllARCHLKGFENHYPH-------QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMV 203
Cdd:PRK10938   96 DDTGRTTAEiiQDEVKDP--ARCEQLAQQFGITAlldrrfkYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
                         170
                  ....*....|....*....
gi 1737829014 204 LQQDLAQmLASEGKTALMI 222
Cdd:PRK10938  174 LAELLAS-LHQSGITLVLV 191
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
46-239 1.60e-07

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 50.05  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  46 QGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNmgaglyapsegQVTLAgkpvrgpsqqvafmlqkdLLMpwRSIQ 125
Cdd:cd03227     3 VLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILD-----------AIGLA------------------LGG--AQSA 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 126 KNVELGMQIRGRSKAERAEVAKALlarchlkgfenhypHQLSGGMRQRAALARTLA---VEPDVL-LMDEPFSALDAQTk 201
Cdd:cd03227    52 TRRRSGVKAGCIVAAVSAELIFTR--------------LQLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRD- 116
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1737829014 202 mvlQQDLAQMLAS---EGKTALMITHDLaEAIALSDRVFVM 239
Cdd:cd03227   117 ---GQALAEAILEhlvKGAQVIVITHLP-ELAELADKLIHI 153
PLN03130 PLN03130
ABC transporter C family member; Provisional
21-240 2.45e-07

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 52.05  E-value: 2.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   21 HAQPAAAPLPFAIEYRGVTRRFKNrqgkgEMTAV-SDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG 99
Cdd:PLN03130  1226 NRPPPGWPSSGSIKFEDVVLRYRP-----ELPPVlHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG 1300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  100 KPVR----------------GP---SQQVAFMLQ-------KDLlmpWRSIQKnVELGMQIRGRSKAERAEVAKallarc 153
Cdd:PLN03130  1301 CDISkfglmdlrkvlgiipqAPvlfSGTVRFNLDpfnehndADL---WESLER-AHLKDVIRRNSLGLDAEVSE------ 1370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  154 hlkGFENhyphqLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASegKTALMITHDLAEAIAlS 233
Cdd:PLN03130  1371 ---AGEN-----FSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKS--CTMLIIAHRLNTIID-C 1439

                   ....*..
gi 1737829014  234 DRVFVMS 240
Cdd:PLN03130  1440 DRILVLD 1446
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
32-253 2.90e-07

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 51.43  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  32 AIEYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRG-PSQQVA 110
Cdd:PRK15064  319 ALEVENLTKGFDNG------PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGyYAQDHA 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 111 FMLQKDL-LMPWRSiqknvelgmQIRGRSKAEraEVAKALLARCHLKGFE-NHYPHQLSGGMRQRAALARTLAVEPDVLL 188
Cdd:PRK15064  393 YDFENDLtLFDWMS---------QWRQEGDDE--QAVRGTLGRLLFSQDDiKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737829014 189 MDEPFSALDAQTKMVLQQDLAQMlasEGkTALMITHdlaeaialsDRVFVMSerPGTIIEEITVD 253
Cdd:PRK15064  462 MDEPTNHMDMESIESLNMALEKY---EG-TLIFVSH---------DREFVSS--LATRIIEITPD 511
PLN03232 PLN03232
ABC transporter C family member; Provisional
13-248 7.88e-07

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 50.36  E-value: 7.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   13 AEAYADARHAQPAAA-PLPFAIEYRGVTRRFKnrqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPS 91
Cdd:PLN03232  1214 SEATAIIENNRPVSGwPSRGSIKFEDVHLRYR----PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE 1289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   92 EGQVTLAGKPVrgpsqqVAFMLqKDL-----LMPWRSIQKNVELGMQIRGRSKAERAEVAKALlARCHLKGFENHYPHQL 166
Cdd:PLN03232  1290 KGRIMIDDCDV------AKFGL-TDLrrvlsIIPQSPVLFSGTVRFNIDPFSEHNDADLWEAL-ERAHIKDVIDRNPFGL 1361
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  167 -----------SGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLASegKTALMITHDLaEAIALSDR 235
Cdd:PLN03232  1362 daevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS--CTMLVIAHRL-NTIIDCDK 1438
                          250
                   ....*....|...
gi 1737829014  236 VFVMSErpGTIIE 248
Cdd:PLN03232  1439 ILVLSS--GQVLE 1449
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
56-213 1.16e-06

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 49.91  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLyAPSEGQVTLAGKPVRGPSQQV---AF-MLQKDLLMPWRSIQKNVELG 131
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTwrkAFgVIPQKVFIFSGTFRKNLDPY 1315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  132 MQIrgrSKAERAEVAKALLARCHLKGFENHYPHQL-------SGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVL 204
Cdd:TIGR01271 1316 EQW---SDEEIWKVAEEVGLKSVIEQFPDKLDFVLvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQII 1392

                   ....*....
gi 1737829014  205 QQDLAQMLA 213
Cdd:TIGR01271 1393 RKTLKQSFS 1401
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
42-224 1.55e-06

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 47.56  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  42 FKNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG-------KPVRGpsqQVAFMLQ 114
Cdd:PRK13541    4 LHQLQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNcninniaKPYCT---YIGHNLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 115 KDLLMpwrSIQKNVELGMQIRgrskaERAEVAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFS 194
Cdd:PRK13541   81 LKLEM---TVFENLKFWSEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
                         170       180       190
                  ....*....|....*....|....*....|
gi 1737829014 195 ALDAQTKMVLqQDLAQMLASEGKTALMITH 224
Cdd:PRK13541  153 NLSKENRDLL-NNLIVMKANSGGIVLLSSH 181
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
4-227 2.03e-06

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 48.86  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   4 SIQLKDANVAEAYA-DARHAQPAAAPLpfaIEYRGVTRRFKNRqgkgemTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLN 82
Cdd:PRK10938  234 SEQLEGVQLPEPDEpSARHALPANEPR---IVLNNGVVSYNDR------PILHNLSWQVNPGEHWQIVGPNGAGKSTLLS 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  83 MGAGLYAPS-EGQVTLAGKPvRGPSQQVAFMLQK------DLLMPWR--SIQKNVEL-------GMqIRGRSKAERaEVA 146
Cdd:PRK10938  305 LITGDHPQGySNDLTLFGRR-RGSGETIWDIKKHigyvssSLHLDYRvsTSVRNVILsgffdsiGI-YQAVSDRQQ-KLA 381
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 147 KALLARCHLKGFENHYP-HQLSGGmRQRAAL-ARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMLaSEGKTALM--- 221
Cdd:PRK10938  382 QQWLDILGIDKRTADAPfHSLSWG-QQRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLI-SEGETQLLfvs 459
                         250
                  ....*....|....*
gi 1737829014 222 ---------ITHDLA 227
Cdd:PRK10938  460 hhaedapacITHRLE 474
PLN03073 PLN03073
ABC transporter F family; Provisional
165-224 2.73e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 48.32  E-value: 2.73e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 165 QLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQDLAQMlaseGKTALMITH 224
Cdd:PLN03073  344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW----PKTFIVVSH 399
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
54-202 2.98e-06

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: 48.21  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  54 VSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYapsegqvtlagkPVRG-----PSQQVAFMLQKDLLMPWRSIQKNV 128
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW------------PVYGgrltkPAKGKLFYVPQRPYMTLGTLRDQI 535
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 129 -----ELGMQIRGRSKAEraevAKALLARCHLK-------GFE--NHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFS 194
Cdd:TIGR00954 536 iypdsSEDMKRRGLSDKD----LEQILDNVQLThileregGWSavQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
                         170
                  ....*....|
gi 1737829014 195 AL--DAQTKM 202
Cdd:TIGR00954 612 AVsvDVEGYM 621
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
61-224 3.72e-06

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 48.18  E-value: 3.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   61 IKAGEFVSLIGPSGCGKSTLLNMGAGlyAPSEGQVTLAGKPVRGPSQQVAF------MLQKDLLMPWRSIQKNVELGMQI 134
Cdd:TIGR00956  786 VKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPLDSSFqrsigyVQQQDLHLPTSTVRESLRFSAYL 863
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  135 RGRSKAERAEVAKALLARCHLKGFENhYPHQLSG----GM----RQRAALARTLAVEPDVLL-MDEPFSALDAQTKMVLQ 205
Cdd:TIGR00956  864 RQPKSVSKSEKMEYVEEVIKLLEMES-YADAVVGvpgeGLnveqRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSIC 942
                          170
                   ....*....|....*....
gi 1737829014  206 QdLAQMLASEGKTALMITH 224
Cdd:TIGR00956  943 K-LMRKLADHGQAILCTIH 960
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
61-260 4.44e-06

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: 46.83  E-value: 4.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAG-----KPVRGPSQQVAFMLQKDLLMPwRSIQKNVELGMQIR 135
Cdd:cd03288    44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidiskLPLHTLRSRLSIILQDPILFS-GSIRFNLDPECKCT 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 136 GRSKAERAEVA------KAL---LARCHLKGFENhyphqLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQQ 206
Cdd:cd03288   123 DDRLWEALEIAqlknmvKSLpggLDAVVTEGGEN-----FSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQK 197
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1737829014 207 DLaqMLASEGKTALMITHdLAEAIALSDRVFVMSErpGTIIEEITVD--LPHRDNP 260
Cdd:cd03288   198 VV--MTAFADRTVVTIAH-RVSTILDADLVLVLSR--GILVECDTPEnlLAQEDGV 248
PLN03073 PLN03073
ABC transporter F family; Provisional
56-241 8.66e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 46.78  E-value: 8.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  56 DVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVtlagkpVRGPSQQVAFMLQK--DLLmpwrSIQKNVELGMq 133
Cdd:PLN03073  527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVRMAVFSQHhvDGL----DLSSNPLLYM- 595
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 134 irgrSKAERAEVAKALlaRCHLKGF--------ENHYphQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTKMVLQ 205
Cdd:PLN03073  596 ----MRCFPGVPEQKL--RAHLGSFgvtgnlalQPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALI 667
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1737829014 206 QDLAqmLASEGktALMITHDLAEAIALSDRVFVMSE 241
Cdd:PLN03073  668 QGLV--LFQGG--VLMVSHDEHLISGSVDELWVVSE 699
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
53-239 1.32e-05

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 46.26  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  53 AVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGKPVRGPSQQVAF-----MLQKDL-LMPWRSIQK 126
Cdd:PRK10982   13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALengisMVHQELnLVLQRSVMD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 NVELG-MQIRG----RSKAERAevAKALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEPDVLLMDEPFSALDAQTK 201
Cdd:PRK10982   93 NMWLGrYPTKGmfvdQDKMYRD--TKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEV 170
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1737829014 202 MVLQQdLAQMLASEGKTALMITHDLAEAIALSDRVFVM 239
Cdd:PRK10982  171 NHLFT-IIRKLKERGCGIVYISHKMEEIFQLCDEITIL 207
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
52-241 1.58e-05

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: 45.62  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  52 TAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYApSEGQVTLAG-----KPVRGPSQQVAFMLQKDLLMPwRSIQK 126
Cdd:cd03289    18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGvswnsVPLQKWRKAFGVIPQKVFIFS-GTFRK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 127 NVELGMQirgRSKAERAEVAKALlarcHLKGFENHYPHQL-----------SGGMRQRAALARTLAVEPDVLLMDEPFSA 195
Cdd:cd03289    96 NLDPYGK---WSDEEIWKVAEEV----GLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1737829014 196 LDAQTKMVLQQDLAQMLAseGKTALMITHDLaEAIALSDRVFVMSE 241
Cdd:cd03289   169 LDPITYQVIRKTLKQAFA--DCTVILSEHRI-EAMLECQRFLVIEE 211
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
61-225 4.09e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 44.78  E-value: 4.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  61 IKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGkpvrgpSQQVAFMLQKDLLMPWRSIQ---------KNVELG 131
Cdd:PRK10636   24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG------NWQLAWVNQETPALPQPALEyvidgdreyRQLEAQ 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 132 MQ-------------IRGRSKAERAEVAKALLARC-HLKGFENHYPHQ----LSGGMRQRAALARTLAVEPDVLLMDEPF 193
Cdd:PRK10636   98 LHdanerndghaiatIHGKLDAIDAWTIRSRAASLlHGLGFSNEQLERpvsdFSGGWRMRLNLAQALICRSDLLLLDEPT 177
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1737829014 194 SALDAQTKMVLQqdlaQMLASEGKTALMITHD 225
Cdd:PRK10636  178 NHLDLDAVIWLE----KWLKSYQGTLILISHD 205
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
61-197 5.19e-05

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 43.63  E-value: 5.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  61 IKAGEFVSLIGPSGCGKSTLLNMGAGL--YAPSEGQVTLAGK---------------------PVRGPSQQVAFMLQKDL 117
Cdd:PRK09580   24 VRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKdllelspedragegifmafqyPVEIPGVSNQFFLQTAL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 118 --LMPWRSIQKNVELGMQIRGRSKAERAEVAKALLARCHLKGFenhyphqlSGGMRQRAALARTLAVEPDVLLMDEPFSA 195
Cdd:PRK09580  104 naVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGF--------SGGEKKRNDILQMAVLEPELCILDESDSG 175

                  ..
gi 1737829014 196 LD 197
Cdd:PRK09580  176 LD 177
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
24-225 6.11e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 44.39  E-value: 6.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  24 PAAAPLPFAIEYRG-------VTRRFKNRQGKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVT 96
Cdd:PRK10636  291 PAHVDNPFHFSFRApeslpnpLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG 370
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  97 LAgKPVRgpsqqVAFMLQKDL--LMPWRS-IQKNVELGMQirgrskaeraEVAKALlaRCHLKGFENH------YPHQLS 167
Cdd:PRK10636  371 LA-KGIK-----LGYFAQHQLefLRADESpLQHLARLAPQ----------ELEQKL--RDYLGGFGFQgdkvteETRRFS 432
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1737829014 168 GGMRQRAALARTLAVEPDVLLMDEPFSALDaqtkMVLQQDLAQMLASEGKTALMITHD 225
Cdd:PRK10636  433 GGEKARLVLALIVWQRPNLLLLDEPTNHLD----LDMRQALTEALIDFEGALVVVSHD 486
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
69-225 7.30e-05

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 44.11  E-value: 7.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  69 LIGPSGCGKSTLLNMGAGLYAPSEGQVTLAgkpvrgPSQQVAFMLQKDLLMPWRSIQKNVELG-------MQIRGR--SK 139
Cdd:PRK15064   32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD------PNERLGKLRQDQFAFEEFTVLDTVIMGhtelwevKQERDRiyAL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 140 AERAE-----VAKALLARCHLKGF-----------------ENHYP--HQLSGGMRQRAALARTLAVEPDVLLMDEPFSA 195
Cdd:PRK15064  106 PEMSEedgmkVADLEVKFAEMDGYtaearagelllgvgipeEQHYGlmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNN 185
                         170       180       190
                  ....*....|....*....|....*....|
gi 1737829014 196 LDAQTKmvlqQDLAQMLASEGKTALMITHD 225
Cdd:PRK15064  186 LDINTI----RWLEDVLNERNSTMIIISHD 211
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
69-226 1.21e-04

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 42.30  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  69 LIGPSGCGKSTLLN-MGAGLYAPSEGQVTLAGKPVRGPSQQVAFML------------------QKDLLMPWRSIQKNVE 129
Cdd:COG0419    28 IVGPNGAGKSTILEaIRYALYGKARSRSKLRSDLINVGSEEASVELefehggkryrierrqgefAEFLEAKPSERKEALK 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 130 --LGM----QIRGRSKAERAEVAKALLARCHLKGFENHY---------PHQLSGGMRQRAALARTLAvepdvLLMDepFS 194
Cdd:COG0419   108 rlLGLeiyeELKERLKELEEALESALEELAELQKLKQEIlaqlsgldpIETLSGGERLRLALADLLS-----LILD--FG 180
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1737829014 195 ALDAQTKmvlqQDLAQMLasegKTALMITHDL 226
Cdd:COG0419   181 SLDEERL----ERLLDAL----EELAIITHVI 204
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
166-244 2.65e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 42.51  E-value: 2.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  166 LSGGMRQRAALARTLAVEPD--VLLMDEPFSALDAQTKMVLQQdLAQMLASEGKTALMITHDlAEAIALSDRVFVMSERP 243
Cdd:PRK00635   477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLIN-VIKKLRDQGNTVLLVEHD-EQMISLADRIIDIGPGA 554

                   .
gi 1737829014  244 G 244
Cdd:PRK00635   555 G 555
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
71-244 9.41e-04

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: 39.56  E-value: 9.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  71 GPSGCGKSTLLNmgAGLYApsegqvtLAGKPVRGPSQQ---VAFMLQKDLLmpwrsiqkNVELGMQIRGRS-KAER---- 142
Cdd:cd03279    35 GPTGAGKSTILD--AITYA-------LYGKTPRYGRQEnlrSVFAPGEDTA--------EVSFTFQLGGKKyRVERsrgl 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014 143 -AEVAK--ALLARCHLKGFENHYPHQLSGGMRQRAALARTLAVEP----------DVLLMDEPFSALDAQTKMVLQQDLA 209
Cdd:cd03279    98 dYDQFTriVLLPQGEFDRFLARPVSTLSGGETFLASLSLALALSEvlqnrggarlEALFIDEGFGTLDPEALEAVATALE 177
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1737829014 210 QmLASEGKTALMITH--DLAEAIALsdRVFVMSERPG 244
Cdd:cd03279   178 L-IRTENRMVGVISHveELKERIPQ--RLEVIKTPGG 211
PTZ00243 PTZ00243
ABC transporter; Provisional
24-239 1.43e-03

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 40.15  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   24 PAAAPLPF---AIEYRGVTRRFKnrqgKGEMTAVSDVSIGIKAGEFVSLIGPSGCGKSTLLNMGAGLYAPSEGQVTLAGK 100
Cdd:PTZ00243  1297 TSAAPHPVqagSLVFEGVQMRYR----EGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGR 1372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  101 PV-----RGPSQQVAfMLQKDLLMPWRSIQKNVELGMQirgrskAERAEVAKAL---------------LARCHLKGFEN 160
Cdd:PTZ00243  1373 EIgayglRELRRQFS-MIPQDPVLFDGTVRQNVDPFLE------ASSAEVWAALelvglrervasesegIDSRVLEGGSN 1445
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014  161 HyphqlSGGMRQRAALARTLAVE-PDVLLMDEPFS----ALDAQTKMVLqqdlaqMLASEGKTALMITHDLaEAIALSDR 235
Cdd:PTZ00243  1446 Y-----SVGQRQLMCMARALLKKgSGFILMDEATAnidpALDRQIQATV------MSAFSAYTVITIAHRL-HTVAQYDK 1513

                   ....
gi 1737829014  236 VFVM 239
Cdd:PTZ00243  1514 IIVM 1517
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
3-80 3.23e-03

class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276859 [Multi-domain]  Cd Length: 871  Bit Score: 38.96  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737829014   3 RSIQLKDANVAEAYADARHAQPAAAPLPFAIEYRGVTRRFKNRQGKGEM--TAVSDVSIGIKAGEFVSLIGPSGCGKSTL 80
Cdd:cd14894    38 RFTSIYDEQVVLTYADTANAETVLAPHPFAIAKQSLVRLFFDNEHTMPLpsTISSNRSMTEGRGQSLFLCGESGSGKTEL 117
 
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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